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Conserved domains on  [gi|755503902|ref|XP_011238432|]
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long-chain fatty acid transport protein 3 isoform X2 [Mus musculus]

Protein Classification

acyl-CoA synthetase family protein( domain architecture ID 102275)

acyl-CoA synthetase family protein functions in fatty acid synthesis, and may catalyze the ATP-dependent activation of fatty acids in a two-step reaction to form acyl-CoA esters; belongs to the class I adenylate-forming enzyme superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
37-480 0e+00

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd05938:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 537  Bit Score: 808.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  37 KLACARPLCPPLYAEDP---CCTASAAAVRVRScwpqlglptlVEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLL 113
Cdd:cd05938   53 KLGCPVAFLNTNIRSKSllhCFRCCGAKVLVVA----------PELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 114 SEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLG 193
Cdd:cd05938  123 DKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLG 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 194 IVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGP 273
Cdd:cd05938  203 IGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGP 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPF 353
Cdd:cd05938  283 IRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPF 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 354 LGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:cd05938  363 LGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 755503902 434 TVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:cd05938  443 TVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQ 489
 
Name Accession Description Interval E-value
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
37-480 0e+00

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 808.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  37 KLACARPLCPPLYAEDP---CCTASAAAVRVRScwpqlglptlVEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLL 113
Cdd:cd05938   53 KLGCPVAFLNTNIRSKSllhCFRCCGAKVLVVA----------PELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 114 SEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLG 193
Cdd:cd05938  123 DKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLG 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 194 IVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGP 273
Cdd:cd05938  203 IGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGP 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPF 353
Cdd:cd05938  283 IRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPF 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 354 LGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:cd05938  363 LGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 755503902 434 TVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:cd05938  443 TVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQ 489
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
76-482 6.02e-170

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 495.16  E-value: 6.02e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  76 LVEFLESLEPDLPALRAmglhLWATGPETNVA--GISNLLSEAADQVDEPvpgyLSAPQNIM--DTCLYIFTSGTTGLPK 151
Cdd:PRK08279 144 LVEAFEEARADLARPPR----LWVAGGDTLDDpeGYEDLAAAAAGAPTTN----PASRSGVTakDTAFYIYTSGTTGLPK 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 AARISHLKVLQC-QGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYI 230
Cdd:PRK08279 216 AAVMSHMRWLKAmGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYI 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 231 GELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGR-ASWLYKhi 309
Cdd:PRK08279 296 GELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRvPLWLAH-- 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 310 fPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAgAPELAKDKLLKDVFWSGDVFFNTGDLLVCDE 389
Cdd:PRK08279 374 -PYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRGPFDGYT-DPEASEKKILRDVFKKGDAWFNTGDLMRDDG 451
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 390 QGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLP 469
Cdd:PRK08279 452 FGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLP 531
                        410
                 ....*....|...
gi 755503902 470 PYARPRFLRLQVT 482
Cdd:PRK08279 532 AYAVPLFVRLVPE 544
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
137-479 3.22e-66

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 222.38  E-value: 3.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 137 TCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQF 215
Cdd:COG0318  102 TALILYTSGTTGRPKGVMLTHRNLLaNAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERV 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPlQILETYGMTEGN-VATFN- 291
Cdd:COG0318  182 LELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGV-RIVEGYGLTETSpVVTVNp 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 ---YTGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLl 368
Cdd:COG0318  261 edpGERRPGSVGRP-------LPGVEVR--------IVDEDGR--ELPPGEVGEIV--VRGPNVMKGYWNDPEATAEAF- 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 kdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALA 448
Cdd:COG0318  321 ------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVVAFVV 393
                        330       340       350
                 ....*....|....*....|....*....|.
gi 755503902 449 LRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:COG0318  394 LRPGAELDAEELRAFLRERLARYKVPRRVEF 424
AMP-binding pfam00501
AMP-binding enzyme;
56-406 7.46e-43

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 158.63  E-value: 7.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902   56 TASAAAVRVRSCWPQLGLPTLVEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPgylsaPQNIM 135
Cdd:pfam00501  81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPP-----PPDPD 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  136 DTCLYIFTSGTTGLPKAARISHL----KVLQCQGFYHLC-GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF 210
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRnlvaNVLSIKRVRPRGfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  211 SA---SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVR--LAVGSGLRPDTWERFLRRFGPlQILETYGMTEG 285
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlvLSGGAPLPPELARRFRELFGG-ALVNGYGLTET 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  286 NVATFNY------TGRQGAVGRaswlykhifPFSLIRY---DVMTGEPIRnaqghcmttsPGEPGLLVapVSQQSPFLGY 356
Cdd:pfam00501 315 TGVVTTPlpldedLRSLGSVGR---------PLPGTEVkivDDETGEPVP----------PGEPGELC--VRGPGVMKGY 373
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 755503902  357 AGAPELAkdkllKDVFWSGDvFFNTGDLLVCDEQGFLHFHDRTGDTFRWK 406
Cdd:pfam00501 374 LNDPELT-----AEAFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
112-395 1.32e-16

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 81.93  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  112 LLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIyLALPLYHMSGS 190
Cdd:TIGR01733 100 ELAALDDAPAPPPPDAPSGPD---DLAYVIYTSGSTGRPKGVVVTHRSLVNlLAWLARRYGLDPDDRV-LQFASLSFDAS 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  191 LLGIVGCLGIGATVVL------KPKFSASQFWDDcqKHRVTVFQ---YIGELCrylvnqPPSKAECDHKVRLAVGSG--L 259
Cdd:TIGR01733 176 VEEIFGALLAGATLVVppedeeRDDAALLAALIA--EHPVTVLNltpSLLALL------AAALPPALASLRLVILGGeaL 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  260 RPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWlykhifpfslirydVMTGEPIRNAQ-----GHCMT 334
Cdd:TIGR01733 248 TPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP--------------VPIGRPLANTRlyvldDDLRP 313
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902  335 TSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGD--VFFNTGDLLVCDEQGFLHF 395
Cdd:TIGR01733 314 VPVGVVGELY--IGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEF 374
 
Name Accession Description Interval E-value
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
37-480 0e+00

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 808.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  37 KLACARPLCPPLYAEDP---CCTASAAAVRVRScwpqlglptlVEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLL 113
Cdd:cd05938   53 KLGCPVAFLNTNIRSKSllhCFRCCGAKVLVVA----------PELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 114 SEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLG 193
Cdd:cd05938  123 DKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLG 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 194 IVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGP 273
Cdd:cd05938  203 IGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGP 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPF 353
Cdd:cd05938  283 IRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPF 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 354 LGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:cd05938  363 LGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 755503902 434 TVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:cd05938  443 TVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQ 489
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
134-480 3.10e-176

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 505.35  E-value: 3.10e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 134 IMDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05940   80 VVDAALYIYTSGTTGLPKAAIISHRRAWRgGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSA 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 292
Cdd:cd05940  160 SNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAGAPELAKdKLLKDVF 372
Cdd:cd05940  240 FGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAATEK-KILRDVF 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 373 WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPP 452
Cdd:cd05940  319 KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPN 398
                        330       340
                 ....*....|....*....|....*...
gi 755503902 453 QALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:cd05940  399 EEFDLSALAAHLEKNLPGYARPLFLRLQ 426
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
76-482 6.02e-170

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 495.16  E-value: 6.02e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  76 LVEFLESLEPDLPALRAmglhLWATGPETNVA--GISNLLSEAADQVDEPvpgyLSAPQNIM--DTCLYIFTSGTTGLPK 151
Cdd:PRK08279 144 LVEAFEEARADLARPPR----LWVAGGDTLDDpeGYEDLAAAAAGAPTTN----PASRSGVTakDTAFYIYTSGTTGLPK 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 AARISHLKVLQC-QGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYI 230
Cdd:PRK08279 216 AAVMSHMRWLKAmGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYI 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 231 GELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGR-ASWLYKhi 309
Cdd:PRK08279 296 GELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRvPLWLAH-- 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 310 fPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAgAPELAKDKLLKDVFWSGDVFFNTGDLLVCDE 389
Cdd:PRK08279 374 -PYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRGPFDGYT-DPEASEKKILRDVFKKGDAWFNTGDLMRDDG 451
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 390 QGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLP 469
Cdd:PRK08279 452 FGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLP 531
                        410
                 ....*....|...
gi 755503902 470 PYARPRFLRLQVT 482
Cdd:PRK08279 532 AYAVPLFVRLVPE 544
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
131-479 9.95e-144

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 423.76  E-value: 9.95e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 131 PQNIMDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:cd05939  100 DVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRiAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKK 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVAT 289
Cdd:cd05939  180 FSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSL 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSP---FLGYAGAPELAKdK 366
Cdd:cd05939  260 VNIDNHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlrrFDGYVNEGATNK-K 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAA 446
Cdd:cd05939  339 IARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAA 418
                        330       340       350
                 ....*....|....*....|....*....|...
gi 755503902 447 LAlRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05939  419 IV-DPERKVDLDRFSAVLAKSLPPYARPQFIRL 450
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
136-479 2.59e-119

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 360.98  E-value: 2.59e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd05937   88 DPAILIYTSGTTGLPKAAAISWRRTLVtSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQ 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNY-T 293
Cdd:cd05937  168 FWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnV 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 294 G--RQGAVGRASWLYKHIF--PFSLIRYDVMTGEPIR-NAQGHCMTTSPGEPGLLVA--PVSQQSPFLGYAGAPELAKDK 366
Cdd:cd05937  248 GdfGAGAIGHHGLIRRWKFenQVVLVKMDPETDDPIRdPKTGFCVRAPVGEPGEMLGrvPFKNREAFQGYLHNEDATESK 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAA 446
Cdd:cd05937  328 LVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAA 407
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 755503902 447 LALR----PPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05937  408 ITLEessaVPTEFTKSLLASLARKNLPSYAVPLFLRL 444
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
134-479 2.19e-74

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 242.97  E-value: 2.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 134 IMDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05934   80 VVDPASILYTSGTTGPPKGVVITHANLTfAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSA 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVATFN- 291
Cdd:cd05934  160 SRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGp 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 --YTGRQGAVGRASWLYKhifpfslIRydvmtgepIRNAQGHcmTTSPGEPG-LLVAPVSQQSPFLGYAGAPElAKDKLL 368
Cdd:cd05934  239 rdEPRRPGSIGRPAPGYE-------VR--------IVDDDGQ--ELPAGEPGeLVIRGLRGWGFFKGYYNMPE-ATAEAM 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 KdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHEGR-AGMAAL 447
Cdd:cd05934  301 R------NGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVA--VPDEVGEdEVKAVV 372
                        330       340       350
                 ....*....|....*....|....*....|..
gi 755503902 448 ALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05934  373 VLRPGETLDPEELFAFCEGQLAYFKVPRYIRF 404
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
137-479 3.22e-66

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 222.38  E-value: 3.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 137 TCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQF 215
Cdd:COG0318  102 TALILYTSGTTGRPKGVMLTHRNLLaNAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERV 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPlQILETYGMTEGN-VATFN- 291
Cdd:COG0318  182 LELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGV-RIVEGYGLTETSpVVTVNp 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 ---YTGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLl 368
Cdd:COG0318  261 edpGERRPGSVGRP-------LPGVEVR--------IVDEDGR--ELPPGEVGEIV--VRGPNVMKGYWNDPEATAEAF- 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 kdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALA 448
Cdd:COG0318  321 ------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVVAFVV 393
                        330       340       350
                 ....*....|....*....|....*....|.
gi 755503902 449 LRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:COG0318  394 LRPGAELDAEELRAFLRERLARYKVPRRVEF 424
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
136-478 7.00e-64

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 212.53  E-value: 7.00e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd04433    1 DPALILYTSGTTGKPKGVVLSHRNLLaAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPlQILETYGMTEGNVATFNY 292
Cdd:cd04433   80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVsgGAPLPPELLERFEEAPGI-KLVNGYGLTETGGTVATG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TG-----RQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKL 367
Cdd:cd04433  159 PPdddarKPGSVGRP-------VPGVEVR--------IVDPDGG--ELPPGEIGELV--VRGPSVMKGYWNNPEATAAVD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 368 lkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 447
Cdd:cd04433  220 -------EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVAVV 291
                        330       340       350
                 ....*....|....*....|....*....|.
gi 755503902 448 ALRPPQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd04433  292 VLRPGADLDAEELRAHVRERLAPYKVPRRVV 322
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
75-480 8.86e-52

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 185.73  E-value: 8.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  75 TLVEFLESLEPDLPALRamglHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAAR 154
Cdd:PRK06155 127 ALLAALEAADPGDLPLP----AVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPG---DTAAILYTSGTTGPSKGVC 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 155 ISHLKvlqcqgFY-------HLCGVHQEDVIYLALPLYHMSgSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVF 227
Cdd:PRK06155 200 CPHAQ------FYwwgrnsaEDLEIGADDVLYTTLPLFHTN-ALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVT 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 228 QYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNV--ATFNYTGRQGAVGRaswl 305
Cdd:PRK06155 273 YLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLDGYGSTETNFviAVTHGSQRPGSMGR---- 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 306 ykhifpfslirydVMTGEPIRNAQGHCMTTSPGEPGLLVapVSQQSPFL---GYAGAPElakdkllKDVFWSGDVFFNTG 382
Cdd:PRK06155 348 -------------LAPGFEARVVDEHDQELPDGEPGELL--LRADEPFAfatGYFGMPE-------KTVEAWRNLWFHTG 405
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 383 DLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAgMAALALRPPQALNLVQLYS 462
Cdd:PRK06155 406 DRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV-MAAVVLRDGTALEPVALVR 484
                        410
                 ....*....|....*...
gi 755503902 463 HVSENLPPYARPRFLRLQ 480
Cdd:PRK06155 485 HCEPRLAYFAVPRYVEFV 502
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
135-479 3.99e-48

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 175.60  E-value: 3.99e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 135 MDTCLYIFTSGTTGLPKAARISHLKVLQCQgfYHLC---GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFS 211
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAG--RALTerfGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFS 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVA-TF 290
Cdd:PRK13388 228 ASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIvVR 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 NYTGRQGAVGRAswlykhiFPfSLIRYDVMTGEPirnaqghCMTTSPGEPGLLVAP-------VSQQ--SPFLGYAGAPE 361
Cdd:PRK13388 307 EPGTPPGSIGRG-------AP-GVAIYNPETLTE-------CAVARFDAHGALLNAdeaigelVNTAgaGFFEGYYNNPE 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 LAKDKLLKDVFWSGDVFFNtgdllvcDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGR 441
Cdd:PRK13388 372 ATAERMRHGMYWSGDLAYR-------DADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE-RVGD 443
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 755503902 442 AGMAALALRPPQALNLVQL--YSHVSENLPPYARPRFLRL 479
Cdd:PRK13388 444 QVMAALVLRDGATFDPDAFaaFLAAQPDLGTKAWPRYVRI 483
PRK07867 PRK07867
acyl-CoA synthetase; Validated
135-479 7.13e-48

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 174.87  E-value: 7.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 135 MDTCLYIFTSGTTGLPKAARISHLKV-----LQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVasagvMLAQRF----GLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRK 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVAt 289
Cdd:PRK07867 228 FSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFG-CVVVDGFGSTEGGVA- 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYT--GRQGAVGRAswlykhifPFSLIRYDVMTGEPIRNAQ--GHCMTTSPGEPGLLVApVSQQSPFLGYAGAPELAKD 365
Cdd:PRK07867 306 ITRTpdTPPGALGPL--------PPGVAIVDPDTGTECPPAEdaDGRLLNADEAIGELVN-TAGPGGFEGYYNDPEADAE 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 366 KLLKDVFWSGDVFFntgdllvCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMA 445
Cdd:PRK07867 377 RMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDP-VVGDQVMA 448
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 755503902 446 ALALRPPQALNLVQL--YSHVSENLPPYARPRFLRL 479
Cdd:PRK07867 449 ALVLAPGAKFDPDAFaeFLAAQPDLGPKQWPSYVRV 484
AMP-binding pfam00501
AMP-binding enzyme;
56-406 7.46e-43

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 158.63  E-value: 7.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902   56 TASAAAVRVRSCWPQLGLPTLVEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPgylsaPQNIM 135
Cdd:pfam00501  81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPP-----PPDPD 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  136 DTCLYIFTSGTTGLPKAARISHL----KVLQCQGFYHLC-GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF 210
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRnlvaNVLSIKRVRPRGfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  211 SA---SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVR--LAVGSGLRPDTWERFLRRFGPlQILETYGMTEG 285
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlvLSGGAPLPPELARRFRELFGG-ALVNGYGLTET 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  286 NVATFNY------TGRQGAVGRaswlykhifPFSLIRY---DVMTGEPIRnaqghcmttsPGEPGLLVapVSQQSPFLGY 356
Cdd:pfam00501 315 TGVVTTPlpldedLRSLGSVGR---------PLPGTEVkivDDETGEPVP----------PGEPGELC--VRGPGVMKGY 373
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 755503902  357 AGAPELAkdkllKDVFWSGDvFFNTGDLLVCDEQGFLHFHDRTGDTFRWK 406
Cdd:pfam00501 374 LNDPELT-----AEAFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
129-479 1.33e-39

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 150.13  E-value: 1.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 129 SAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLK 207
Cdd:cd05941   83 SEPSLVLDPALILYTSGTTGRPKGVVLTHANLAaNVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 208 PKFSASQFWDDCQKHRVTVFQ-----YIGELCRYLVNQPPSK---AECDHKVRLAV-GSG-LRPDTWERFLRRFGpLQIL 277
Cdd:cd05941  163 PKFDPKEVAISRLMPSITVFMgvptiYTRLLQYYEAHFTDPQfarAAAAERLRLMVsGSAaLPVPTLEEWEAITG-HTLL 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 278 ETYGMTEGNVATFN-YTG--RQGAVGRAswlykhiFPFSLIR-YDVMTGEPirnaqghcmtTSPGEPG-LLVApvsqqSP 352
Cdd:cd05941  242 ERYGMTEIGMALSNpLDGerRPGTVGMP-------LPGVQARiVDEETGEP----------LPRGEVGeIQVR-----GP 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 353 --FLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTG-DTFRWKGENVATTEVAEVLETLDFLQEVN 429
Cdd:cd05941  300 svFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECA 373
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755503902 430 IYGVTVPGHeGRAGMAALALRPP-QALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05941  374 VIGVPDPDW-GERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLIL 423
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
136-475 6.00e-38

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 145.78  E-value: 6.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHqEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFS 211
Cdd:cd05936  126 DVAVLQYTSGTTGVPKGAMLTHrnlvANALQIKAWLEDLLEG-DDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFR 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVTVFQ-----YIGelcryLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTE 284
Cdd:cd05936  205 PIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTG-VPIVEGYGLTE 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 -GNVATFN-YTG--RQGAVGraswlykHIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAP 360
Cdd:cd05936  279 tSPVVAVNpLDGprKPGSIG-------IPLPGTEVK--------IVDDDGE--ELPPGEVGELW--VRGPQVMKGYWNRP 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 361 ElAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEG 440
Cdd:cd05936  340 E-ETAEAFVD----G--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDP-YSG 411
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 755503902 441 RAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05936  412 EAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR 446
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
106-471 1.07e-35

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 139.66  E-value: 1.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 106 VAGISNLLSEAADQVDEPVPGYLSAPQNimDTCLYIFTSGTTGLPKAARISH----LKVLQCQGFYHLCgVHQEDVIYLA 181
Cdd:cd05911  119 VLSIEDLLSPTLGEEDEDLPPPLKDGKD--DTAAILYSSGTTGLPKGVCLSHrnliANLSQVQTFLYGN-DGSNDVILGF 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 182 LPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKVRLAVGSG-L 259
Cdd:cd05911  196 LPLYHIYG-LFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPlLDKYDLSSLRVILSGGApL 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 260 RPDTWERFLRRFGPLQILETYGMTEGNVATF---NYTGRQGAVGRaswlykhIFPFSLIRYDVMTGepiRNAQGhcmtts 336
Cdd:cd05911  275 SKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSVGR-------LLPNVEAKIVDDDG---KDSLG------ 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 337 PGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVA 416
Cdd:cd05911  339 PNEPGEIC--VRGPQVMKGYYNNPEATKETFDED----G--WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELE 410
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 417 EVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPY 471
Cdd:cd05911  411 AVLLEHPGVADAAVIGIPDE-VSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY 464
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
96-486 1.72e-35

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 139.82  E-value: 1.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  96 HLWATGP----ETNVAGISNLLSEAADQVDEPVPgyLSAPqnimDTCLYIFTSGTTGLPKAARISHLKvLQCQGFYHL-- 169
Cdd:PRK08008 136 HICLTRValpaDDGVSSFTQLKAQQPATLCYAPP--LSTD----DTAEILFTSGTTSRPKGVVITHYN-LRFAGYYSAwq 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 170 CGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDH 249
Cdd:PRK08008 209 CALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQH 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 250 KVR-----LAVGSGLRPDtwerFLRRFGpLQILETYGMTEGNVATFNYTG----RQGAVGRASWLYKhifpfslirydvm 320
Cdd:PRK08008 289 CLRevmfyLNLSDQEKDA----FEERFG-VRLLTSYGMTETIVGIIGDRPgdkrRWPSIGRPGFCYE------------- 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 321 tgEPIRNAQGHCMttSPGEPG-LLVAPVSQQSPFLGYAGAPElAKDKLLkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRT 399
Cdd:PRK08008 351 --AEIRDDHNRPL--PAGEIGeICIKGVPGKTIFKEYYLDPK-ATAKVL-----EADGWLHTGDTGYVDEEGFFYFVDRR 420
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 400 GDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEgRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:PRK08008 421 CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRD-EAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEI 499

                 ....*...
gi 755503902 480 QVT-SRSC 486
Cdd:PRK08008 500 RKDlPRNC 507
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
134-478 3.16e-34

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 134.66  E-value: 3.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 134 IMDTCLYIFTSGTTGLPKAARISHLKVLqcqGFYHLCGVHQ----EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:cd17631   97 FDDLALLMYTSGTTGRPKGAMLTHRNLL---WNAVNALAALdlgpDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVF-----QYigelcrYLVNQPPSKAECDH-KVR-LAVGSGLRPDTWERFLRRFGPlQILETYGM 282
Cdd:cd17631  174 FDPETVLDLIERHRVTSFflvptMI------QALLQHPRFATTDLsSLRaVIYGGAPMPERLLRALQARGV-KFVQGYGM 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 283 TE-GNVATFNYTGRQ----GAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--FLG 355
Cdd:cd17631  247 TEtSPGVTFLSPEDHrrklGSAGRPV-------FFVEVR--------IVDPDGR--EVPPGEVGEIVV----RGPhvMAG 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtV 435
Cdd:cd17631  306 YWNRPEATAAAF-------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--V 376
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 755503902 436 PgHE--GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd17631  377 P-DEkwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVE 420
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
136-475 1.87e-32

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 130.51  E-value: 1.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVlqCQGFYHLCGVHQ---EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05926  150 DLALILHTSGTTGRPKGVPLTHRNL--AASATNITNTYKltpDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSA 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAEC-DHKVRLA--VGSGLRPDTWERFLRRFGpLQILETYGMTEgnvAT 289
Cdd:cd05926  228 STFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIrsCSASLPPAVLEALEATFG-APVLEAYGMTE---AA 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTGRQ--------GAVGRASwlykhifpfslirydvmtGEPIR--NAQGHCMTtsPGEPGLLVapVSQQSPFLGYAGA 359
Cdd:cd05926  304 HQMTSNPlppgprkpGSVGKPV------------------GVEVRilDEDGEILP--PGVVGEIC--LRGPNVTRGYLNN 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 360 PELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHE 439
Cdd:cd05926  362 PEANAEAAFKD----G--WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE-KY 434
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 755503902 440 GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05926  435 GEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPK 470
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
100-475 8.95e-32

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 129.46  E-value: 8.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 100 TGPETNVAGISNLLSEAADQVDEPVPGYLSApqniMDTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHLcGVHQED 176
Cdd:COG0365  153 TGADVPMEGDLDWDELLAAASAEFEPEPTDA----DDPLFILYTSGTTGKPKGVVHTHggyLVHAATTAKYVL-DLKPGD 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 177 VIYLALPLYHMSGSLLGIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFqyigelC------RYLVNQPPSKAE 246
Cdd:COG0365  228 VFWCTADIGWATGHSYIVYGPLLNGATVVLyegRPDFpDPGRLWELIEKYGVTVF------FtaptaiRALMKAGDEPLK 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 247 cDH---KVRLA--VGSGLRPDTWERFLRRFGpLQILETYGMTE--GNVATFNYTG--RQGAVGRaswlykhifPFSLIRY 317
Cdd:COG0365  302 -KYdlsSLRLLgsAGEPLNPEVWEWWYEAVG-VPIVDGWGQTEtgGIFISNLPGLpvKPGSMGK---------PVPGYDV 370
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 318 DVM--TGEPIRnaqghcmttsPGEPGLLVAPVSQQSPFLGYAGAPElakdkLLKDVFWS--GDVFFnTGDLLVCDEQGFL 393
Cdd:COG0365  371 AVVdeDGNPVP----------PGEEGELVIKGPWPGMFRGYWNDPE-----RYRETYFGrfPGWYR-TGDGARRDEDGYF 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 394 HFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVT-VPgHEGRaGMAALA---LRPPQALN--LVQ-LYSHVSE 466
Cdd:COG0365  435 WILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA---AVVgVP-DEIR-GQVVKAfvvLKPGVEPSdeLAKeLQAHVRE 509

                 ....*....
gi 755503902 467 NLPPYARPR 475
Cdd:COG0365  510 ELGPYAYPR 518
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
74-475 1.36e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 128.38  E-value: 1.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  74 PTLVEFLESLEPDLPALRamglHLWATGPETN------VAGISNLLSEAADQVDEPVPGylsapqnIMDTCLYIFTSGTT 147
Cdd:PRK06187 111 SEFVPLLAAILPQLPTVR----TVIVEGDGPAaplapeVGEYEELLAAASDTFDFPDID-------ENDAAAMLYTSGTT 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 148 GLPKAARISH----LKVLQCQGFYHLcgvHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHR 223
Cdd:PRK06187 180 GHPKGVVLSHrnlfLHSLAVCAWLKL---SRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDPENLLDLIETER 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 224 VTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTE-GNVATFNY-------- 292
Cdd:PRK06187 256 VTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFG-IDLVQGYGMTEtSPVVSVLPpedqlpgq 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHCMTTSPGEPGLLVApvsqQSPFL--GYAGAPELAKDKLLKD 370
Cdd:PRK06187 335 WTKRRSAGRP-------LPGVEAR--------IVDDDGDELPPDGGEVGEIIV----RGPWLmqGYWNRPEATAETIDGG 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 371 vfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALR 450
Cdd:PRK06187 396 --W-----LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDE-KWGERPVAVVVLK 467
                        410       420
                 ....*....|....*....|....*
gi 755503902 451 PPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK06187 468 PGATLDAKELRAFLRGRLAKFKLPK 492
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
71-478 1.25e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 125.40  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  71 LGLPTLVEFLESLEPDLPALRamglHLWATGPETNVAGISNLLSE----AADQVDEPVPGYlsAPQNIMDTclyIFTSGT 146
Cdd:PRK07656 107 FVLGLFLGVDYSATTRLPALE----HVVICETEEDDPHTEKMKTFtdflAAGDPAERAPEV--DPDDVADI---LFTSGT 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 147 TGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVT 225
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSnAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERIT 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 226 VFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGN-VATFNYTGRQ-----G 297
Cdd:PRK07656 258 VLPGPPTMYNSLLQHPDRSAEDLSSLRLAVtgAASMPVALLERFESELGVDIVLTGYGLSEASgVTTFNRLDDDrktvaG 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 298 AVGRAswlykhifpfslirydvMTGEPIRNAQGHCMTTSPGEPG-LLVapvsqQSP--FLGYAGAPELAKDKLlkdvfwS 374
Cdd:PRK07656 338 TIGTA-----------------IAGVENKIVNELGEEVPVGEVGeLLV-----RGPnvMKGYYDDPEATAAAI------D 389
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 375 GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GRAGMAALALRPPQ 453
Cdd:PRK07656 390 ADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG--VPDERlGEVGKAYVVLKPGA 467
                        410       420
                 ....*....|....*....|....*
gi 755503902 454 ALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:PRK07656 468 ELTEEELIAYCREHLAKYKVPRSIE 492
PRK07868 PRK07868
acyl-CoA synthetase; Validated
176-478 6.41e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 112.89  E-value: 6.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 176 DVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV 255
Cdd:PRK07868 647 DTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFI 726
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 256 GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTG-RQGAVGRAswlykhiFPFS----LIRYDVMTGEPIRNAQG 330
Cdd:PRK07868 727 GSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaKIGSKGRP-------LPGAgrveLAAYDPEHDLILEDDRG 799
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 331 HCMTTSPGEPGLLvapvsqqspfLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENV 410
Cdd:PRK07868 800 FVRRAEVNEVGVL----------LARARGPIDPTASVKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPV 869
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 411 ATTEVAEVLETLDFLQEVNIYGVTVPGHEgrAGMAALALRPPQALNLVQLYSHVSEnLPPYARPRFLR 478
Cdd:PRK07868 870 YTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAAVTLRPGAAITAADLTEALAS-LPVGLGPDIVH 934
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
87-475 1.25e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 110.86  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  87 LPALRAMGLHLwaTGPETNVAGISNLLSEAA----DQVDEPVPgylsAPQnimDTCLYIFTSGTTGLPKAARISH--LKV 160
Cdd:PRK05605 176 IPALRKARAAL--TGPAPGTVPWETLVDAAIggdgSDVSHPRP----TPD---DVALILYTSGTTGKPKGAQLTHrnLFA 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 161 LQCQGFYHLCGV-HQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVN 239
Cdd:PRK05605 247 NAAQGKAWVPGLgDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 240 QPPSKAECDHKVRLAVgSG---LRPDTWERFLRRFGPLqILETYGMTE------GNvaTFNYTGRQGAVGRAswlykhiF 310
Cdd:PRK05605 327 AAEERGVDLSGVRNAF-SGamaLPVSTVELWEKLTGGL-LVEGYGLTEtspiivGN--PMSDDRRPGYVGVP-------F 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 311 PFSLIRydvmtgepIRNAQGHCMTTSPGEPGLLVAPVSQQspFLGYAGAPELAKDKLLKDvfWsgdvfFNTGDLLVCDEQ 390
Cdd:PRK05605 396 PDTEVR--------IVDPEDPDETMPDGEEGELLVRGPQV--FKGYWNRPEETAKSFLDG--W-----FRTGDVVVMEED 458
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 391 GFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHEGRAGM-AALALRPPQALNLVQLYSHVSENLP 469
Cdd:PRK05605 459 GFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVG--LPREDGSEEVvAAVVLEPGAALDPEGLRAYCREHLT 536

                 ....*.
gi 755503902 470 PYARPR 475
Cdd:PRK05605 537 RYKVPR 542
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
136-475 1.90e-24

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 105.88  E-value: 1.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHlcGVHQEDVIY-LALP--LYHMSGSLLGIvgcLGIGATVVL--K 207
Cdd:cd05972   82 DPALIYFTSGTTGLPKGVLHTHsypLGHIPTAAYWL--GLRPDDIHWnIADPgwAKGAWSSFFGP---WLLGATVFVyeG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 208 PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHkVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEG 285
Cdd:cd05972  157 PRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-LRLVVSAGepLNPEVIEWWRAATG-LPIRDGYGQTET 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVATFNYTG---RQGAVGRASWLYKhifpFSLIRYDvmtGEPIrnaqghcmttSPGEPGLLVAPVSQQSPFLGYAGAPEl 362
Cdd:cd05972  235 GLTVGNFPDmpvKPGSMGRPTPGYD----VAIIDDD---GREL----------PPGEEGDIAIKLPPPGLFLGYVGDPE- 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 aKDKllkdVFWSGDVFFnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQ--EVNIYGVTVPGHEG 440
Cdd:cd05972  297 -KTE----ASIRGDYYL-TGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL-----LEhpAVAEAAVVGSPDPV 365
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 755503902 441 RAGM--AALALR----PPQALNLvQLYSHVSENLPPYARPR 475
Cdd:cd05972  366 RGEVvkAFVVLTsgyePSEELAE-ELQGHVKKVLAPYKYPR 405
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
136-477 2.49e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 104.28  E-value: 2.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQcQGFY--HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSA 212
Cdd:cd05917    3 DVINIQFTSGTTGSPKGATLTHHNIVN-NGYFigERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQ-----YIGELCRylvnqpPSKAECD-HKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:cd05917   82 LAVLEAIEKEKCTALHgvptmFIAELEH------PDFDKFDlSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 GNVATFNYTG------RQGAVGRaswlykhIFPFSLIRYDVMTG--EPIRNAQGHCMTTspgepGLLVapvsqqspFLGY 356
Cdd:cd05917  156 TSPVSTQTRTddsiekRVNTVGR-------IMPHTEAKIVDPEGgiVPPVGVPGELCIR-----GYSV--------MKGY 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVP 436
Cdd:cd05917  216 WNDPEKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG--VP 287
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 755503902 437 GHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd05917  288 DERyGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYV 329
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
78-475 1.46e-22

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 101.29  E-value: 1.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  78 EFLESLEPDLPALRAMGLHLWATGPETNVAGISNLlseaADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISH 157
Cdd:cd05959  110 ELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLL----AELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLH 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 158 lkvlqcQGFYHLC--------GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF-SASQFWDDCQKHRVTVFQ 228
Cdd:cd05959  186 ------ADIYWTAelyarnvlGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFF 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 229 YIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTE-GNVATFNYTG--RQGAVGRAS 303
Cdd:cd05959  260 GVPTLYAAMLAAPNLPSRDLSSLRLCVSAGeaLPAEVGERWKARFG-LDILDGIGSTEmLHIFLSNRPGrvRYGTTGKPV 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 304 WLYKhifpfslIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvfWsgdvfFNTGD 383
Cdd:cd05959  339 PGYE-------VE--------LRDEDGG--DVADGEPGELY--VRGPSSATMYWNNRDKTRDTFQGE--W-----TRTGD 392
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 384 LLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAgMAALALRP---PQALNLVQL 460
Cdd:cd05959  393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKP-KAFVVLRPgyeDSEALEEEL 471
                        410
                 ....*....|....*
gi 755503902 461 YSHVSENLPPYARPR 475
Cdd:cd05959  472 KEFVKDRLAPYKYPR 486
PRK07470 PRK07470
acyl-CoA synthetase; Validated
136-475 1.90e-22

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 100.89  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVlqcqGFY---HLC----GVHQEDVIYLALPLYHMSG--SLLGIVGclgiGATVVL 206
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQM----AFVitnHLAdlmpGTTEQDASLVVAPLSHGAGihQLCQVAR----GAATVL 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 KP--KFSASQFWDDCQKHRVTVFQYIGELCRYLVnQPPSKAECDH-KVRLAVGSG---LRPDTwERFLRRFGPLqILETY 280
Cdd:PRK07470 236 LPseRFDPAEVWALVERHRVTNLFTVPTILKMLV-EHPAVDRYDHsSLRYVIYAGapmYRADQ-KRALAKLGKV-LVQYF 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 281 GMTEgnvATFNYT--------------GRQGAVGRASwlykhifpfslirydvmTGE--PIRNAQGHCMttSPGEPGLLV 344
Cdd:PRK07470 313 GLGE---VTGNITvlppalhdaedgpdARIGTCGFER-----------------TGMevQIQDDEGREL--PPGETGEIC 370
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 345 apVSQQSPFLGYAGAPElAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:PRK07470 371 --VIGPAVFAGYYNNPE-ANAKAFRD-GW-----FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPA 441
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755503902 425 LQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK07470 442 VSEVAVLGVPDPVW-GEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPK 491
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
141-479 2.18e-22

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 99.91  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHlkvlqcQGFYHLCGVHQEDV------IYLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FS 211
Cdd:cd05930   99 IYTSGSTGKPKGVMVEH------RGLVNLLLWMQEAYpltpgdRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEevrKD 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAecDHKVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTEGNV-A 288
Cdd:cd05930  173 PEALADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGeaLPPDLVRRWRELLPGARLVNLYGPTEATVdA 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFnytgrqgavgraswlykHIFPFSLIRYDVMT-GEPIRNAQ-----GHCMTTSPGEPGLLVapVSQQSPFLGYAGAPEL 362
Cdd:cd05930  251 TY-----------------YRVPPDDEEDGRVPiGRPIPNTRvyvldENLRPVPPGVPGELY--IGGAGLARGYLNRPEL 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 AKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDT-----FRwkgenVATTEVAEVLETLDFLQEVniygVTVPG 437
Cdd:cd05930  312 TAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQvkirgYR-----IELGEIEAALLAHPGVREA----AVVAR 382
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 755503902 438 HEGRAGM---AALALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd05930  383 EDGDGEKrlvAYVVPDEGGELDEEELRAHLAERLPDYMVPsAFVVL 428
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
110-419 2.83e-22

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 100.39  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 110 SNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLK-VLQCQGF--YHLCGVHQEDVIYLALPLYH 186
Cdd:cd05904  133 FDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNlIAMVAQFvaGEGSNSDSEDVFLCVLPMFH 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 187 MSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFqyigelcrYLVnqPP-----SKAECDHKVRLA----VGS 257
Cdd:cd05904  213 IYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHL--------PVV--PPivlalVKSPIVDKYDLSslrqIMS 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 258 G---LRPDTWERFLRRFGPLQILETYGMTE-GNVATFNYT-----GRQGAVGR--ASWLYKHIfpfsliryDVMTGEPIr 326
Cdd:cd05904  283 GaapLGKELIEAFRAKFPNVDLGQGYGMTEsTGVVAMCFApekdrAKYGSVGRlvPNVEAKIV--------DPETGESL- 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 327 naqghcmttSPGEPG-LLVapvsqQSPFL--GYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTF 403
Cdd:cd05904  354 ---------PPNQTGeLWI-----RGPSImkGYLNNPEATAATIDKE----G--WLHTGDLCYIDEDGYLFIVDRLKELI 413
                        330
                 ....*....|....*.
gi 755503902 404 RWKGENVATTEVAEVL 419
Cdd:cd05904  414 KYKGFQVAPAELEALL 429
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
136-451 1.17e-21

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 97.55  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd05935   85 DLALIPYTSGTTGLPKGCMHTHFSAAaNALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRET 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEG-NVATFN 291
Cdd:cd05935  165 ALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTG-LRFVEGYGLTETmSQTHTN 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTGRQgavgRASWLYKHIFPFSLIRYDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDv 371
Cdd:cd05935  244 PPLRP----KLQCLGIP*FGVDARVIDIETGREL----------PPNEVGEIV--VRGPQIFKGYWNRPEETEESFIEI- 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 372 fwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHE-GRAGMAALALR 450
Cdd:cd05935  307 --KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCV--ISVPDERvGEEVKAFIVLR 382

                 .
gi 755503902 451 P 451
Cdd:cd05935  383 P 383
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
112-479 3.42e-21

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 96.74  E-value: 3.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 112 LLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSG- 189
Cdd:cd05922   97 LDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLaNARSIAEYLGITADDRALTVLPLSYDYGl 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 190 SLLGIvgCLGIGATVVLKPKFSASQ-FWDDCQKHRVTVFQ---YIGELCRYLVNQPpskAECDHKVRLAVGSGLRPDTWE 265
Cdd:cd05922  174 SVLNT--HLLRGATLVLTNDGVLDDaFWEDLREHGATGLAgvpSTYAMLTRLGFDP---AKLPSLRYLTQAGGRLPQETI 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 266 RFLRRFGPL-QILETYGMTEgnvATFNYT--------GRQGAVGRAswlykhiFP---FSLIRYDvmtGEPirnaqghcm 333
Cdd:cd05922  249 ARLRELLPGaQVYVMYGQTE---ATRRMTylpperilEKPGSIGLA-------IPggeFEILDDD---GTP--------- 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 334 tTSPGEPGLLVApvsqQSPF--LGYAGAP-ELAKDKLLKDVFWsgdvffnTGDLLVCDEQGFLHFHDRTGDTFRWKGENV 410
Cdd:cd05922  307 -TPPGEPGEIVH----RGPNvmKGYWNDPpYRRKEGRGGGVLH-------TGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755503902 411 ATTEVAEVLETLDFLQEVNIYGVTVPGHEgraGMAALALRPPQaLNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05922  375 SPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPDK-IDPKDVLRSLAERLPPYKVPATVRV 439
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
136-478 9.04e-21

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 93.72  E-value: 9.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLAL-PLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd17638    1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIInPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 292
Cdd:cd17638   81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtgAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMCR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TGRqgavgraswlykhifPFSLIRYDVmtGEPIRNAQGHCmttspGEPGLLVapVSQQSPFLGYAGAPELAKDKLlkdvf 372
Cdd:cd17638  161 PGD---------------DAETVATTC--GRACPGFEVRI-----ADDGEVL--VRGYNVMQGYLDDPEATAEAI----- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 373 wSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GRAGMAALALRP 451
Cdd:cd17638  212 -DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG--VPDERmGEVGKAFVVARP 288
                        330       340
                 ....*....|....*....|....*..
gi 755503902 452 PQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd17638  289 GVTLTEEDVIAWCRERLANYKVPRFVR 315
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
139-475 1.09e-20

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 93.24  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAARISH---LKVLQCQGfyHLCGVHQEDVIYLALPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd17633    3 FYIgFTSGTTGLPKAYYRSErswIESFVCNE--DLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQppskAECDHKVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 292
Cdd:cd17633   80 WIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGqkLFESTKKKLKNIFPKANLIEFYGTSELSFITYNF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TG---RQGAVGRaswlykhIFPFSLIRydvmtgepIRNAQGhcmttspGEPGLLVApvsqQSP--FLGYAGAPELAKDKl 367
Cdd:cd17633  156 NQesrPPNSVGR-------PFPNVEIE--------IRNADG-------GEIGKIFV----KSEmvFSGYVRGGFSNPDG- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 368 lkdvfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTvpgHEGRaGMAAL 447
Cdd:cd17633  209 -----W-----MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP---DARF-GEIAV 274
                        330       340
                 ....*....|....*....|....*...
gi 755503902 448 ALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd17633  275 ALYSGDKLTYKQLKRFLKQKLSRYEIPK 302
PRK07788 PRK07788
acyl-CoA synthetase; Validated
77-475 1.39e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 95.38  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  77 VEFLESLEPDLPALRAMGLHlwATGPETNVAGISNLLSEAADQVDEPVPgylSAPQNimdTCLYIFTSGTTGLPKAARIS 156
Cdd:PRK07788 157 TDLLSALPPDLGRLRAWGGN--PDDDEPSGSTDETLDDLIAGSSTAPLP---KPPKP---GGIVILTSGTTGTPKGAPRP 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 157 HLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCR 235
Cdd:PRK07788 229 EPSPLApLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLS 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 236 YLVNQPP---SKAECDH-KVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTEGNVATFnyTGRQ------GAVGRaswl 305
Cdd:PRK07788 308 RILDLGPevlAKYDTSSlKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAFATI--ATPEdlaeapGTVGR---- 380
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 306 ykhifPFSLIR---YDvMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGapelAKDKLLKDVFWSgdvffnTG 382
Cdd:PRK07788 381 -----PPKGVTvkiLD-ENGNEV----------PRGVVGRIF--VGNGFPFEGYTD----GRDKQIIDGLLS------SG 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 383 DLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP--GHEGRagmAALALRPPQALNLVQL 460
Cdd:PRK07788 433 DVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefGQRLR---AFVVKAPGAALDEDAI 509
                        410
                 ....*....|....*
gi 755503902 461 YSHVSENLPPYARPR 475
Cdd:PRK07788 510 KDYVRDNLARYKVPR 524
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
136-475 1.77e-20

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 94.07  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLK-VLQCQGF-YHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF-SA 212
Cdd:cd05919   92 DIAYLLYSSGTTGPPKGVMHAHRDpLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTA 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTEgNVATF 290
Cdd:cd05919  172 ERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATE-VGHIF 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 --NYTG--RQGAVGRaswlykhIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDK 366
Cdd:cd05919  250 lsNRPGawRLGSTGR-------PVPGYEIR--------LVDEEGH--TIPPGEEGDLL--VRGPSAAVGYWNNPEKSRAT 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTvPGHEGRAGMAA 446
Cdd:cd05919  311 FN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVP-ESTGLSRLTAF 382
                        330       340       350
                 ....*....|....*....|....*....|..
gi 755503902 447 LALRPPQALNLV---QLYSHVSENLPPYARPR 475
Cdd:cd05919  383 VVLKSPAAPQESlarDIHRHLLERLSAHKVPR 414
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
136-419 1.84e-20

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 93.98  E-value: 1.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH--LKVLQCQGFYHLcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSAS 213
Cdd:cd05903   94 AVALLLFTSGTTGEPKGVMHSHntLSASIRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPD 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQ----YIGELCRYLVNQPPskAECDHKVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTEGNVAT 289
Cdd:cd05903  173 KALALMREHGVTFMMgatpFLTDLLNAVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECPGAV 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTgrQGAVGRASWLYKHIFPfslirydvmtGEPIRNAQGHCMTTSPGEPGLLVApvsqQSP--FLGYAGAPELAKDKL 367
Cdd:cd05903  250 TSIT--PAPEDRRLYTDGRPLP----------GVEIKVVDDTGATLAPGVEGELLS----RGPsvFLGYLDRPDLTADAA 313
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755503902 368 lkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:cd05903  314 -------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLL 358
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
131-475 3.13e-20

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 94.33  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 131 PQNimDTCLYIFTSGTTGLPKAARISHLKVLQCQgfyhLCGVH-------QEDVIYLALPLYHMSGslLGIVGCLGI--G 201
Cdd:PRK06710 204 PEN--DLALLQYTGGTTGFPKGVMLTHKNLVSNT----LMGVQwlynckeGEEVVLGVLPFFHVYG--MTAVMNLSImqG 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 202 ATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV-GSGLRP-DTWERFLRRFGPlQILET 279
Cdd:PRK06710 276 YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSAPLPvEVQEKFETVTGG-KLVEG 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 280 YGMTEGNVAT---FNYTGR-QGAVGrASWLYKHIFPFSLirydvMTGEPIRnaqghcmttsPGEPGLLVapVSQQSPFLG 355
Cdd:PRK06710 355 YGLTESSPVThsnFLWEKRvPGSIG-VPWPDTEAMIMSL-----ETGEALP----------PGEIGEIV--VKGPQIMKG 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTV 435
Cdd:PRK06710 417 YWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPD 489
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 755503902 436 PgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK06710 490 P-YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPK 528
PRK07529 PRK07529
AMP-binding domain protein; Validated
107-419 5.09e-20

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 93.87  E-value: 5.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 107 AGISNLLSEAADQvdePVPGYLSAPQ-NIMDTCLYIFTSGTTGLPKAARISHL-KVLQCQGFYHLCGVHQEDVIYLALPL 184
Cdd:PRK07529 187 ARILDFDAELARQ---PGDRLFSGRPiGPDDVAAYFHTGGTTGMPKLAQHTHGnEVANAWLGALLLGLGPGDTVFCGLPL 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 185 YHMSGSLLGIVGCLGIGATVVLKPKFSA------SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDhKVRLAV--G 256
Cdd:PRK07529 264 FHVNALLVTGLAPLARGAHVVLATPQGYrgpgviANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDIS-SLRYALcgA 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 257 SGLRPDTWERFLRRFGpLQILETYGMTEGN-VATFNYTG---RQGAVGRAswlykhiFPFSLIRydVMTGEPIRNAQGHC 332
Cdd:PRK07529 343 APLPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNPPDgerRIGSVGLR-------LPYQRVR--VVILDDAGRYLRDC 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 333 mttSPGEPGLLVapVSQQSPFLGYAgapELAKDKLLkdvfWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVAT 412
Cdd:PRK07529 413 ---AVDEVGVLC--IAGPNVFSGYL---EAAHNKGL----WLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDP 480

                 ....*..
gi 755503902 413 TEVAEVL 419
Cdd:PRK07529 481 AAIEEAL 487
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
136-478 1.97e-19

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 91.00  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ-CQGF-YHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSAS 213
Cdd:cd05958   98 DICILAFTSGTTGAPKATMHFHRDPLAsADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPD 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEGNVATFN 291
Cdd:cd05958  178 LLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGeaLPAALHRAWKEATG-IPIIDGIGSTEMFHIFIS 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTGRQGAVGRaswlykhifpfslirydvmTGEP-------IRNAQGHcmTTSPGEPGLLVApvsqQSPfLGYAGapeLAk 364
Cdd:cd05958  257 ARPGDARPGA-------------------TGKPvpgyeakVVDDEGN--PVPDGTIGRLAV----RGP-TGCRY---LA- 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DKLLKDVFwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGhEGRAGM 444
Cdd:cd05958  307 DKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDES-RGVVVK 383
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 755503902 445 AALALRP---PQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd05958  384 AFVVLRPgviPGPVLARELQDHAKAHIAPYKYPRAIE 420
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
83-474 2.39e-19

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 91.11  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  83 LEPDLPA--LRAM-------------GLHLWATGPETNVagisnLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTT 147
Cdd:cd12117   77 LDPELPAerLAFMladagakvlltdrSLAGRAGGLEVAV-----VIDEALDAGPAGNPAVPVSPD---DLAYVMYTSGST 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 148 GLPKAARISHLKVLQ-CQGFYHLcGVHQEDVIYLALPLyHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHR 223
Cdd:cd12117  149 GRPKGVAVTHRGVVRlVKNTNYV-TLGPDDRVLQTSPL-AFDASTFEIWGALLNGARLVLAPKgtlLDPDALGALIAEEG 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 224 VTVFQYIGELCRYLVNQPPskaECDHKVR--LAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGR 301
Cdd:cd12117  227 VTVLWLTAALFNQLADEDP---ECFAGLRelLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVA 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 302 ASwlykhifpfslirydVMTGEPIRNAQGHCMTTS-----PGEPGLLV---APVSqqspfLGYAGAPELAKDKLLKDVFW 373
Cdd:cd12117  304 GS---------------IPIGRPIANTRVYVLDEDgrpvpPGVPGELYvggDGLA-----LGYLNRPALTAERFVADPFG 363
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 374 SGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVTVpgHEGRAGMAALA--LRP 451
Cdd:cd12117  364 PGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREA---VVVV--REDAGGDKRLVayVVA 438
                        410       420
                 ....*....|....*....|...
gi 755503902 452 PQALNLVQLYSHVSENLPPYARP 474
Cdd:cd12117  439 EGALDAAELRAFLRERLPAYMVP 461
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
141-475 4.32e-19

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 89.71  E-value: 4.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAarishlkVLQCQG--FYHL------CGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05912   83 MYTSGTTGKPKG-------VQQTFGnhWWSAigsalnLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDA 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPlqILETYGMTE--GNVATF 290
Cdd:cd05912  155 EQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIP--VYQSYGMTEtcSQIVTL 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 NYT---GRQGAVGRASwlykhiFPFSLirydvmtgePIRNAQGhcmttSPGEPG--LLVAP-VSQqspflGYAGAPELAK 364
Cdd:cd05912  233 SPEdalNKIGSAGKPL------FPVEL---------KIEDDGQ-----PPYEVGeiLLKGPnVTK-----GYLNRPDATE 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGHE----G 440
Cdd:cd05912  288 E-----SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL-----LSHPAIKEAGVVGIPddkwG 355
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 755503902 441 RAGMAALALRPPqaLNLVQLYSHVSENLPPYARPR 475
Cdd:cd05912  356 QVPVAFVVSERP--ISEEELIAYCSEKLAKYKVPK 388
PRK06145 PRK06145
acyl-CoA synthetase; Validated
125-490 9.33e-19

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 89.56  E-value: 9.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 125 PGYLSAPQNIMDtclYIFTSGTTGLPKAARISHLKVlQCQGFYHLC--GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGA 202
Cdd:PRK06145 142 PQAAVAPTDLVR---LMYTSGTTDRPKGVMHSYGNL-HWKSIDHVIalGLTASERLLVVGPLYHVGAFDLPGIAVLWVGG 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 203 TVVLKPKFSASQFWDDCQKHRVTVFQYIG-ELCRYLVNQPPSKAECDhKVRLAVGSGLRpdTWERFLRRFGPL----QIL 277
Cdd:PRK06145 218 TLRIHREFDPEAVLAAIERHRLTCAWMAPvMLSRVLTVPDRDRFDLD-SLAWCIGGGEK--TPESRIRDFTRVftraRYI 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 278 ETYGMTE---GNvaTFNYTGRQ----GAVGRAswlYKHIfpfslirydvmtgePIRNAQGHCMTTSPGEPG--LLVAPVS 348
Cdd:PRK06145 295 DAYGLTEtcsGD--TLMEAGREiekiGSTGRA---LAHV--------------EIRIADGAGRWLPPNMKGeiCMRGPKV 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 349 QQspflGYAGAPELAKDKLLKDVFWSGDVFFntgdllvCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEV 428
Cdd:PRK06145 356 TK----GYWKDPEKTAEAFYGDWFRSGDVGY-------LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEA 424
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 429 NIYGVtvpgHEGRAG---MAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQvtsRSCP-NPS 490
Cdd:PRK06145 425 AVIGV----HDDRWGeriTAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVR---DELPrNPS 483
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
106-474 1.24e-18

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 88.87  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 106 VAGISNLLSEAADQVDEPVPgyLSAPQNIMDTCLYIFTSGTTGLPKAarishlkVLQCQGfYHL---------CGVHQED 176
Cdd:PRK03640 114 IPGISVKFAELMNGPKEEAE--IQEEFDLDEVATIMYTSGTTGKPKG-------VIQTYG-NHWwsavgsalnLGLTEDD 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 177 VIYLALPLYHMSG-SLLgiVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPsKAECDHKVR-LA 254
Cdd:PRK03640 184 CWLAAVPIFHISGlSIL--MRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLG-EGTYPSSFRcML 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 255 VGSGLRP-DTWERFLRRFGPlqILETYGMTE--GNVATFNYTGRQGAVGRASwlyKHIFPFSL-IRYDVMTGEPirNAQG 330
Cdd:PRK03640 261 LGGGPAPkPLLEQCKEKGIP--VYQSYGMTEtaSQIVTLSPEDALTKLGSAG---KPLFPCELkIEKDGVVVPP--FEEG 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 331 HCMTTSPGepgllVAPvsqqspflGYagapeLAKDKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENV 410
Cdd:PRK03640 334 EIVVKGPN-----VTK--------GY-----LNREDATRETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 393
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 411 ATTEVAEVLETLDFLQEVNIYGVTvpghEGRAGMAALA-LRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK03640 394 YPAEIEEVLLSHPGVAEAGVVGVP----DDKWGQVPVAfVVKSGEVTEEELRHFCEEKLAKYKVP 454
PRK07514 PRK07514
malonyl-CoA synthase; Validated
75-456 2.75e-18

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 88.01  E-value: 2.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  75 TLVE---FLESLEPDL--------PALRAMGLHLWATGPET-NVAGISNLLSEAADQVDEPVPgylsAPQNIMDTCLYIF 142
Cdd:PRK07514  88 TLAEldyFIGDAEPALvvcdpanfAWLSKIAAAAGAPHVETlDADGTGSLLEAAAAAPDDFET----VPRGADDLAAILY 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 143 TSGTTGLPKAARISH------LKVL-QCQGFyhlcgvHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQF 215
Cdd:PRK07514 164 TSGTTGRSKGAMLSHgnllsnALTLvDYWRF------TPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAV 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDdcQKHRVTVFQ-----YIgelcRYLVNQPPSKAECDHkVRLAV-GSG-LRPDTWERFLRRFGpLQILETYGMTEGNVA 288
Cdd:PRK07514 238 LA--LMPRATVMMgvptfYT----RLLQEPRLTREAAAH-MRLFIsGSApLLAETHREFQERTG-HAILERYGMTETNMN 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFN-YTG--RQGAVGraswlykhiFPF---SLIRYDVMTGEPIrnaqghcmttSPGEPGLLvaPVSQQSPFLGYAGAPEL 362
Cdd:PRK07514 310 TSNpYDGerRAGTVG---------FPLpgvSLRVTDPETGAEL----------PPGEIGMI--EVKGPNVFKGYWRMPEK 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 AKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRA 442
Cdd:PRK07514 369 TAEEF------RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEG 441
                        410
                 ....*....|....
gi 755503902 443 GMAALALRPPQALN 456
Cdd:PRK07514 442 VTAVVVPKPGAALD 455
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
142-433 3.78e-18

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 87.80  E-value: 3.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSllgIVGCL-----GIGATVVLKPKfSA 212
Cdd:PRK08974 213 YTGGTTGVAKGAMLTHrnmlANLEQAKAAYGPLLHPGKELVVTALPLYHIFAL---TVNCLlfielGGQNLLITNPR-DI 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKaECD-HKVRLAVGSGLR-----PDTWERFLRRFgplqILETYGMTEGN 286
Cdd:PRK08974 289 PGFVKELKKYPFTAITGVNTLFNALLNNEEFQ-ELDfSSLKLSVGGGMAvqqavAERWVKLTGQY----LLEGYGLTECS 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 ----VATFNYTGRQGAVGraswlykhiFPFSlirydvMTGEPIRNAQGHcmTTSPGEPGLLVAPVSQQspFLGYAGAPEl 362
Cdd:PRK08974 364 plvsVNPYDLDYYSGSIG---------LPVP------STEIKLVDDDGN--EVPPGEPGELWVKGPQV--MLGYWQRPE- 423
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755503902 363 AKDKLLKDVFWSgdvffnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:PRK08974 424 ATDEVIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
78-460 4.62e-18

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 87.42  E-value: 4.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  78 EFLESLEPDLPALRamglHLWATGPETNVaGISNLLSEAADQVDEPVPGYLSAPQ-NIMDTCLYIFTSGTTGLPKAARIS 156
Cdd:PRK13295 144 AMARRLRPELPALR----HVVVVGGDGAD-SFEALLITPAWEQEPDAPAILARLRpGPDDVTQLIYTSGTTGEPKGVMHT 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 157 HLKVLQCQGFY-HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTvFQ-----YI 230
Cdd:PRK13295 219 ANTLMANIVPYaERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVT-FTmastpFL 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 231 GELCRYLVNQPPSKAECdhKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVATFNYTGRqgAVGRASWLYKHIF 310
Cdd:PRK13295 298 TDLTRAVKESGRPVSSL--RTFLCAGAPIPGALVERARAALG-AKIVSAWGMTENGAVTLTKLDD--PDERASTTDGCPL 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 311 PFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDkllkdvfwSGDVFFNTGDLLVCDEQ 390
Cdd:PRK13295 373 PGVEVR--------VVDADGA--PLPAGQIGRLQ--VRGCSNFGGYLKRPQLNGT--------DADGWFDTGDLARIDAD 432
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902 391 GFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPghEGRAGMAALA---LRPPQALNLVQL 460
Cdd:PRK13295 433 GYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAI--VAYP--DERLGERACAfvvPRPGQSLDFEEM 501
PRK08316 PRK08316
acyl-CoA synthetase; Validated
74-475 5.84e-18

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 86.91  E-value: 5.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  74 PTLVEFLESLEPDLPALRAMGLHLWATG-PETNVAGISNLLSEAADQVDEPVPgylsapqNIMDTCLYIFTSGTTGLPKA 152
Cdd:PRK08316 116 PALAPTAEAALALLPVDTLILSLVLGGReAPGGWLDFADWAEAGSVAEPDVEL-------ADDDLAQILYTSGTESLPKG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 153 ARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVF---- 227
Cdd:PRK08316 189 AMLTHRALIaEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERITSFfapp 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 228 -QYIGelcryLVNQPpskaECDhKVRLavgSGLR---------P-DTWERFLRRFGPLQILETYGMTE-GNVATF----N 291
Cdd:PRK08316 269 tVWIS-----LLRHP----DFD-TRDL---SSLRkgyygasimPvEVLKELRERLPGLRFYNCYGQTEiAPLATVlgpeE 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTGRQGAVGRASwlykhIFPFSLIRYDvmTGEPIrnaqghcmttSPGEPGLLVApvsqQSPFL--GYAGAPELAKDkllk 369
Cdd:PRK08316 336 HLRRPGSAGRPV-----LNVETRVVDD--DGNDV----------APGEVGEIVH----RSPQLmlGYWDDPEKTAE---- 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 370 dVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALAL 449
Cdd:PRK08316 391 -AFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP-KWIEAVTAVVVP 466
                        410       420
                 ....*....|....*....|....*.
gi 755503902 450 RPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK08316 467 KAGATVTEDELIAHCRARLAGFKVPK 492
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
129-398 1.37e-17

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 85.85  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 129 SAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL----QCQGFYHLcgvHQEDVIYLALPLYHMSGSLLGIVGCLGIGATV 204
Cdd:cd05909  141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLanveQITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 205 VLKPK-FSASQFWDDCQKHRVTVFQYIGELCRYLVNQppSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYG 281
Cdd:cd05909  218 VFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYG 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTEG----NVATFNYTGRQGAVGRaswlykhifPFSLIRY---DVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFL 354
Cdd:cd05909  295 TTECspviSVNTPQSPNKEGTVGR---------PLPGMEVkivSVETHEEV----------PIGEGGLLL--VRGPNVML 353
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 755503902 355 GYAGAPElakdkllKDVFWSGDVFFNTGDLLVCDEQGFLHFHDR 398
Cdd:cd05909  354 GYLNEPE-------LTSFAFGDGWYDTGDIGKIDGEGFLTITGR 390
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
136-447 3.00e-17

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 84.57  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPkfSASQ 214
Cdd:cd05907   88 DLATIIYTSGTTGRPKGVMLSHRNILsNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAET 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHK---VRLAVGSGLR----------PDTwERFLRRFGpLQILETYG 281
Cdd:cd05907  166 LLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKrklFDLAVGGRLRfaasggaplpAEL-LHFFRALG-IPVYEGYG 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTE-GNVATFNYTGRQ--GAVGRaswlykhifpfslirydVMTGEPIR-NAQGHCMTTSPgepgllvapvsqqSPFLGYA 357
Cdd:cd05907  244 LTEtSAVVTLNPPGDNriGTVGK-----------------PLPGVEVRiADDGEILVRGP-------------NVMLGYY 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 358 GAPELAKDKLLKDVfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRW-KGENVATTEVAEVLETLDFLQEVNIYGvtvp 436
Cdd:cd05907  294 KNPEATAEALDADG-W-----LHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG---- 363
                        330
                 ....*....|.
gi 755503902 437 ghEGRAGMAAL 447
Cdd:cd05907  364 --DGRPFLVAL 372
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
102-477 3.01e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 84.83  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 102 PETNVAGISNLLSEAADQVdEPVPGYLSAPQNIMdtclyiFTSGTTGLPKAARISHLKvLQCQGFYHLCGVH---QEDVI 178
Cdd:PRK07786 148 SDDSVLGYEDLLAEAGPAH-APVDIPNDSPALIM------YTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNGadiNSDVG 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 179 YLALPLYHMSGslLGIVGC-LGIGATVVLKP--KFSASQFWDDCQKHRVT-VFQYIGELCRYLVNQPPSKAECDHKVrLA 254
Cdd:PRK07786 220 FVGVPLFHIAG--IGSMLPgLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTgIFLVPAQWQAVCAEQQARPRDLALRV-LS 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 255 VGSGLRPDTwerFLRR----FGPLQILETYGMTEGNVATFNYTG-----RQGAVGRaswlykhIFPFSLIRY--DVMTGE 323
Cdd:PRK07786 297 WGAAPASDT---LLRQmaatFPEAQILAAFGQTEMSPVTCMLLGedairKLGSVGK-------VIPTVAARVvdENMNDV 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 324 PirnaqghcmttsPGEPGLLV--APVSQQspflGYAGAPELAkdkllKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGD 401
Cdd:PRK07786 367 P------------VGEVGEIVyrAPTLMS----GYWNNPEAT-----AEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKD 423
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755503902 402 TFRWKGENVATTEVAEVLETLDFLQEVNIYGVTvpgHE--GRAGMAALALRPPQA-LNLVQLYSHVSENLPPYARPRFL 477
Cdd:PRK07786 424 MIISGGENIYCAEVENVLASHPDIVEVAVIGRA---DEkwGEVPVAVAAVRNDDAaLTLEDLAEFLTDRLARYKHPKAL 499
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
141-477 3.25e-17

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 83.09  E-value: 3.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQCQ-GFYHLCGVHQEDVIYLALPLYHMSG-SLLGIVGCLGiGATVVLkPKFSASQFWDD 218
Cdd:cd17637    6 IHTAAVAGRPRGAVLSHGNLIAANlQLIHAMGLTEADVYLNMLPLFHIAGlNLALATFHAG-GANVVM-EKFDPAEALEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 219 CQKHRVTVFqyiGELcrylvnqPP---SKAECDHKVRLAVGSgLR-------PDTWERFLRRfGPLQILETYGMTE-GNV 287
Cdd:cd17637   84 IEEEKVTLM---GSF-------PPilsNLLDAAEKSGVDLSS-LRhvlgldaPETIQRFEET-TGATFWSLYGQTEtSGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFN-YTGRQGAVGRASwlykhifPFSLIRYDVMTGEPIRnaqghcmttsPGEPGLLVApvsqQSP--FLGYAGAPELAK 364
Cdd:cd17637  152 VTLSpYRERPGSAGRPG-------PLVRVRIVDDNDRPVP----------AGETGEIVV----RGPlvFQGYWNLPELTA 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWK--GENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRA 442
Cdd:cd17637  211 Y-----TFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDP-KWGEG 282
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 755503902 443 GMAALALRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd17637  283 IKAVCVLKPGATLTADELIEFVGSRIARYKKPRYV 317
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
136-477 4.00e-17

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 84.47  E-value: 4.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHLCgvhQEDVIYLALP----LYHMSGSLLG--IVGClgigATVVL 206
Cdd:cd05970  186 DILLVYFSSGTTGMPKMVEHDFtypLGHIVTAKYWQNV---REGGLHLTVAdtgwGKAVWGKIYGqwIAGA----AVFVY 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 K-PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDhKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMT 283
Cdd:cd05970  259 DyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLS-SLRYCTTAGeaLNPEVFNTFKEKTG-IKLMEGFGQT 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 284 EGNVATFNYTG---RQGAVGRASWLYkhifPFSLIRYD---VMTGEpirnaQGH-CMTTSPGEP-GLlvapvsqqspFLG 355
Cdd:cd05970  337 ETTLTIATFPWmepKPGSMGKPAPGY----EIDLIDREgrsCEAGE-----EGEiVIRTSKGKPvGL----------FGG 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTV 435
Cdd:cd05970  398 YYKDAEKTAE-----VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPD 470
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 755503902 436 PgHEGRAGMAALAL----RPPQALNlVQLYSHVSENLPPYARPRFL 477
Cdd:cd05970  471 P-IRGQVVKATIVLakgyEPSEELK-KELQDHVKKVTAPYKYPRIV 514
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
136-472 4.93e-17

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 82.91  E-value: 4.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHL-KVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL------KP 208
Cdd:cd05944    3 DVAAYFHTGGTTGTPKLAQHTHSnEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 209 KFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGN-V 287
Cdd:cd05944   83 PGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATG-LPVVEGYGLTEATcL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFNYTG---RQGAVGRAswlykhiFPFSLIRYDVMTGEPirNAQGHCmttSPGEpgllVAPVSQQSPflgyaGAPELAK 364
Cdd:cd05944  162 VAVNPPDgpkRPGSVGLR-------LPYARVRIKVLDGVG--RLLRDC---APDE----VGEICVAGP-----GVFGGYL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGM 444
Cdd:cd05944  221 YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDA-HAGELPV 299
                        330       340
                 ....*....|....*....|....*...
gi 755503902 445 AALALRPPQALNLVQLYSHVSENLPPYA 472
Cdd:cd05944  300 AYVQLKPGAVVEEEELLAWARDHVPERA 327
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
38-475 5.60e-17

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 84.17  E-value: 5.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  38 LACAR--PLCPPLYAEdpcCTASAAAVRVRSCWPQLgLPTLVEFLESLEP-DLPALRAMGLHLWATGPETNVA----GIS 110
Cdd:cd17634  127 LACARigAVHSVIFGG---FAPEAVAGRIIDSSSRL-LITADGGVRAGRSvPLKKNVDDALNPNVTSVEHVIVlkrtGSD 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 111 NLLSEAAD-----QVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISH--LKVLQCQGFYHLCGVHQEDVIYLALP 183
Cdd:cd17634  203 IDWQEGRDlwwrdLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVYAATTMKYVFDYGPGDIYWCTAD 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 184 LYHMSGSLLGIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE----CDHKVRLAV 255
Cdd:cd17634  283 VGWVTGHSYLLYGPLACGATTLLyegVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEgtdrSSLRILGSV 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 256 GSGLRPDTWERFLRRFGPLQ--ILETYGMTEgnVATFNYTGRQGAVGRASWlyKHIFPFSLIRYDVMtgepirNAQGHcm 333
Cdd:cd17634  363 GEPINPEAYEWYWKKIGKEKcpVVDTWWQTE--TGGFMITPLPGAIELKAG--SATRPVFGVQPAVV------DNEGH-- 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 334 TTSPGEPGLLVAPVSQQSPFLGYAGAPelakDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATT 413
Cdd:cd17634  431 PQPGGTEGNLVITDPWPGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTA 506
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 414 EVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALR----PPQALNlVQLYSHVSENLPPYARPR 475
Cdd:cd17634  507 EIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNhgvePSPELY-AELRNWVRKEIGPLATPD 570
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
112-395 1.32e-16

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 81.93  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  112 LLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIyLALPLYHMSGS 190
Cdd:TIGR01733 100 ELAALDDAPAPPPPDAPSGPD---DLAYVIYTSGSTGRPKGVVVTHRSLVNlLAWLARRYGLDPDDRV-LQFASLSFDAS 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  191 LLGIVGCLGIGATVVL------KPKFSASQFWDDcqKHRVTVFQ---YIGELCrylvnqPPSKAECDHKVRLAVGSG--L 259
Cdd:TIGR01733 176 VEEIFGALLAGATLVVppedeeRDDAALLAALIA--EHPVTVLNltpSLLALL------AAALPPALASLRLVILGGeaL 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  260 RPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWlykhifpfslirydVMTGEPIRNAQ-----GHCMT 334
Cdd:TIGR01733 248 TPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP--------------VPIGRPLANTRlyvldDDLRP 313
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902  335 TSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGD--VFFNTGDLLVCDEQGFLHF 395
Cdd:TIGR01733 314 VPVGVVGELY--IGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEF 374
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
136-434 2.76e-16

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 80.38  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH------LKVLQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:cd17635    2 DPLAVIFTSGTTGEPKAVLLANktffavPDILQKEGL----NWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRP-DTWERFLRRFGPLQILETYGMTEGNVA 288
Cdd:cd17635   78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSETGTA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFNYTGRQ----GAVGraswlykHIFP---FSLIRYDVMTGepIRNAQGHCMTTSPGEpgllvapvsqqspFLGYAGAPE 361
Cdd:cd17635  158 LCLPTDDDsieiNAVG-------RPYPgvdVYLAATDGIAG--PSASFGTIWIKSPAN-------------MLGYWNNPE 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902 362 LAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVT 434
Cdd:cd17635  216 RTAEVLI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIS 281
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
38-474 7.94e-16

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 80.32  E-value: 7.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  38 LACAR------PLCPPLYAEDPCCTASAAAVRVrscwpqlglpTLVEFLESLEPDLPALRAMGLHLWATGPETNVAGIsn 111
Cdd:PRK05852  86 LAASRadlvvvPLDPALPIAEQRVRSQAAGARV----------VLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGT-- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 112 lLSEAADQVDEPVPgYLSAPQNIM-DTCLYIFTSGTTGLPKAARISHLKVLQ-----CQGFyhlcGVHQEDVIYLALPLY 185
Cdd:PRK05852 154 -LSVHLDAATEPTP-ATSTPEGLRpDDAMIMFTGGTTGLPKMVPWTHANIASsvraiITGY----RLSPRDATVAVMPLY 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 186 HMSGSLLGIVGCLGIGATVVL--KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKA--ECDHKVRL--AVGSGL 259
Cdd:PRK05852 228 HGHGLIAALLATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPsgRKPAALRFirSCSAPL 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 260 RPDTWERFLRRFGPlQILETYGMTEG--NVATFNYTGRQ---------GAVGRAswlykhifpfslirydvmTGEPIRNA 328
Cdd:PRK05852 308 TAETAQALQTEFAA-PVVCAFGMTEAthQVTTTQIEGIGqtenpvvstGLVGRS------------------TGAQIRIV 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 329 QGHCMTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGE 408
Cdd:PRK05852 369 GSDGLPLPAGAVGEVW--LRGTTVVRGYLGDPTITAANFT-------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGE 439
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 409 NVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK05852 440 KISPERVEGVLASHPNVMEAAVFGVPDQLY-GEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIP 504
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
136-433 8.85e-16

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 80.25  E-value: 8.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH-------LKVLQCQGFYHlcGVHqEDVIYLaLPLYHMSGSLLGIVGCLGIGATVVLKP 208
Cdd:cd05923  151 QPAFVFYTSGTTGLPKGAVIPQraaesrvLFMSTQAGLRH--GRH-NVVLGL-MPLYHVIGFFAVLVAALALDGTYVVVE 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 209 KFSASQFWDDCQKHRVTVFQYIGELCRYLVN---QPPSKAECDHKVRLAvGSGLrPDTWERFLRRFGPLQILETYGMTEG 285
Cdd:cd05923  227 EFDPADALKLIEQERVTSLFATPTHLDALAAaaeFAGLKLSSLRHVTFA-GATM-PDAVLERVNQHLPGEKVNIYGTTEA 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVATFNYTGRQGAVGRASWlykhifpFSLIRYDVMTGEPIRNAqghcmttSPGEPGLLVAPVSQQSPFLGYAGAPELAKD 365
Cdd:cd05923  305 MNSLYMRDARTGTEMRPGF-------FSEVRIVRIGGSPDEAL-------ANGEEGELIVAAAADAAFTGYLNQPEATAK 370
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 366 KLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:cd05923  371 KLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV 431
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
142-479 2.01e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 79.05  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHLKVLQCQGFY-HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSASQFWDDC 219
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNILNNGYFVaESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAV 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 220 QKHRVTVFQ-----YIGELcrylvnQPPSKAECD-HKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFN 291
Cdd:PRK12583 288 EEERCTALYgvptmFIAEL------DHPQRGNFDlSSLRTGImaGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQ 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTG------RQGAVGRaswlykhifpfSLIRYDVmtgePIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKD 365
Cdd:PRK12583 362 TTAaddlerRVETVGR-----------TQPHLEV----KVVDPDGA--TVPRGEIGELC--TRGYSVMKGYWNNPEATAE 422
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 366 KLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMA 445
Cdd:PRK12583 423 SI------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY-GEEIVA 495
                        330       340       350
                 ....*....|....*....|....*....|....
gi 755503902 446 ALALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:PRK12583 496 WVRLHPGHAASEEELREFCKARIAHFKVPRYFRF 529
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
136-398 2.02e-15

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 79.97  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMsgslLGIVG------CLGIGATVVLKP 208
Cdd:PRK08633  783 DTATIIFSSGSEGEPKGVMLSHHNILsNIEQISDVFNLRNDDVILSSLPFFHS----FGLTVtlwlplLEGIKVVYHPDP 858
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  209 kFSASQFWDDCQKHRVTVFQYIGELCR-YLVNQPPSKAECDhKVRLAVgSG---LRPDTWERFLRRFGpLQILETYGMTE 284
Cdd:PRK08633  859 -TDALGIAKLVAKHRATILLGTPTFLRlYLRNKKLHPLMFA-SLRLVV-AGaekLKPEVADAFEEKFG-IRILEGYGATE 934
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  285 GN-VATFN-----------YTG-RQGAVGRAswlykhiFPFSLIR-YDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQ 350
Cdd:PRK08633  935 TSpVASVNlpdvlaadfkrQTGsKEGSVGMP-------LPGVAVRiVDPETFEEL----------PPGEDGLIL--IGGP 995
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 755503902  351 SPFLGYAGAPELAKdKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDR 398
Cdd:PRK08633  996 QVMKGYLGDPEKTA-EVIKDIDGIG--WYVTGDKGHLDEDGFLTITDR 1040
PRK13382 PRK13382
bile acid CoA ligase;
141-475 2.04e-15

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 79.03  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKvlqcqGFYHLCGV------HQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:PRK13382 202 LLTSGTTGTPKGARRSGPG-----GIGTLKAIldrtpwRAEEPTVIVAPMFHAWG-FSQLVLAASLACTIVTRRRFDPEA 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPP---SKAECDH-KVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTE-GNVAT 289
Cdd:PRK13382 276 TLDLIDRHRATGLAVVPVMFDRIMDLPAevrNRYSGRSlRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEaGMIAT 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTGRQGA---VGRASwlykhifpfslirydvmTGEPIRNAQGHCMTTSPGEPGLLVapVSQQSPFLGYagAPELAKDk 366
Cdd:PRK13382 355 ATPADLRAApdtAGRPA-----------------EGTEIRILDQDFREVPTGEVGTIF--VRNDTQFDGY--TSGSTKD- 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 llkdvFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAA 446
Cdd:PRK13382 413 -----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQY-GQRLAAF 484
                        330       340
                 ....*....|....*....|....*....
gi 755503902 447 LALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK13382 485 VVLKPGASATPETLKQHVRDNLANYKVPR 513
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
128-474 6.05e-15

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 77.10  E-value: 6.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  128 LSAPQNIMDTCLYIFTSGTTGLPKAARISH-------LKVLQCQGFYhlcgvhQEDVIYLALPLYHMSGslLGIV-GCLG 199
Cdd:TIGR01923 104 LSASFNMDQIATLMFTSGTTGKPKAVPHTFrnhyasaVGSKENLGFT------EDDNWLLSLPLYHISG--LSILfRWLI 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  200 IGATVVLKPKFSasQFWDDCQKHRVTVFQYI-GELCRYLvnQPPSKAECDHKVRLavGSGLRPDTWERFLRRFGpLQILE 278
Cdd:TIGR01923 176 EGATLRIVDKFN--QLLEMIANERVTHISLVpTQLNRLL--DEGGHNENLRKILL--GGSAIPAPLIEEAQQYG-LPIYL 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  279 TYGMTE--GNVATFN--YTGRQGAVGRASwlykhifPFSLIRYDVmtgePIRNAQGHCMTTSPGepgllvapvsqqsPFL 354
Cdd:TIGR01923 249 SYGMTEtcSQVTTATpeMLHARPDVGRPL-------AGREIKIKV----DNKEGHGEIMVKGAN-------------LMK 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  355 GYAGAPELAkdKLLKDVFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniygVT 434
Cdd:TIGR01923 305 GYLYQGELT--PAFEQQGW-----FNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEA----VV 373
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 755503902  435 VPGHEGRAGMAALA-LRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:TIGR01923 374 VPKPDAEWGQVPVAyIVSESDISQAKLIAYLTEKLAKYKVP 414
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
82-419 1.69e-14

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 76.32  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  82 SLEPDLPALRAMGLhLWATGPETNVAGISNLLSEAadqvdEPvpgyLSAPQNIM--DTCLYIFTSGTTGLPKAARISHLK 159
Cdd:PRK06087 142 PLQNQLPQLQQIVG-VDKLAPATSSLSLSQIIADY-----EP----LTTAITTHgdELAAVLFTSGTEGLPKGVMLTHNN 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 160 VLQCQGFYhLCGVH--QEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVT----VFQYIGEL 233
Cdd:PRK06087 212 ILASERAY-CARLNltWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcmlgATPFIYDL 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 234 CRYLVNQPPSKAECdhKVRLAVGSGLRPDTWERFLRRfgPLQILETYGMTEGNVATF----NYTGRQGAV-GRAswlykh 308
Cdd:PRK06087 291 LNLLEKQPADLSAL--RFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSPHAVvnldDPLSRFMHTdGYA------ 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 309 ifpfslirydvMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQspFLGYAGAPELAkDKLLKDVFWsgdvfFNTGDLLVCD 388
Cdd:PRK06087 361 -----------AAGVEIKVVDEARKTLPPGCEGEEASRGPNV--FMGYLDEPELT-ARALDEEGW-----YYSGDLCRMD 421
                        330       340       350
                 ....*....|....*....|....*....|.
gi 755503902 389 EQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK06087 422 EAGYIKITGRKKDIIVRGGENISSREVEDIL 452
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
142-480 1.81e-14

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 76.07  E-value: 1.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQE--DVIYLALPLYHM----SGSL--LGIVGClgigATVVLKPK 209
Cdd:PRK08751 215 YTGGTTGVAKGAMLTHrnlvANMQQAHQWLAGTGKLEEgcEVVITALPLYHIfaltANGLvfMKIGGC----NHLISNPR 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 fSASQFWDDCQKHRVTVFQYIGELCRYLVNQPpSKAECDH---KVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGN 286
Cdd:PRK08751 291 -DMPGFVKELKKTRFTAFTGVNTLFNGLLNTP-GFDQIDFsslKMTLGGGMAVQRSVAERWKQVTG-LTLVEAYGLTETS 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 VATFnytgrqgavgraswlykhIFPFSLIRYDVMTGEPI-------RNAQGHCMTTspGEPGLLVAPVSQQspFLGYAGA 359
Cdd:PRK08751 368 PAAC------------------INPLTLKEYNGSIGLPIpstdaciKDDAGTVLAI--GEIGELCIKGPQV--MKGYWKR 425
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 360 PELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE 439
Cdd:PRK08751 426 PEETAKVM------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG--VPDEK 497
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 755503902 440 GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:PRK08751 498 SGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFR 538
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
128-476 3.24e-14

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 75.16  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 128 LSAPQNImdtcLY-IFTSGTTGLPKAARISHLKVLQcqgfyHLCGVHQEdvIYLALPLYHMSGSLLG-------IVGCLG 199
Cdd:cd17644  102 LTQPENL----AYvIYTSGSTGKPKGVMIEHQSLVN-----LSHGLIKE--YGITSSDRVLQFASIAfdvaaeeIYVTLL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 200 IGATVVLKPK---FSASQFWDDCQKHRVTVFQYIGELCRYLVNQ-PPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGP 273
Cdd:cd17644  171 SGATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLElLLSTIDLPSSLRLVIvgGEAVQPELVRQWQKNVGN 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 L-QILETYGMTEGNVATFnytgrqgavgraswLYKHIFPFSLIRYDVMTGEPIRNAQGHCM-----TTSPGEPG-LLVAP 346
Cdd:cd17644  251 FiQLINVYGPTEATIAAT--------------VCRLTQLTERNITSVPIGRPIANTQVYILdenlqPVPVGVPGeLHIGG 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 347 VSQQSpflGYAGAPELAKDKLLKDVFWS--GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:cd17644  317 VGLAR---GYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHND 393
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 425 LQEvniygVTVPGHEGRAG----MAALALRPPQALNLVQLYSHVSENLPPYARPRF 476
Cdd:cd17644  394 VKT-----AVVIVREDQPGnkrlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSA 444
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
136-411 6.29e-14

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 74.75  E-value: 6.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGiVGCLGIGATVVlkpkFSAS- 213
Cdd:COG1022  184 DLATIIYTSGTTGRPKGVMLTHRNLLsNARALLERLPLGPGDRTLSFLPLAHVFERTVS-YYALAAGATVA----FAESp 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 -QFWDDCQKHRVTVF-------------------------------------QYIgelCRYLVNQPPSKAE------CD- 248
Cdd:COG1022  259 dTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkrklfrwalavgrRYA---RARLAGKSPSLLLrlkhalADk 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 249 ---HKVRLAVG-------SG---LRPDTwERFLRRFGpLQILETYGMTE-GNVATFNYTGRQ--GAVGRAswlykhiFPF 312
Cdd:COG1022  336 lvfSKLREALGgrlrfavSGgaaLGPEL-ARFFRALG-IPVLEGYGLTEtSPVITVNRPGDNriGTVGPP-------LPG 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 313 SLIRydvmtgepIrnaqghcmttspGEPG-LLVapvsqQSP--FLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDE 389
Cdd:COG1022  407 VEVK--------I------------AEDGeILV-----RGPnvMKGYYKNPEATAEAFDAD----G--WLHTGDIGELDE 455
                        330       340
                 ....*....|....*....|....*
gi 755503902 390 QGFLHFHDRTGDTFrwK---GENVA 411
Cdd:COG1022  456 DGFLRITGRKKDLI--VtsgGKNVA 478
PRK09088 PRK09088
acyl-CoA synthetase; Validated
139-479 6.73e-14

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 74.07  E-value: 6.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWD 217
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQtAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 218 DCQKHRVTVFQYIG--ELCRYLVNQPP-SKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE-GNVATFNY- 292
Cdd:PRK09088 219 RLGDPALGITHYFCvpQMAQAFRAQPGfDAAALRHLTALFTGGAPHAAEDILGWLDDG-IPMVDGFGMSEaGTVFGMSVd 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 ----TGRQGAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPG--LLVAPvsqqSPFLGYAGAPELAKDK 366
Cdd:PRK09088 298 cdviRAKAGAAGIPT-------PTVQTR--------VVDDQGN--DCPAGVPGelLLRGP----NLSPGYWRRPQATARA 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAA 446
Cdd:PRK09088 357 F------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADA-QWGEVGYLA 429
                        330       340       350
                 ....*....|....*....|....*....|...
gi 755503902 447 LALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:PRK09088 430 IVPADGAPLDLERIRSHLSTRLAKYKVPKHLRL 462
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
130-480 8.25e-14

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 73.96  E-value: 8.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 130 APQNImdtclyIFTSGTTGLPKAARISHLKVLQCQGF----YHLCGVHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVV 205
Cdd:PRK12406 153 QPQSM------IYTSGTTGHPKGVRRAAPTPEQAAAAeqmrALIYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLV 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 206 LKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPskaecdhKVRLAVG-SGLR----------PDTWERFLRRFGPL 274
Cdd:PRK12406 226 LQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPE-------EVRAKYDvSSLRhvihaaapcpADVKRAMIEWWGPV 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 275 qILETYGMTEGNVATF----NYTGRQGAVGRASwlykhifPFSLIRYDVMTGEPIrnaqghcmttSPGEPGLLVAPVSQQ 350
Cdd:PRK12406 299 -IYEYYGSTESGAVTFatseDALSHPGTVGKAA-------PGAELRFVDEDGRPL----------PQGEIGEIYSRIAGN 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 351 SPFLgYAGAPElAKDKLLKDVF-WSGDVffntGDLlvcDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVN 429
Cdd:PRK12406 361 PDFT-YHNKPE-KRAEIDRGGFiTSGDV----GYL---DADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCA 431
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755503902 430 IYGvtVPGHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:PRK12406 432 VFG--IPDAEfGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIM 481
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
84-398 8.37e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 74.23  E-value: 8.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  84 EPDLPALRAMGLHLWatgpetnvagisnllSEAADQVDEPvPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVL-Q 162
Cdd:PRK08314 158 EPPLQALAPGGVVAW---------------KEALAAGLAP-PPHTAGPD---DLAVLPYTSGTTGVPKGCMHTHRTVMaN 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 163 CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKfsasqfWD-----DC-QKHRVTVFQYIGELCRY 236
Cdd:PRK08314 219 AVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR------WDreaaaRLiERYRVTHWTNIPTMVVD 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 237 LVNQPPSKAECDHKVRLAVGSGLR-PD-TWERFLRRFGpLQILETYGMTE------GN-----------VATFNYTGRqg 297
Cdd:PRK08314 293 FLASPGLAERDLSSLRYIGGGGAAmPEaVAERLKELTG-LDYVEGYGLTEtmaqthSNppdrpklqclgIPTFGVDAR-- 369
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 298 avgraswlykhifpfsLIryDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKdvfWSGDV 377
Cdd:PRK08314 370 ----------------VI--DPETLEEL----------PPGEVGEIV--VHGPQVFKGYWNRPEATAEAFIE---IDGKR 416
                        330       340
                 ....*....|....*....|.
gi 755503902 378 FFNTGDLLVCDEQGFLHFHDR 398
Cdd:PRK08314 417 FFRTGDLGRMDEEGYFFITDR 437
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
141-475 9.38e-14

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 73.44  E-value: 9.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQcqgFY-HLCG---VHQEDVIyLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSAS 213
Cdd:cd05945  103 IFTSGSTGRPKGVQISHDNLVS---FTnWMLSdfpLGPGDVF-LNQAPFSFDLSVMDLYPALASGATLVPVPRdatADPK 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVF---QYIGELCR----YLVNQPPSkaecdhkVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:cd05945  179 QLFRFLAEHGITVWvstPSFAAMCLlsptFTPESLPS-------LRHFLFCGevLPHKTARALQQRFPDARIYNTYGPTE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 GNVATfnytgrqgavgraswLYKHIFPFSLIRYDVMT-GEP-------IRNAQGHCMttSPGEPGLLVapVSQQSPFLGY 356
Cdd:cd05945  252 ATVAV---------------TYIEVTPEVLDGYDRLPiGYAkpgaklvILDEDGRPV--PPGEKGELV--ISGPSVSKGY 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLKDvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVP 436
Cdd:cd05945  313 LNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKY 387
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 755503902 437 GHEGRAGMAA-LALRPP-QALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05945  388 KGEKVTELIAfVVPKPGaEAGLTKAIKAELAERLPPYMIPR 428
PRK07638 PRK07638
acyl-CoA synthetase; Validated
118-475 1.06e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 73.66  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 118 DQVDEPVPGYLSAP---QNIMDTCLYI-FTSGTTGLPKA---ARISHLKVLQCQGfyHLCGVHQEDVIYLALPLYHmSGS 190
Cdd:PRK07638 122 DEWKRMIEKYLPTYapiENVQNAPFYMgFTSGSTGKPKAflrAQQSWLHSFDCNV--HDFHMKREDSVLIAGTLVH-SLF 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 191 LLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQppsKAECDHKVRLaVGSGLRpdtW-----E 265
Cdd:PRK07638 199 LYGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKE---NRVIENKMKI-ISSGAK---WeaeakE 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 266 RFLRRFGPLQILETYGMTEGNVATF----NYTGRQGAVGRaswlykhifPFSLIRYDvmtgepIRNAQGHcmTTSPGEPG 341
Cdd:PRK07638 272 KIKNIFPYAKLYEFYGASELSFVTAlvdeESERRPNSVGR---------PFHNVQVR------ICNEAGE--EVQKGEIG 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 342 LLVApvsqQSP--FLGYAGAPELAKDklLKDVFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK07638 335 TVYV----KSPqfFMGYIIGGVLARE--LNADGW-----MTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVL 403
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 420 ETLDFLQEVNIYGVTVPghegRAGMAALALRPPQAlNLVQLYSHVSENLPPYARPR 475
Cdd:PRK07638 404 HEHPAVDEIVVIGVPDS----YWGEKPVAIIKGSA-TKQQLKSFCLQRLSSFKIPK 454
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
73-475 1.50e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 73.01  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  73 LPTLVEFLESLEPDLPALRAMGlhlwatGPETNVAGISNLLSEAADQ-VDEPVPGYLsapqniMdtcLYifTSGTTGLPK 151
Cdd:PRK08276  94 ADTAAELAAELPAGVPLLLVVA------GPVPGFRSYEEALAAQPDTpIADETAGAD------M---LY--SSGTTGRPK 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 AAR--ISHLKVLQCQG------FYHLCGVhqEDVIYLA-LPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKH 222
Cdd:PRK08276 157 GIKrpLPGLDPDEAPGmmlallGFGMYGG--PDSVYLSpAPLYH-TAPLRFGMSALALGGTVVVMEKFDAEEALALIERY 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 223 RVTVFQYIGELCRYLVNQPPS-KAECD---HKVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTEGNVATF----NYTG 294
Cdd:PRK08276 234 RVTHSQLVPTMFVRMLKLPEEvRARYDvssLRVAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEGGGVTVitseDWLA 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 295 RQGAVGRAsWLYK-HIFPfslirydvMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKllkdvfW 373
Cdd:PRK08276 313 HPGSVGKA-VLGEvRILD--------EDGNEL----------PPGEIGTVY--FEMDGYPFEYHNDPEKTAAA------R 365
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 374 SGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV--------------TVPGHE 439
Cdd:PRK08276 366 NPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpdeemgervkavvqPADGAD 445
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 755503902 440 GRAGMAAlalrppqalnlvQLYSHVSENLPPYARPR 475
Cdd:PRK08276 446 AGDALAA------------ELIAWLRGRLAHYKCPR 469
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
131-475 1.80e-13

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 72.97  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 131 PQNIMDTCLYIFTSGTTGLPKAARIShlkvlQCQGFYHlcGVHQ--------EDVIYLALPLYHMSGSLLGIVGCLGIGA 202
Cdd:PRK06839 145 EKNESASFIICYTSGTTGKPKGAVLT-----QENMFWN--ALNNtfaidltmHDRSIVLLPLFHIGGIGLFAFPTLFAGG 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 203 TVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG------LRPDTWERFLrRFGplqi 276
Cdd:PRK06839 218 VIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpeeLMREFIDRGF-LFG---- 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 lETYGMTEGNVATF-----NYTGRQGAVGRaswlykhifPFSLIRYDVmtgepIRNAQGHcmtTSPGEPGLLVapVSQQS 351
Cdd:PRK06839 293 -QGFGMTETSPTVFmlseeDARRKVGSIGK---------PVLFCDYEL-----IDENKNK---VEVGEVGELL--IRGPN 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 352 PFLGYAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIY 431
Cdd:PRK06839 353 VMKEYWNRPDATEETI-------QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVV 425
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 755503902 432 GVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK06839 426 GRQHV-KWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK 468
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
136-477 1.92e-13

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 72.50  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHlkvlqcQGFYHLcgVHQEDVIY--LALPLYHMSGSLLGI-------VGCLGIGATVVL 206
Cdd:cd17650   94 DLAYVIYTSGTTGKPKGVMVEH------RNVAHA--AHAWRREYelDSFPVRLLQMASFSFdvfagdfARSLLNGGTLVI 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 KP---KFSASQFWDDCQKHRVTVFQYIGELCRYLVnqppskAECD-HKVR------LAVGSGLRPDTWERFL-RRFGP-L 274
Cdd:cd17650  166 CPdevKLDPAALYDLILKSRITLMESTPALIRPVM------AYVYrNGLDlsamrlLIVGSDGCKAQDFKTLaARFGQgM 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 275 QILETYGMTEGNVATFNYTGRQGAVGRASwlykhifpfsliryDVMTGEPIRNAQGHCMTTS----P----GEPGLLVAP 346
Cdd:cd17650  240 RIINSYGVTEATIDSTYYEEGRDPLGDSA--------------NVPIGRPLPNTAMYVLDERlqpqPvgvaGELYIGGAG 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 347 VSQqspflGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQ 426
Cdd:cd17650  306 VAR-----GYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQL-----AR 375
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755503902 427 EVNIYGVTVPGHEGRAGMAALA--LRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd17650  376 HPAIDEAVVAVREDKGGEARLCayVVAAATLNTAELRAFLAKELPSYMIPSYY 428
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
136-475 2.16e-13

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 72.53  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ--CQGFYHLcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSA 212
Cdd:cd05969   90 DPTLLHYTSGTTGTPKGVLHVHDAMIFyyFTGKYVL-DLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVyEGRFDA 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVF----QYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE-GNV 287
Cdd:cd05969  169 ESWYGIIERVKVTVWytapTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTEtGSI 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFNYTG---RQGAVGRaswlykhifPFSLIRYDVMT--GEPIRnaqghcmttsPGEPGLLVAPVSQQSPFLGYAGAPEl 362
Cdd:cd05969  248 MIANYPCmpiKPGSMGK---------PLPGVKAAVVDenGNELP----------PGTKGILALKPGWPSMFRGIWNDEE- 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 akdkLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRA 442
Cdd:cd05969  308 ----RYKNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP-LRGEI 380
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 755503902 443 GMAALALR----PPQALNlVQLYSHVSENLPPYARPR 475
Cdd:cd05969  381 IKAFISLKegfePSDELK-EEIINFVRQKLGAHVAPR 416
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
136-475 2.26e-13

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 72.56  E-value: 2.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVlqCQGFYH------LCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPK 209
Cdd:cd17642  185 QVALIMNSSGSTGLPKGVQLTHKNI--VARFSHardpifGNQIIPDTAILTVIPFHHGFG-MFTTLGYLICGFRVVLMYK 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKVRLAVGSG-LRPDTWERFLRRFGPLQILETYGMTEGNV 287
Cdd:cd17642  262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTS 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 A---TFNYTGRQGAVGRaswlykhIFPFSLIRY-DVMTGEpirnaqghcmTTSPGEPGLLVApvsqQSPFL--GYAGAPE 361
Cdd:cd17642  342 AiliTPEGDDKPGAVGK-------VVPFFYAKVvDLDTGK----------TLGPNERGELCV----KGPMImkGYVNNPE 400
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 LAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGR 441
Cdd:cd17642  401 ATKALIDKD-GW-----LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDE-DAGE 473
                        330       340       350
                 ....*....|....*....|....*....|....
gi 755503902 442 AGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd17642  474 LPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLR 507
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
127-480 2.49e-13

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 71.96  E-value: 2.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 127 YLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHL---CGVHQEDVIYLALPLyhmSGSLLGIVGCLGIGAT 203
Cdd:cd17653  100 TTDSPD---DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPArldVGPGSRVAQVLSIAF---DACIGEIFSTLCNGGT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 204 VVLK-PKFSASQFWDDC----------QKHRVTVFQYIGELcrYLVNQPPSKAecdhkvrLAvgsglrpDTWeRFLRRFg 272
Cdd:cd17653  174 LVLAdPSDPFAHVARTVdalmstpsilSTLSPQDFPNLKTI--FLGGEAVPPS-------LL-------DRW-SPGRRL- 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 273 plqiLETYGMTEGNVATfnytgrqgavgraswLYKHIFPfsliRYDVMTGEPIRNA-----QGHCMTTSPGEPGLLVapV 347
Cdd:cd17653  236 ----YNAYGPTECTISS---------------TMTELLP----GQPVTIGKPIPNStcyilDADLQPVPEGVVGEIC--I 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 348 SQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDflQE 427
Cdd:cd17653  291 SGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQ--PE 368
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755503902 428 VNIYGVTVpgHEGRagmaALALRPPQALNLVQLYSHVSENLPPYARP-RFLRLQ 480
Cdd:cd17653  369 VTQAAAIV--VNGR----LVAFVTPETVDVDGLRSELAKHLPSYAVPdRIIALD 416
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
122-437 3.37e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 72.14  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 122 EPVPGYLSAPQNIMDTClyiFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMsGSLLGIVGCLGI 200
Cdd:PLN02860 162 TTELDYAWAPDDAVLIC---FTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCHI-GGLSSALAMLMV 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 201 GATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKA--ECDHKVR--LAVGSGLRPDTWERFLRRFGPLQI 276
Cdd:PLN02860 238 GACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMtwKVFPSVRkiLNGGGSLSSRLLPDAKKLFPNAKL 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 LETYGMTEG-NVATFN--YTGRQGAVGRASWLYKHIFPFSLIRYD-VMTGEPIRNAQ-GHCMTTSPGEPGLLVapvsqQS 351
Cdd:PLN02860 318 FSAYGMTEAcSSLTFMtlHDPTLESPKQTLQTVNQTKSSSVHQPQgVCVGKPAPHVElKIGLDESSRVGRILT-----RG 392
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 352 P--FLGYAG-APELAKDKllkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQEV 428
Cdd:PLN02860 393 PhvMLGYWGqNSETASVL-------SNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVL-----SQHP 460

                 ....*....
gi 755503902 429 NIYGVTVPG 437
Cdd:PLN02860 461 GVASVVVVG 469
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
117-479 3.64e-13

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 72.14  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 117 ADQVDEPVPGYlsAPQNIMDTCLYIFTSGTTGLPKAARISH----LKVlqCQGFYHLCGVHQEDVIYLALPLYHMSGSLL 192
Cdd:cd05968  220 DEEKETAGDGA--ERTESEDPLMIIYTSGTTGKPKGTVHVHagfpLKA--AQDMYFQFDLKPGDLLTWFTDLGWMMGPWL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 193 gIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFQYIGELCRYLV--NQPPSKAECDHKVRLAVGSG--LRPDTW 264
Cdd:cd05968  296 -IFGGLILGATMVLydgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGepWNPEPW 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 265 ERFLRRFGplqiletygmtEGNVATFNYTG----RQGAVGraSWLYKHIFPFSL------IRYDVM--TGEPIRNAQGHC 332
Cdd:cd05968  375 NWLFETVG-----------KGRNPIINYSGgteiSGGILG--NVLIKPIKPSSFngpvpgMKADVLdeSGKPARPEVGEL 441
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 333 MTTSPGePGLlvapvsqQSPFLGyagapelaKDKLLKDVFWSG-DVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVA 411
Cdd:cd05968  442 VLLAPW-PGM-------TRGFWR--------DEDRYLETYWSRfDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVG 505
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755503902 412 TTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRP---PQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05968  506 PAEIESVLNAHPAVLESAAIGVPHP-VKGEAIVCFVVLKPgvtPTEALAEELMERVADELGKPLSPERILF 575
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
142-477 6.83e-13

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 71.20  E-value: 6.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFY---HLCGVHQEDVIYL-ALPLYHMSGslLGIVGCLGI--GATVVLKPK-F 210
Cdd:PRK07059 211 YTGGTTGVSKGATLLHrnivANVLQMEAWLqpaFEKKPRPDQLNFVcALPLYHIFA--LTVCGLLGMrtGGRNILIPNpR 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 211 SASQFWDDCQKHRVTVFQYIGELCRYLVNQPP-SKAECDhKVRLAVGSGL---RPdTWERFLRRFGpLQILETYGMTEGN 286
Cdd:PRK07059 289 DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDfDKLDFS-KLIVANGGGMavqRP-VAERWLEMTG-CPITEGYGLSETS 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 -VATFNytgrqgavgraswlykhifPFSLIRYDVMTGEP-------IRNAQGHCMttSPGEPGLLVAPVSQQSPflGYAG 358
Cdd:PRK07059 366 pVATCN-------------------PVDATEFSGTIGLPlpstevsIRDDDGNDL--PLGEPGEICIRGPQVMA--GYWN 422
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 359 AP-ELAKdkllkdvFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPg 437
Cdd:PRK07059 423 RPdETAK-------VMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDE- 494
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 755503902 438 HEGRAgMAALALRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:PRK07059 495 HSGEA-VKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFV 533
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
141-479 7.91e-13

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 70.80  E-value: 7.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQ----CQgfyHLCGVHQEDVIYlalpLYHMSG---SLLGIVGCLGIGATVVLKPKF--- 210
Cdd:cd17643   99 IYTSGSTGRPKGVVVSHANVLAlfaaTQ---RWFGFNEDDVWT----LFHSYAfdfSVWEIWGALLHGGRLVVVPYEvar 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 211 SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPL--QILETYGMTEGN 286
Cdd:cd17643  172 SPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDrpQLVNMYGITETT 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 V-ATFNYTGRQGAVGRASwlykhifpfSLIrydvmtGEPIRNAQGHCMTTS-----PGEPGLLVAPVSQQSPflGYAGAP 360
Cdd:cd17643  252 VhVTFRPLDAADLPAAAA---------SPI------GRPLPGLRVYVLDADgrpvpPGVVGELYVSGAGVAR--GYLGRP 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 361 ELAKDKLLKDVFWS-GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVTVpgHE 439
Cdd:cd17643  315 ELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDA---AVIV--RE 389
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 755503902 440 GRAG----MAALALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd17643  390 DEPGdtrlVAYVVADDGAAADIAELRALLKELLPDYMVPaRYVPL 434
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
136-477 1.18e-12

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 70.15  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAA------RISHLKVLQcqgFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL--K 207
Cdd:cd05971   89 DPALIIYTSGTTGPPKGAlhahrvLLGHLPGVQ---FPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrM 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 208 PKFSASQFWDDCQKHRVT-VFQYIGELcRYLVNQPPSKAECDHKVRlAVGSGLRPD-----TWERflRRFGpLQILETYG 281
Cdd:cd05971  166 TKFDPKAALDLMSRYGVTtAFLPPTAL-KMMRQQGEQLKHAQVKLR-AIATGGESLgeellGWAR--EQFG-VEVNEFYG 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTEGNVATFN----YTGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGhcMTTSPGEPGLLVAPVSQQSPFLGYA 357
Cdd:cd05971  241 QTECNLVIGNcsalFPIKPGSMGKP-------IPGHRVA--------IVDDNG--TPLPPGEVGEIAVELPDPVAFLGYW 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 358 GAPELAKDKLLKDvfwsgdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPg 437
Cdd:cd05971  304 NNPSATEKKMAGD-------WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP- 375
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 755503902 438 HEGRAGMAALALRP----PQALNlVQLYSHVSENLPPYARPRFL 477
Cdd:cd05971  376 IRGEIVKAFVVLNPgetpSDALA-REIQELVKTRLAAHEYPREI 418
PLN02574 PLN02574
4-coumarate--CoA ligase-like
136-475 1.92e-12

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 69.87  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQE----DVIYLA-LPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIaMVELFVRFEASQYEypgsDNVYLAaLPMFHIYGLSLFVVGLLSLGSTIVVMRR 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKVRLaVGSGLRP---DTWERFLRRFGPLQILETYGMTEG 285
Cdd:PLN02574 279 FDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQ-VSCGAAPlsgKFIQDFVQTLPHVDFIQGYGMTES 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NvatfnytgrqgAVGRASWLYKHIFPFSLIRYDV--MTGEPIRNAQGHCMttSPGEPGLLVApvsqQSPFL--GYAGAPE 361
Cdd:PLN02574 358 T-----------AVGTRGFNTEKLSKYSSVGLLApnMQAKVVDWSTGCLL--PPGNCGELWI----QGPGVmkGYLNNPK 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 LAKDKLLKDVfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-G 440
Cdd:PLN02574 421 ATQSTIDKDG-W-----LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA--VPDKEcG 492
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 755503902 441 RAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PLN02574 493 EIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVR 527
PRK07787 PRK07787
acyl-CoA synthetase; Validated
137-479 2.02e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 69.25  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 137 TCLYIFTSGTTGLPKAARISHLKVLQC-QGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQF 215
Cdd:PRK07787 130 PALIVYTSGTTGPPKGVVLSRRAIAADlDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDDCQKHRV------TVFQYIGElcrylvnqPPSKAECDHKVRLAV-GSGLRPDT-WERFLRRFGpLQILETYGMTEG-- 285
Cdd:PRK07787 210 AQALSEGGTlyfgvpTVWSRIAA--------DPEAARALRGARLLVsGSAALPVPvFDRLAALTG-HRPVERYGMTETli 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVAT-FNYTGRQGAVGRAswlykhiFPFSLIRYDVMTGEPIrnaqghcmtTSPGEPgllVAPVSQQSP--FLGYAGAPEL 362
Cdd:PRK07787 281 TLSTrADGERRPGWVGLP-------LAGVETRLVDEDGGPV---------PHDGET---VGELQVRGPtlFDGYLNRPDA 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 AKDKllkdvfWSGDVFFNTGDLLVCDEQGFLHFHDRTG-DTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGR 441
Cdd:PRK07787 342 TAAA------FTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQR 415
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 755503902 442 AGMAALALRPPQALNLVQlysHVSENLPPYARPRFLRL 479
Cdd:PRK07787 416 IVAYVVGADDVAADELID---FVAQQLSVHKRPREVRF 450
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
81-475 2.17e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 69.33  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  81 ESLEPDLPALRamgLHLWATGPETnVAGISNLLSEAADQVDEPVPGylsapQNIMDTCLYifTSGTTGLPKAAR--ISHL 158
Cdd:PRK13391 111 RALLKQCPGVR---HRLVLDGDGE-LEGFVGYAEAVAGLPATPIAD-----ESLGTDMLY--SSGTTGRPKGIKrpLPEQ 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 159 KVLQCQGFYHLCGV---HQEDVIYLA-LPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELC 234
Cdd:PRK13391 180 PPDTPLPLTAFLQRlwgFRSDMVYLSpAPLYH-SAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMF 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 235 RYLVNQPpskaecdHKVRLAVG-SGLR----------PDTWERFLRRFGPLqILETYGMTEGNVATF----NYTGRQGAV 299
Cdd:PRK13391 259 SRMLKLP-------EEVRDKYDlSSLEvaihaaapcpPQVKEQMIDWWGPI-IHEYYAATEGLGFTAcdseEWLAHPGTV 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 300 GRAswlykhifpfslirydvMTGEP-IRNAQGHCMttSPGEPGLLVapVSQQSPFlGYAGAPELAKDKLLKDVFWSgdvf 378
Cdd:PRK13391 331 GRA-----------------MFGDLhILDDDGAEL--PPGEPGTIW--FEGGRPF-EYLNDPAKTAEARHPDGTWS---- 384
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 379 fNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETL--------------DFLQEVNIYGVTVPGHEGRAGM 444
Cdd:PRK13391 385 -TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHpkvadaavfgvpneDLGEEVKAVVQPVDGVDPGPAL 463
                        410       420       430
                 ....*....|....*....|....*....|.
gi 755503902 445 AAlalrppqalnlvQLYSHVSENLPPYARPR 475
Cdd:PRK13391 464 AA------------ELIAFCRQRLSRQKCPR 482
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
136-475 2.27e-12

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 69.08  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARIShLKVLQCQGFY--HLCGVHQEDVIY-LALP-----LYHmsgsllGIVGCLGIG-ATVVL 206
Cdd:cd05973   89 DPFVMMFTSGTTGLPKGVPVP-LRALAAFGAYlrDAVDLRPEDSFWnAADPgwaygLYY------AITGPLALGhPTILL 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSkAECDHKVRLAV----GSGLRPDTWERFLRRFGpLQILETYGM 282
Cdd:cd05973  162 EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRvssaGEPLTPEVIRWFDAALG-VPIHDHYGQ 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 283 TEGNVATFNYTG-----RQGAVGRAswlykhiFP-FSLIRYDVMTGEPirnaqghcmttSPGEPGLLVAPVSQqSP---F 353
Cdd:cd05973  240 TELGMVLANHHAlehpvHAGSAGRA-------MPgWRVAVLDDDGDEL-----------GPGEPGRLAIDIAN-SPlmwF 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 354 LGYAGAPELAKDkllkdvfwsGDvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYG- 432
Cdd:cd05973  301 RGYQLPDTPAID---------GG-YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGv 370
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 433 -------------VTVPGHEGRAGMAAlalrppqalnlvQLYSHVSENLPPYARPR 475
Cdd:cd05973  371 pdpertevvkafvVLRGGHEGTPALAD------------ELQLHVKKRLSAHAYPR 414
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
141-480 2.87e-12

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 68.91  E-value: 2.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVL-----QCQGFyhlcGVHQED-VIYLALPLYHMsgSLLGIVGCLGIGATVVLKP---KFS 211
Cdd:cd17651  142 IYTSGSTGRPKGVVMPHRSLAnlvawQARAS----SLGPGArTLQFAGLGFDV--SVQEIFSTLCAGATLVLPPeevRTD 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVT-------VFQYIGELCRYLVNQPPSKAE-CDHKVRLAVGSGLRpdtweRFLRRFGPLQILETYGMT 283
Cdd:cd17651  216 PPALAAWLDEQRISrvflptvALRALAEHGRPLGVRLAALRYlLTGGEQLVLTEDLR-----EFCAGLPGLRLHNHYGPT 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 284 EGNVATfnytgrqgavgraswlyKHIFPFSLIRYD--VMTGEPIRNAQGHCMTTS-----PGEPG-LLVAPVSQQSpflG 355
Cdd:cd17651  291 ETHVVT-----------------ALSLPGDPAAWPapPPIGRPIDNTRVYVLDAAlrpvpPGVPGeLYIGGAGLAR---G 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLdflqeVNIYGVTV 435
Cdd:cd17651  351 YLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH-----PGVREAVV 425
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 755503902 436 PGHEGRAGMAALA----LRPPQALNLVQLYSHVSENLPPYARP-RFLRLQ 480
Cdd:cd17651  426 LAREDRPGEKRLVayvvGDPEAPVDAAELRAALATHLPEYMVPsAFVLLD 475
PRK12467 PRK12467
peptide synthase; Provisional
83-474 3.85e-12

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 69.80  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902   83 LEPDLPA------LRAMGLHLWATGPETNV-----AGISNL-LSEAADQVD---EPVPGYLSAPQNImdtCLYIFTSGTT 147
Cdd:PRK12467  592 LDPEYPQdrlaymLDDSGVRLLLTQSHLLAqlpvpAGLRSLcLDEPADLLCgysGHNPEVALDPDNL---AYVIYTSGST 668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  148 GLPKAARISHLKVLQcqgfyHLCGVHQE-----DVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDC 219
Cdd:PRK12467  669 GQPKGVAISHGALAN-----YVCVIAERlqlaaDDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALM 743
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  220 QKHRVTVFQYIGELCRYLVnQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGP-LQILETYGMTEGNVATFNYT-GRQG 297
Cdd:PRK12467  744 ADQGVTVLKIVPSHLQALL-QASRVALPRPQRALVCGGEALQVDLLARVRALGPgARLINHYGPTETTVGVSTYElSDEE 822
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  298 AVGRASWLYKHIFPFSLIRYDvmtgepirnaqgHCMTTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVF-WSG 375
Cdd:PRK12467  823 RDFGNVPIGQPLANLGLYILD------------HYLNPVPvGVVGELY--IGGAGLARGYHRRPALTAERFVPDPFgADG 888
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  376 DVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHEGRAGMAAL--ALRP-- 451
Cdd:PRK12467  889 GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV--LAQPGDAGLQLVAYLvpAAVAdg 966
                         410       420
                  ....*....|....*....|....*
gi 755503902  452 --PQALNLvQLYSHVSENLPPYARP 474
Cdd:PRK12467  967 aeHQATRD-ELKAQLRQVLPDYMVP 990
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
83-479 4.36e-12

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 68.16  E-value: 4.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  83 LEPDLPALRamgLHLWATGpetnvAGISNLLSEAADQvdepvPGYLsapqnimdtclyIFTSGTTGLPKAARISHLKVLQ 162
Cdd:cd17649   67 LDPEYPAER---LRYMLED-----SGAGLLLTHHPRQ-----LAYV------------IYTSGSTGTPKGVAVSHGPLAA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 163 -CQGFYHLCGVHQEDVIylaLPLYHMS--GSLLGIVGCLGIGATVVLKPKfsasQFWDDCQ-------KHRVTVFQ---- 228
Cdd:cd17649  122 hCQATAERYGLTPGDRE---LQFASFNfdGAHEQLLPPLICGACVVLRPD----ELWASADelaemvrELGVTVLDlppa 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 229 YIGELCRYLVNQPPSKAEcdhKVRLAV--GSGLRPDTWERFLRrfGPLQILETYGMTEGNVATFNYTGRQGAvgRASWLY 306
Cdd:cd17649  195 YLQQLAEEADRTGDGRPP---SLRLYIfgGEALSPELLRRWLK--APVRLFNAYGPTEATVTPLVWKCEAGA--ARAGAS 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 307 KHIfpfslirYDVMTGEPIRNAQGHCMTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFW-SGDVFFNTGDLL 385
Cdd:cd17649  268 MPI-------GRPLGGRSAYILDADLNPVPVGVTGELY--IGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLA 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 386 VCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVS 465
Cdd:cd17649  339 RWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALR 418
                        410
                 ....*....|....*
gi 755503902 466 ENLPPYARP-RFLRL 479
Cdd:cd17649  419 ASLPDYMVPaHLVFL 433
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
142-483 4.37e-12

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 68.48  E-value: 4.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHlkvlqcQGFY-------HLCGVHQEDViYL-ALPLYHMSGsLLGIVGCLGIGATVVLKPKFSAS 213
Cdd:cd12118  140 YTSGTTGRPKGVVYHH------RGAYlnalaniLEWEMKQHPV-YLwTLPMFHCNG-WCFPWTVAAVGGTNVCLRKVDAK 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE-CDHKVRLAVGSGLRPdtwERFLRRFGPL--QILETYGMTEG-NVAT 289
Cdd:cd12118  212 AIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARpLPHRVHVMTAGAPPP---AAVLAKMEELgfDVTHVYGLTETyGPAT 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNY----------------TGRQGavgraswlykhifpfslIRYDVMTGEPIRNAQGhcMTTSP------GE---PGLLV 344
Cdd:cd12118  289 VCAwkpewdelpteerarlKARQG-----------------VRYVGLEEVDVLDPET--MKPVPrdgktiGEivfRGNIV 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 345 ApvsqqspfLGYAGAPElAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:cd12118  350 M--------KGYLKNPE-ATAEAFRG-GW-----FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA 414
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755503902 425 LQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR---FLRLQVTS 483
Cdd:cd12118  415 VLEAAVVARPDE-KWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKtvvFGELPKTS 475
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
141-284 6.13e-12

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 68.73  E-value: 6.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  141 IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLyhmS--GSLLGIVGCLGIGATVVLKPK---FSASQ 214
Cdd:COG1020   623 IYTSGSTGRPKGVMVEHRALVNlLAWMQRRYGLGPGDRVLQFASL---SfdASVWEIFGALLSGATLVLAPPearRDPAA 699
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902  215 FWDDCQKHRVTVFQ----YIGELCRYLVNQPPSkaecdhkVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:COG1020   700 LAELLARHRVTVLNltpsLLRALLDAAPEALPS-------LRLVLVGGeaLPPELVRRWRARLPGARLVNLYGPTE 768
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
136-475 6.33e-12

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 66.97  E-value: 6.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd17630    1 RLATVILTSGSTGTPKAVVHTAANLLaSAAGLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 fwddcQKHRVTVFQYIG----ELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLqiLETYGMTE--GNVA 288
Cdd:cd17630   80 -----EDLAPPGVTHVSlvptQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPL--YTTYGMTEtaSQVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFNYTG-RQGAVGRaswlykhifPFSLIRYDVmtgepirnaqghcmtTSPGEpgLLVAPVSQQSPFLGYAGAPELAKDKl 367
Cdd:cd17630  153 TKRPDGfGRGGVGV---------LLPGRELRI---------------VEDGE--IWVGGASLAMGYLRGQLVPEFNEDG- 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 368 lkdvfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 447
Cdd:cd17630  206 -----W-----FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE-ELGQRPVAVI 274
                        330       340
                 ....*....|....*....|....*...
gi 755503902 448 ALRPPqaLNLVQLYSHVSENLPPYARPR 475
Cdd:cd17630  275 VGRGP--ADPAELRAWLKDKLARFKLPK 300
PRK06178 PRK06178
acyl-CoA synthetase; Validated
64-474 8.39e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 67.76  E-value: 8.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  64 VRSCWPQLGLPT-LVEFLESLEPDLPALRAMGLHlwaTGPETNVAGISNLLS-EAADQVDEPVP-GYLSAPQNIMdtcly 140
Cdd:PRK06178 144 VEQVRAETSLRHvIVTSLADVLPAEPTLPLPDSL---RAPRLAAAGAIDLLPaLRACTAPVPLPpPALDALAALN----- 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 iFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLA-LPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDD 218
Cdd:PRK06178 216 -YTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSfLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAA 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 219 CQKHRVTVfqyigelCRYLVNQP------PSKAECDHKVRLAVGS-----GLRPDTWERFLRRFGPLQILETYGMTEGNV 287
Cdd:PRK06178 295 VERYRVTR-------TVMLVDNAvelmdhPRFAEYDLSSLRQVRVvsfvkKLNPDYRQRWRALTGSVLAEAAWGMTETHT 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 A-TFNyTGRQgaVGRASWLYKHIF-----PFSLIRY-DVMTGEPIrnaqghcmttsP-GEPGLLVapVSQQSPFLGYAGA 359
Cdd:PRK06178 368 CdTFT-AGFQ--DDDFDLLSQPVFvglpvPGTEFKIcDFETGELL-----------PlGAEGEIV--VRTPSLLKGYWNK 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 360 PELAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVaEVLetldFLQEVNIYGVTVPG-- 437
Cdd:PRK06178 432 PEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEV-EAL----LGQHPAVLGSAVVGrp 499
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 755503902 438 --HEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK06178 500 dpDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP 538
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
141-475 1.27e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 66.96  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAAR--ISHLKVLQ--------CQGFYhlcGVHQEDVIYLALPLYHMSG-SLLGIVGCLGigATVVLKPK 209
Cdd:PRK13390 154 LYSSGTTGFPKGIQpdLPGRDVDApgdpivaiARAFY---DISESDIYYSSAPIYHAAPlRWCSMVHALG--GTVVLAKR 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGEL-CRYLVNQPPSKAECDHKVRLAVGSGLRP---DTWERFLRRFGPLqILETYGMTEG 285
Cdd:PRK13390 229 FDAQATLGHVERYRITVTQMVPTMfVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvDVKHAMIDWLGPI-VYEYYSSTEA 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVATFNYTGR----QGAVGRAswlykhifpfslirydVMTGEPIRNAQGHCMTTspGEPGlLVAPVSQQSPFlGYAGAPE 361
Cdd:PRK13390 308 HGMTFIDSPDwlahPGSVGRS----------------VLGDLHICDDDGNELPA--GRIG-TVYFERDRLPF-RYLNDPE 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 -LAKDKLLKDVFWSgdvffNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP--GH 438
Cdd:PRK13390 368 kTAAAQHPAHPFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPemGE 442
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 755503902 439 EGRAGMAALA-LRPPQALNLvQLYSHVSENLPPYARPR 475
Cdd:PRK13390 443 QVKAVIQLVEgIRGSDELAR-ELIDYTRSRIAHYKAPR 479
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
141-479 1.88e-11

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 66.53  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHL----KVLQCQGFYhlcGVHQEDVIYLALPLyHMSGSLLGIVGCLGIGATVVL-------KPK 209
Cdd:cd17646  144 IYTSGSTGRPKGVMVTHAgivnRLLWMQDEY---PLGPGDRVLQKTPL-SFDVSVWELFWPLVAGARLVVarpgghrDPA 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFwddcQKHRVTVFQYIGELCRYLVNQPpsKAECDHKVRLAVGSG--LRPDTWERFLRRFG-PLQILetYGMTEgn 286
Cdd:cd17646  220 YLAALI----REHGVTTCHFVPSMLRVFLAEP--AAGSCASLRRVFCSGeaLPPELAARFLALPGaELHNL--YGPTE-- 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 vATFNYTGRQ--GAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMTTS-----PGEPGLLV---APVSQqspflGY 356
Cdd:cd17646  290 -AAIDVTHWPvrGPAETPS---------------VPIGRPVPNTRLYVLDDAlrpvpVGVPGELYlggVQLAR-----GY 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDflqEVNiyGVTVP 436
Cdd:cd17646  349 LGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHP---AVT--HAVVV 423
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755503902 437 GHEGRAGMAAL-----ALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd17646  424 ARAAPAGAARLvgyvvPAAGAAGPDTAALRAHLAERLPEYMVPaAFVVL 472
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
136-475 2.22e-11

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 65.48  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH--LKVLQCQGFYHLCGVHQED-------------VIYLALPLYHMSGSLLGIVGCLGI 200
Cdd:cd05924    4 DDLYILYTGGTTGMPKGVMWRQedIFRMLMGGADFGTGEFTPSedahkaaaaaagtVMFPAPPLMHGTGSWTAFGGLLGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 201 GATVVLKPKFSASQFWDDCQKHRVTVFQYIGE-LCRYLVNQPPSKAECDHKVRLAVGSG---LRPDTWERFLRRFGPLQI 276
Cdd:cd05924   84 QTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPNITL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 LETYGMTEGNVATFNYTGRQGAVGRaswlykhifPFSLIRYDVMTGEPirnaQGHCMTTSPGEPGLL----VAPvsqqsp 352
Cdd:cd05924  164 VDAFGSSETGFTGSGHSAGSGPETG---------PFTRANPDTVVLDD----DGRVVPPGSGGVGWIarrgHIP------ 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 353 fLGYAGAPELAKD--KLLKDVFWSgdvffNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETldflqEVNI 430
Cdd:cd05924  225 -LGYYGDEAKTAEtfPEVDGVRYA-----VPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS-----HPAV 293
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755503902 431 YGVTVPGHE----GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05924  294 YDVLVVGRPderwGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPK 342
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
110-411 2.24e-11

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 66.34  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 110 SNLLSEAADQVDEPVPGylsaPQNIMDTclyIFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMS 188
Cdd:cd05932  119 DDLIAQHPPLEERPTRF----PEQLATL---IYTSGTTGQPKGVMLTFGSfAWAAQAGIEHIGTEENDRMLSYLPLAHVT 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 189 GSLLGIVGCLgIGATVVLKPKfSASQFWDDCQKHRVTVFQYIGELC-----RYLVNQPPSK-----------AECDHKV- 251
Cdd:cd05932  192 ERVFVEGGSL-YGGVLVAFAE-SLDTFVEDVQRARPTLFFSVPRLWtkfqqGVQDKIPQQKlnlllkipvvnSLVKRKVl 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 252 --------RLAV-GSGLRPDTWERFLRRFGpLQILETYGMTEG-NVATFNYTGRQ--GAVGRASwlykhifPFSLIRYDv 319
Cdd:cd05932  270 kglgldqcRLAGcGSAPVPPALLEWYRSLG-LNILEAYGMTENfAYSHLNYPGRDkiGTVGNAG-------PGVEVRIS- 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 320 mtgepirnAQGHCMTTSPGEpgllvapvsqqspFLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRT 399
Cdd:cd05932  341 --------EDGEILVRSPAL-------------MMGYYKDPEATAEAF------TADGFLRTGDKGELDADGNLTITGRV 393
                        330
                 ....*....|...
gi 755503902 400 GDTFRW-KGENVA 411
Cdd:cd05932  394 KDIFKTsKGKYVA 406
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
133-482 2.49e-11

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 65.88  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 133 NIMDTCLYIFTSGTTGLPKAARISHLKVLQCQ----GFYHLCGVHQEDVIYLA-----LPLYHMSGSLLGivgclgiGAT 203
Cdd:cd17648   92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRtslsERYFGRDNGDEAVLFFSnyvfdFFVEQMTLALLN-------GQK 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 204 VVLKP---KFSASQFWDDCQKHRVTvfqyigelcrYLvNQPPSK------AECDH-KVRLAVGSGLRPDTWERFLRRFgP 273
Cdd:cd17648  165 LVVPPdemRFDPDRFYAYINREKVT----------YL-SGTPSVlqqydlARLPHlKRVDAAGEEFTAPVFEKLRSRF-A 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEGNVATfnytgrqgavgraswlYKHIFPFSLiRYDVMTGEPIRNAQ----GHCMTTSP----GE---PGL 342
Cdd:cd17648  233 GLIINAYGPTETTVTN----------------HKRFFPGDQ-RFDKSLGRPVRNTKcyvlNDAMKRVPvgavGElylGGD 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 343 LVAPvsqqspflGYAGAPELAKDKLLKDVFWSGD--------VFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTE 414
Cdd:cd17648  296 GVAR--------GYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGE 367
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 415 VAEVLETLDFLQE---VNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP----RFLRLQVT 482
Cdd:cd17648  368 VEAALASYPGVREcavVAKEDASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVParlvRLEGIPVT 442
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
77-419 3.83e-11

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 65.55  E-value: 3.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  77 VEFLESLEPDLPALRamglHLWATGPETNVAGISNLLSEAADqVDEPVPgylsAPQnimDTCLYIFTSGTTGLPK----- 151
Cdd:COG1021  138 RALARELQAEVPSLR----HVLVVGDAGEFTSLDALLAAPAD-LSEPRP----DPD---DVAFFQLSGGTTGLPKliprt 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 ----------AARIshlkvlqcqgfyhlCGVHQEDViYL-ALPLYH-MSGSLLGIVGCLGIGATVVLKPKFSAsqfwDDC 219
Cdd:COG1021  206 hddylysvraSAEI--------------CGLDADTV-YLaALPAAHnFPLSSPGVLGVLYAGGTVVLAPDPSP----DTA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 220 ----QKHRVTVfqyIGelcryLVnqPP-------SKAECDHKVR-LAV----GSGLRPDTWERFLRRFGP-LQilETYGM 282
Cdd:COG1021  267 fpliERERVTV---TA-----LV--PPlallwldAAERSRYDLSsLRVlqvgGAKLSPELARRVRPALGCtLQ--QVFGM 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 283 TEGNVatfNYTG-------RQGAVGRAswlykhIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--F 353
Cdd:COG1021  335 AEGLV---NYTRlddpeevILTTQGRP------ISPDDEVR--------IVDEDGN--PVPPGEVGELLT----RGPytI 391
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 354 LGYAGAPEL-AKdkllkdVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:COG1021  392 RGYYRAPEHnAR------AF-TPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLL 451
PRK12316 PRK12316
peptide synthase; Provisional
130-474 4.18e-11

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 66.52  E-value: 4.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  130 APQNImdtCLYIFTSGTTGLPKAARISHLKVLQcqgfyHLCGVHQE-----DVIYLALPLYHMSGSLLGIVGCLGIGATV 204
Cdd:PRK12316 4692 HPDNL---AYVIYTSGSTGRPKGVAVSHGSLVN-----HLHATGERyeltpDDRVLQFMSFSFDGSHEGLYHPLINGASV 4763
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  205 VLKPkfsaSQFWDDCQ------KHRVTVFQYIGELCRYLVNQPPSKAECDH-KVRLAVGSGLRPDTWERFLRRFGPLQIL 277
Cdd:PRK12316 4764 VIRD----DSLWDPERlyaeihEHRVTVLVFPPVYLQQLAEHAERDGEPPSlRVYCFGGEAVAQASYDLAWRALKPVYLF 4839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  278 ETYGMTEGNVATFNYTGRQGAVGRASwlYKHIfpfslirydvmtGEPIRNAQGHCMTTSpGEPgllvAPVSQQSPFL--- 354
Cdd:PRK12316 4840 NGYGPTETTVTVLLWKARDGDACGAA--YMPI------------GTPLGNRSGYVLDGQ-LNP----LPVGVAGELYlgg 4900
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  355 -----GYAGAPELAKDKLLKDVFWS-GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEv 428
Cdd:PRK12316 4901 egvarGYLERPALTAERFVPDPFGApGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE- 4979
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902  429 niygVTVPGHEGRAGMAALALRPPQALNLV-----------QLYSHVSENLPPYARP 474
Cdd:PRK12316 4980 ----AVVIAQEGAVGKQLVGYVVPQDPALAdadeaqaelrdELKAALRERLPEYMVP 5032
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
90-475 5.89e-11

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 65.00  E-value: 5.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  90 LRAMGLHLWATGPETNVAGIS-NLLSEAADQVdepvpGYLSAPQNIM--DTCLYIFTSGTTGLPKAARISHLKVLQ--CQ 164
Cdd:PLN02330 141 VKGLGLPVIVLGEEKIEGAVNwKELLEAADRA-----GDTSDNEEILqtDLCALPFSSGTTGISKGVMLTHRNLVAnlCS 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 165 GFYhlcGVHQE---DVIYLAL-PLYHMSGsLLGIV-GCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVN 239
Cdd:PLN02330 216 SLF---SVGPEmigQVVTLGLiPFFHIYG-ITGICcATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVK 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 240 QPPSKAECDHKVRL----AVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASwlyKHIFPFSLI 315
Cdd:PLN02330 292 NPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAK---KNSVGFILP 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 316 RYDVMTGEPiRNAQGHCMTTsPGEpgllvAPVSQQSPFLGYAGAPElAKDKLLKDVFWsgdvfFNTGDLLVCDEQGFLHF 395
Cdd:PLN02330 369 NLEVKFIDP-DTGRSLPKNT-PGE-----LCVRSQCVMQGYYNNKE-ETDRTIDEDGW-----LHTGDIGYIDDDGDIFI 435
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 396 HDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PLN02330 436 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACVVINPKAKESEEDILNFVAANVAHYKKV 513

                 .
gi 755503902 475 R 475
Cdd:PLN02330 514 R 514
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
80-480 7.33e-11

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 64.62  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  80 LESLEPDL----PALRAmGLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLsapqnimdtclyIFTSGTTGLPKAARI 155
Cdd:cd12116   80 LEDAEPALvltdDALPD-RLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYV------------IYTSGSTGRPKGVVV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 156 SHLKVL-QCQGFYHLCGVHQEDVIyLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQYIG 231
Cdd:cd12116  147 SHRNLVnFLHSMRERLGLGPGDRL-LAVTTYAFDISLLELLLPLLAGARVVIAPRetqRDPEALARLIEAHSITVMQATP 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 232 ELCRYLVNQPPSKAEcdhKVRLAVG-SGLRPDTWERFLRRFGPLQILetYGMTEGNVATfnytgrqgAVGRASWLYKHIf 310
Cdd:cd12116  226 ATWRMLLDAGWQGRA---GLTALCGgEALPPDLAARLLSRVGSLWNL--YGPTETTIWS--------TAARVTAAAGPI- 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 311 pfslirydvMTGEPIRNAQGHC-----MTTSPGEPG-LLVA--PVSQqspflGYAGAPELAKDKLLKDVFW-SGDVFFNT 381
Cdd:cd12116  292 ---------PIGRPLANTQVYVldaalRPVPPGVPGeLYIGgdGVAQ-----GYLGRPALTAERFVPDPFAgPGSRLYRT 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 382 GDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVTVPGHEGRAGMAALALRP-PQALNLVQL 460
Cdd:cd12116  358 GDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQA---AVVVREDGGDRRLVAYVVLKaGAAPDAAAL 434
                        410       420
                 ....*....|....*....|.
gi 755503902 461 YSHVSENLPPYARP-RFLRLQ 480
Cdd:cd12116  435 RAHLRATLPAYMVPsAFVRLD 455
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
136-466 7.55e-11

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 64.66  E-value: 7.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHlkvlqcQGFYH-------LCGVHQEDVIYLALPLYH---MSGSllGIVGCLGIGATVV 205
Cdd:cd05920  140 EVALFLLSGGTTGTPKLIPRTH------NDYAYnvrasaeVCGLDQDTVYLAVLPAAHnfpLACP--GVLGTLLAGGRVV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 206 LKPKFSASQFWDDCQKHRVT--------VFQYIGELCRYlVNQPPSkaecdHKVRLAVGSGLRPDTWERFLRRFGPlQIL 277
Cdd:cd05920  212 LAPDPSPDAAFPLIEREGVTvtalvpalVSLWLDAAASR-RADLSS-----LRLLQVGGARLSPALARRVPPVLGC-TLQ 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 278 ETYGMTEGNVatfNYT----------GRQGavgraswlyKHIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApv 347
Cdd:cd05920  285 QVFGMAEGLL---NYTrlddpdeviiHTQG---------RPMSPDDEIR--------VVDEEGN--PVPPGEEGELLT-- 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 348 sqQSP--FLGYAGAPEL-AKdkllkdVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:cd05920  341 --RGPytIRGYYRAPEHnAR------AF-TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA 411
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 755503902 425 LQEVNIygVTVPGHE-GRAGMAALALRPPQaLNLVQLYSHVSE 466
Cdd:cd05920  412 VHDAAV--VAMPDELlGERSCAFVVLRDPP-PSAAQLRRFLRE 451
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
128-479 2.86e-10

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 62.73  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 128 LSAPQNIMDTCLYIFTSGTTGLPKAARISHlkvlqcQGFYHLcgVHQ-EDVIYLA----LPLY---HMSGSLLGIVGCLG 199
Cdd:cd17655  130 LEPVSKSDDLAYVIYTSGSTGKPKGVMIEH------RGVVNL--VEWaNKVIYQGehlrVALFasiSFDASVTEIFASLL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 200 IGATVVLKPKFSASQFWDDCQ---KHRVTVfqyigelcrylVNQPPS----------KAECDHKVRLAVGSGLRPDTWER 266
Cdd:cd17655  202 SGNTLYIVRKETVLDGQALTQyirQNRITI-----------IDLTPAhlklldaaddSEGLSLKHLIVGGEALSTELAKK 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 267 FLRRFGP-LQILETYGMTEGNV--ATFNYTGrqgavgraSWLYKHIFPFslirydvmtGEPIRNAQGHCMTTS----P-G 338
Cdd:cd17655  271 IIELFGTnPTITNAYGPTETTVdaSIYQYEP--------ETDQQVSVPI---------GKPLGNTRIYILDQYgrpqPvG 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 339 EPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEV 418
Cdd:cd17655  334 VAGELY--IGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEAR 411
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902 419 LETLDFLQEVNIygVTVPGHEGRAGMAA-LALRPPqaLNLVQLYSHVSENLPPYARPR-FLRL 479
Cdd:cd17655  412 LLQHPDIKEAVV--IARKDEQGQNYLCAyIVSEKE--LPVAQLREFLARELPDYMIPSyFIKL 470
PRK06164 PRK06164
acyl-CoA synthetase; Validated
116-437 4.21e-10

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 62.45  E-value: 4.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 116 AADQVDEPVPGYLSAPQNIMDTCLYIFT-SGTTGLPKAARISHLKVLQcqgfyH------LCGVHQEDVIYLALPlyhMS 188
Cdd:PRK06164 161 LFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLR-----HaraiarAYGYDPGAVLLAALP---FC 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 189 GS--LLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGS---GLRpDT 263
Cdd:PRK06164 233 GVfgFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASfapALG-EL 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 264 WERFLRRFGPLQILetYGMTE------GNVATFNYTGRQGAVGRAswlykhIFPFSLIRY-DVMTGEPIrnaqghcmttS 336
Cdd:PRK06164 312 AALARARGVPLTGL--YGSSEvqalvaLQPATDPVSVRIEGGGRP------ASPEARVRArDPQDGALL----------P 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 337 PGEPGLLvaPVSQQSPFLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVA 416
Cdd:PRK06164 374 DGESGEI--EIRAPSLMRGYLDNPDATARAL------TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
                        330       340
                 ....*....|....*....|.
gi 755503902 417 EVLETLDFLQEVNIYGVTVPG 437
Cdd:PRK06164 446 HALEALPGVAAAQVVGATRDG 466
PLN02246 PLN02246
4-coumarate--CoA ligase
142-284 6.76e-10

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 61.54  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHlKVL------QCQG----FYhlcgVHQEDVIYLALPLYHMSgSLLGIVGC-LGIGATVVLKPKF 210
Cdd:PLN02246 186 YSSGTTGLPKGVMLTH-KGLvtsvaqQVDGenpnLY----FHSDDVILCVLPMFHIY-SLNSVLLCgLRVGAAILIMPKF 259
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 211 SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLaVGSGLRP--DTWERFLRRFGPLQIL-ETYGMTE 284
Cdd:PLN02246 260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGAAPlgKELEDAFRAKLPNAVLgQGYGMTE 335
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
46-454 8.92e-10

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 61.14  E-value: 8.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  46 PPLYAEdpcctASAAAVRVRSCWPQLGLPT-LVEFleSLEPDLPALRAMGLHLwatgpetnvaGISNLLSEAADQVDEPV 124
Cdd:cd05906   97 PPTYDE-----PNARLRKLRHIWQLLGSPVvLTDA--ELVAEFAGLETLSGLP----------GIRVLSIEELLDTAADH 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 125 PGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSL-LGI----VGCL 198
Cdd:cd05906  160 DLPQSRPD---DLALLMLTSGSTGFPKAVPLTHRNILaRSAGKIQHNGLTPQDVFLNWVPLDHVGGLVeLHLravyLGCQ 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 199 GIGA---TVVLKPkfsaSQFWDDCQKHRVTV-----FQYiGELCRYLVNQPPSKAECDhKVRLAVGSG--LRPDTWERFL 268
Cdd:cd05906  237 QVHVpteEILADP----LRWLDLIDRYRVTItwapnFAF-ALLNDLLEEIEDGTWDLS-SLRYLVNAGeaVVAKTIRRLL 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 269 RRFGPLQ-----ILETYGMTE-GNVATFNYTGRQGAVGRASwlykhifPF-SLIRydVMTGEPIRNAQGHCMTTSPGEPG 341
Cdd:cd05906  311 RLLEPYGlppdaIRPAFGMTEtCSGVIYSRSFPTYDHSQAL-------EFvSLGR--PIPGVSMRIVDDEGQLLPEGEVG 381
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 342 LLvaPVSQQSPFLGYAGAPELAKDKLLKDvFWsgdvfFNTGDLLVCDEqGFLHFHDRTGDTFRWKGENVATTEVAEVLET 421
Cdd:cd05906  382 RL--QVRGPVVTKGYYNNPEANAEAFTED-GW-----FRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEE 452
                        410       420       430
                 ....*....|....*....|....*....|...
gi 755503902 422 LDflqevniyGVTVpghegrAGMAALALRPPQA 454
Cdd:cd05906  453 VP--------GVEP------SFTAAFAVRDPGA 471
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
136-432 1.27e-09

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 60.45  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVgCLGIGATVVLKpkfSASQ 214
Cdd:cd17640   89 DLATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQAYT---SIRT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQ---------YIGeLCRYLVNQPPSKAECDH------KVRLAV-GSGLRPDTWERFLRRFGpLQILE 278
Cdd:cd17640  165 LKDDLKRVKPHYIVsvprlweslYSG-IQKQVSKSSPIKQFLFLfflsggIFKFGIsGGGALPPHVDTFFEAIG-IEVLN 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 279 TYGMTE-GNVATFNYTGR--QGAVGraswlykHIFPFSLIRY-DVMTGEPirnaqghcmtTSPGEPGLLVApvsqQSP-- 352
Cdd:cd17640  243 GYGLTEtSPVVSARRLKCnvRGSVG-------RPLPGTEIKIvDPEGNVV----------LPPGEKGIVWV----RGPqv 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 353 FLGYAGAPElAKDKLLkdvfwSGDVFFNTGDL--LVCDeqGFLHFHDRTGDTFRWK-GENVATTEVAEVLETLDFLQEVN 429
Cdd:cd17640  302 MKGYYKNPE-ATSKVL-----DSDGWFNTGDLgwLTCG--GELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIM 373

                 ...
gi 755503902 430 IYG 432
Cdd:cd17640  374 VVG 376
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
141-476 1.45e-09

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 60.26  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQCQGFYHLC-GVHQED--VIYLAlplYHMSGSLLGIVGCLGIGATVVLKP---KFSASQ 214
Cdd:cd17645  110 IYTSGSTGLPKGVMIEHHNLVNLCEWHRPYfGVTPADksLVYAS---FSFDASAWEIFPHLTAGAALHVVPserRLDLDA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPpskaecDHKVRLAVGSGlrpDTWERFLRRfgPLQILETYGMTEGNV-ATfnyt 293
Cdd:cd17645  187 LNDYFNQEGITISFLPTGAAEQFMQLD------NQSLRVLLTGG---DKLKKIERK--GYKLVNNYGPTENTVvAT---- 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 294 grqgavgraswlykhIFPFSLIRYDVMTGEPIRNAQ----GHCMTTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLL 368
Cdd:cd17645  252 ---------------SFEIDKPYANIPIGKPIDNTRvyilDEALQLQPiGVAGELC--IAGEGLARGYLNRPELTAEKFI 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 KDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEvniygVTVPGHEGRAGMAALA 448
Cdd:cd17645  315 VHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL-----AAVLAKEDADGRKYLV 389
                        330       340       350
                 ....*....|....*....|....*....|
gi 755503902 449 --LRPPQALNLVQLYSHVSENLPPYARPRF 476
Cdd:cd17645  390 ayVTAPEEIPHEELREWLKNDLPDYMIPTY 419
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
83-477 1.88e-09

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 59.98  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  83 LEPDLPALRAMGL-----------HLWATGPETNVAGISNLLSEAADQVDEPVPGyLSAPQnimDTCLYIFTSGTTGLPK 151
Cdd:cd12114   67 VDIDQPAARREAIladagarlvltDGPDAQLDVAVFDVLILDLDALAAPAPPPPV-DVAPD---DLAYVIFTSGSTGTPK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 AARISHLKVLQ-CQGFYHLCGVHQEDVIyLALPLYHMSGSLLGIVGCLGIGATVVLKP---KFSASQFWDDCQKHRVTVF 227
Cdd:cd12114  143 GVMISHRAALNtILDINRRFAVGPDDRV-LALSSLSFDLSVYDIFGALSAGATLVLPDearRRDPAHWAELIERHGVTLW 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 228 QYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWL 305
Cdd:cd12114  222 NSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIP 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 306 YKhiFPFSLIRYDVMtgepirNAQG-HCMTTSPGE---PGLLVApvsqqspfLGYAGAPELAKDKLLKDVfwSGDVFFNT 381
Cdd:cd12114  302 YG--RPLANQRYRVL------DPRGrDCPDWVPGElwiGGRGVA--------LGYLGDPELTAARFVTHP--DGERLYRT 363
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 382 GDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETldfLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQ-- 459
Cdd:cd12114  364 GDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA---HPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPda 440
                        410
                 ....*....|....*...
gi 755503902 460 LYSHVSENLPPYARPRFL 477
Cdd:cd12114  441 LRAFLAQTLPAYMIPSRV 458
PRK08315 PRK08315
AMP-binding domain protein; Validated
142-433 5.94e-09

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 58.67  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHLKVL-------QCQGFYHlcgvhqEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLK-PKFSAS 213
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILnngyfigEAMKLTE------EDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPgEGFDPL 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQ-----YIGELcrylvnQPPSKAECDHkvrlavgSGLR---------P-DTWERFLRRFGPLQILE 278
Cdd:PRK08315 280 ATLAAVEEERCTALYgvptmFIAEL------DHPDFARFDL-------SSLRtgimagspcPiEVMKRVIDKMHMSEVTI 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 279 TYGMTEGN-VATFNYTG-----RQGAVGRAswlykhiFPFSLIR-YDVMTGEpirnaqghcmTTSPGEPGLLVApvSQQS 351
Cdd:PRK08315 347 AYGMTETSpVSTQTRTDdplekRVTTVGRA-------LPHLEVKiVDPETGE----------TVPRGEQGELCT--RGYS 407
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 352 PFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFhdrTGdtfRWK------GENVATTEVAEVLETLDFL 425
Cdd:PRK08315 408 VMKGYWNDPEKTAEAIDAD----G--WMHTGDLAVMDEEGYVNI---VG---RIKdmiirgGENIYPREIEEFLYTHPKI 475

                 ....*...
gi 755503902 426 QEVNIYGV 433
Cdd:PRK08315 476 QDVQVVGV 483
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
115-421 7.66e-09

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 58.16  E-value: 7.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 115 EAADQVDEPVPGyLSAPQNIMdtclyiFTSGTTGLPKAARISH----LKVLQCQGFYHLCGvHQEDVIYLA-LPLYHMSG 189
Cdd:cd05929  112 AEGGSPETPIED-EAAGWKML------YSGGTTGRPKGIKRGLpggpPDNDTLMAAALGFG-PGADSVYLSpAPLYHAAP 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 190 SLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPpskAECDHKVRLA-------VGSGLRPD 262
Cdd:cd05929  184 FRWSMTA-LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLP---EAVRNAYDLSslkrvihAAAPCPPW 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 263 TWERFLRRFGPLqILETYGMTEGNVATF----NYTGRQGAVGRAswlykhifpfslirydVMTGEPIRNAQGH-CMTTSP 337
Cdd:cd05929  260 VKEQWIDWGGPI-IWEYYGGTEGQGLTIingeEWLTHPGSVGRA----------------VLGKVHILDEDGNeVPPGEI 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 338 GEPGLLVAPvsqqsPFLgYAGAPELAKDKLLKDVFWSgdvffnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAE 417
Cdd:cd05929  323 GEVYFANGP-----GFE-YTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIEN 390

                 ....
gi 755503902 418 VLET 421
Cdd:cd05929  391 ALIA 394
PRK06188 PRK06188
acyl-CoA synthetase; Validated
91-466 1.14e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 57.69  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  91 RAMGL-HLWATGPetnvAGISNLLSEAADQVdEPVPgyLSAPQNIMDTCLYIFTSGTTGLPKAARISH-----LKVLQCQ 164
Cdd:PRK06188 130 RVPSLkHVLTLGP----VPDGVDLLAAAAKF-GPAP--LVAAALPPDIAGLAYTGGTTGKPKGVMGTHrsiatMAQIQLA 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 165 GFYHlcgvhQEDVIYLAL-PLYHMSGSLlgIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPS 243
Cdd:PRK06188 203 EWEW-----PADPRFLMCtPLSHAGGAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDL 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 244 KAECDHKVRLAV--GSGLRPDTWERFLRRFGPLqILETYGMTE-GNVATF--------NYTGRQGAVGRASwlykhifPF 312
Cdd:PRK06188 276 RTRDLSSLETVYygASPMSPVRLAEAIERFGPI-FAQYYGQTEaPMVITYlrkrdhdpDDPKRLTSCGRPT-------PG 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 313 SLIRYDVMTGEPIrnaqghcmttSPGEPG-LLVApvsqqSPFL--GYAGAPElAKDKLLKDVfWsgdvfFNTGDLLVCDE 389
Cdd:PRK06188 348 LRVALLDEDGREV----------AQGEVGeICVR-----GPLVmdGYWNRPE-ETAEAFRDG-W-----LHTGDVAREDE 405
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 390 QGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSE 466
Cdd:PRK06188 406 DGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHVKE 481
PRK05857 PRK05857
fatty acid--CoA ligase;
141-448 1.28e-08

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 57.71  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLK------VLQCQGFYHLCGVHQEdVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSAS- 213
Cdd:PRK05857 175 IFTSGTTGEPKAVLLANRTffavpdILQKEGLNWVTWVVGE-TTYSPLPATHIGG-LWWILTCLMHGGLCVTGGENTTSl 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 -QFWDDcqkHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWE-RFLRRFGpLQILETYGMTE------- 284
Cdd:PRK05857 253 lEILTT---NAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADvRFIEATG-VRTAQVYGLSEtgctalc 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 -----GNVATFnytgRQGAVGRaswlykhifPFSLIR-YdvmtgepIRNAQGHCMTTSPGEPGLLVAPVSQQSP--FLGY 356
Cdd:PRK05857 329 lptddGSIVKI----EAGAVGR---------PYPGVDvY-------LAATDGIGPTAPGAGPSASFGTLWIKSPanMLGY 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP 436
Cdd:PRK05857 389 WNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE 461
                        330
                 ....*....|..
gi 755503902 437 GHEGRAGMAALA 448
Cdd:PRK05857 462 EFGALVGLAVVA 473
PRK12316 PRK12316
peptide synthase; Provisional
107-474 1.93e-08

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 57.66  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  107 AGISNLLSEAADQVDEpVPGYLSAPQNIMDTCLY-IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPl 184
Cdd:PRK12316 2118 AGVARLPLDRDAEWAD-YPDTAPAVQLAGENLAYvIYTSGSTGLPKGVAVSHGALVAhCQAAGERYELSPADCELQFMS- 2195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  185 YHMSGSLLGIVGCLGIGATVVLKPK--FSASQFWDDCQKHRVTV-------FQYIGELCRYLVNQPPSKAECdhkvrlAV 255
Cdd:PRK12316 2196 FSFDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTIldfppvyLQQLAEHAERDGRPPAVRVYC------FG 2269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  256 GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYT-GRQGAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMT 334
Cdd:PRK12316 2270 GEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKcRPQDPCGAAY---------------VPIGRALGNRRAYILD 2334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  335 TS-----PGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVF-WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGE 408
Cdd:PRK12316 2335 ADlnllaPGMAGELY--LGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGF 2412
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902  409 NVATTEVAEVLETLDFLQEVNIygVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVP 2476
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
136-427 2.22e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 56.68  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd05914   90 DVALINYTSGTTGNSKGVMLTYRNIVsNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FwDDCQKHRVTVFqyIGeLCRYLV-------NQPPSKAECDHKVRLAV-----------------------------GSG 258
Cdd:cd05914  170 I-IALAFAQVTPT--LG-VPVPLViekifkmDIIPKLTLKKFKFKLAKkinnrkirklafkkvheafggnikefvigGAK 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 259 LRPDTwERFLRRFGpLQILETYGMTE-GNVATFNYTGRqgavgraswlykhifpfslIRYDvMTGEPIRNAQghCMTTSP 337
Cdd:cd05914  246 INPDV-EEFLRTIG-FPYTIGYGMTEtAPIISYSPPNR-------------------IRLG-SAGKVIDGVE--VRIDSP 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 338 ---GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRW-KGENVATT 413
Cdd:cd05914  302 dpaTGEGEII--VRGPNVMKGYYKNPEATAEAFDKD-GW-----FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPE 373
                        330       340
                 ....*....|....*....|.
gi 755503902 414 EV-------AEVLETLDFLQE 427
Cdd:cd05914  374 EIeakinnmPFVLESLVVVQE 394
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
141-479 2.74e-08

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 56.17  E-value: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQCQGFY-HLCGVHQedviyLALPLYHMSG----SLLGIVGCLGIGATVVLKPkfSASQF 215
Cdd:cd12115  111 IYTSGSTGRPKGVAIEHRNAAAFLQWAaAAFSAEE-----LAGVLASTSIcfdlSVFELFGPLATGGKVVLAD--NVLAL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDDCQKHRVTVFQYIGELCRYLVNQP--PSKAECdhkVRLAvGSGLRPDTWERFLRRFGPLQILETYGMTEgnvATFNYT 293
Cdd:cd12115  184 PDLPAAAEVTLINTVPSAAAELLRHDalPASVRV---VNLA-GEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYST 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 294 GrqGAVGRASwlykhifpfsliRYDVMTGEPIRNAQGHCMTTS-----PGEPGLLV---APVSQqspflGYAGAPELAKD 365
Cdd:cd12115  257 V--APVPPGA------------SGEVSIGRPLANTQAYVLDRAlqpvpLGVPGELYiggAGVAR-----GYLGRPGLTAE 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 366 KLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVnIYGVTVPGHEGRAGMA 445
Cdd:cd12115  318 RFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA-VVVAIGDAAGERRLVA 396
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 755503902 446 ALALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd12115  397 YIVAEPGAAGLVEDLRRHLGTRLPAYMVPsRFVRL 431
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
136-477 3.16e-08

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 56.33  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLY-IFTSGTTGLPKAARISHLKVLQCQGFY--HLCGVHQEDVIYLALPLYHMSGSllGIVGCLGIGATVVLKP---K 209
Cdd:cd17656  128 DDLLYiIYTSGTTGKPKGVQLEHKNMVNLLHFEreKTNINFSDKVLQFATCSFDVCYQ--EIFSTLLSGGTLYIIReetK 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHR-------VTVFQYIGELCRYLvnqpPSKAEC-DHKVrlAVGSGLR-PDTWERFLRRFGpLQILETY 280
Cdd:cd17656  206 RDVEQLFDLVKRHNievvflpVAFLKFIFSEREFI----NRFPTCvKHII--TAGEQLViTNEFKEMLHEHN-VHLHNHY 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 281 GMTEGNVATfNYTGRQGAvgraswlykHIFPFSLIrydvmtGEPIRNAQ----GHCMTTSP-GEPGLLVapVSQQSPFLG 355
Cdd:cd17656  279 GPSETHVVT-TYTINPEA---------EIPELPPI------GKPISNTWiyilDQEQQLQPqGIVGELY--ISGASVARG 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQE--VNIYGV 433
Cdd:cd17656  341 YLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEavVLDKAD 420
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 755503902 434 TVPGHEGRAGMAALalrppQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd17656  421 DKGEKYLCAYFVME-----QELNISQLREYLAKQLPEYMIPSFF 459
PRK12316 PRK12316
peptide synthase; Provisional
83-474 4.16e-08

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 56.50  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902   83 LEPDLPALRAM------GLHLWATGPE---TNVAGISNLLSEA-ADQVDEPVPGYLSAPQNImdtCLYIFTSGTTGLPKA 152
Cdd:PRK12316 3137 LDPEYPEERLAymledsGAQLLLSQSHlrlPLAQGVQVLDLDRgDENYAEANPAIRTMPENL---AYVIYTSGSTGKPKG 3213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  153 ARISHLKVLQcqgfyHLCGVHQ-----EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLkpkfSASQFWDD-------CQ 220
Cdd:PRK12316 3214 VGIRHSALSN-----HLCWMQQayglgVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL----AGPEDWRDpallvelIN 3284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  221 KHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFlrrFGPLQILETYGMTEgnvatfnytgrqGAVG 300
Cdd:PRK12316 3285 SEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV---FAGLPLYNLYGPTE------------ATIT 3349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  301 RASWLYKHIFPFSlirydVMTGEPIRNAQGHCM----TTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSG 375
Cdd:PRK12316 3350 VTHWQCVEEGKDA-----VPIGRPIANRACYILdgslEPVPvGALGELY--LGGEGLARGYHNRPGLTAERFVPDPFVPG 3422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  376 DVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGHEGRAGMAALALRPPQAL 455
Cdd:PRK12316 3423 ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL-----LEHPWVREAVVLAVDGRQLVAYVVPEDEAGD 3497
                         410
                  ....*....|....*....
gi 755503902  456 NLVQLYSHVSENLPPYARP 474
Cdd:PRK12316 3498 LREALKAHLKASLPEYMVP 3516
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
74-408 8.84e-08

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 54.94  E-value: 8.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  74 PTLVEFLESLEPDLPALRA-----MGLHLWATGPETNVAgISNLLSEAADQVDEPVpgylsAPQNIMDTCLYifTSGTTG 148
Cdd:cd12119  105 RDFLPLLEAIAPRLPTVEHvvvmtDDAAMPEPAGVGVLA-YEELLAAESPEYDWPD-----FDENTAAAICY--TSGTTG 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 149 LPKAARISH-------LKVLQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVgCLGIGATVVLKPKF----SASQFWD 217
Cdd:cd12119  177 NPKGVVYSHrslvlhaMAALLTDGL----GLSESDVVLPVVPMFHVNAWGLPYA-AAMVGAKLVLPGPYldpaSLAELIE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 218 dcqKHRVTVFQ-----YIGELCRYLVNqppsKAECDHKVRLAV-GSGLRPDTWERFLRRFgpLQILETYGMTEgnvatfn 291
Cdd:cd12119  252 ---REGVTFAAgvptvWQGLLDHLEAN----GRDLSSLRRVVIgGSAVPRSLIEAFEERG--VRVIHAWGMTE------- 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 yTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEP-------IRNAQGHCMTTSPGEPGLLVApvsqQSPFL--GYAGAPEl 362
Cdd:cd12119  316 -TSPLGTVARPPSEHSNLSEDEQLALRAKQGRPvpgvelrIVDDDGRELPWDGKAVGELQV----RGPWVtkSYYKNDE- 389
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 755503902 363 akdkllKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGE 408
Cdd:cd12119  390 ------ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGE 429
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
136-480 1.33e-07

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 54.11  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLK--VLQCQGFYHLcGVHQEDViylalplyHMSGSLLG--------IVGCLGIGATVV 205
Cdd:cd05974   86 DPMLLYFTSGTTSKPKLVEHTHRSypVGHLSTMYWI-GLKPGDV--------HWNISSPGwakhawscFFAPWNAGATVF 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 206 L--KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAecDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYG 281
Cdd:cd05974  157 LfnYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASF--DVKLREVVGAGepLNPEVIEQVRRAWG-LTIRDGYG 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTEGNVATFNYTG---RQGAVGRAswlykhifpfsLIRYDVMTGEPIrnaqghcmtTSPGEPGLLVAPVSQQSP---FLG 355
Cdd:cd05974  234 QTETTALVGNSPGqpvKAGSMGRP-----------LPGYRVALLDPD---------GAPATEGEVALDLGDTRPvglMKG 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTV 435
Cdd:cd05974  294 YAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPS 364
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 755503902 436 PGHEGRAGMAALAL-----RPPQALNLVqLYSHVSENLPPYARPRflRLQ 480
Cdd:cd05974  365 PDPVRLSVPKAFIVlragyEPSPETALE-IFRFSRERLAPYKRIR--RLE 411
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
136-288 1.90e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 53.85  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQC-QGFYHLCGVHQE-DVIYLALPLYH-MsgsllGIVGCLGI----GATVVlkp 208
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYANaEAMFVAAEFDVEtDVMVSWLPLFHdM-----GMVGFLTVpmyfGAELV--- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 209 KFSASQFWDD-------CQKHRVTV-----FQYiGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLR---RF 271
Cdd:PRK07768 225 KVTPMDFLRDpllwaelISKYRGTMtaapnFAY-ALLARRLRRQAKPGAFDLSSLRFALngAEPIDPADVEDLLDagaRF 303
                        170
                 ....*....|....*....
gi 755503902 272 G--PLQILETYGMTEGNVA 288
Cdd:PRK07768 304 GlrPEAILPAYGMAEATLA 322
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
82-284 2.41e-07

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 53.40  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  82 SLEPDLPALRAMGLHLWATGPETnVAGISNLLSEAADQVDEPVPGYLsapqnimDTCLYIFTSGTTGLPKAARISHLKVL 161
Cdd:cd05931  104 TTAAALAAVRAFAASRPAAGTPR-LLVVDLLPDTSAADWPPPSPDPD-------DIAYLQYTSGSTGTPKGVVVTHRNLL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 162 -QCQGFYHLCGVHQEDVIYLALPLYH-MsgsllGIVGCLGI----GATVVLkpkFSASQF------W-DDCQKHRVTV-- 226
Cdd:cd05931  176 aNVRQIRRAYGLDPGDVVVSWLPLYHdM-----GLIGGLLTplysGGPSVL---MSPAAFlrrplrWlRLISRYRATIsa 247
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755503902 227 ---FQYigELC-RYLvnQPPSKAECD-HKVRLAVgSG---LRPDTWERFLRRFGPL-----QILETYGMTE 284
Cdd:cd05931  248 apnFAY--DLCvRRV--RDEDLEGLDlSSWRVAL-NGaepVRPATLRRFAEAFAPFgfrpeAFRPSYGLAE 313
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
136-432 4.15e-07

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 52.60  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYH----LCGVHQEDVIYLALPLYHMSGSLLgIVGCLGIGATV------ 204
Cdd:cd05927  115 DLATICYTSGTTGNPKGVMLTHGNIVsNVAGVFKileiLNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIgfysgd 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 205 ---------VLKPKFSAS------QFWDDCQKHRV-------TVFQYIGELCRYLVNQPPSKAE------CDHKVRLAVG 256
Cdd:cd05927  194 irlllddikALKPTVFPGvprvlnRIYDKIFNKVQakgplkrKLFNFALNYKLAELRSGVVRASpfwdklVFNKIKQALG 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 257 SGLR----------PDTwERFLRR-FGpLQILETYGMTEGNVATFnyTGRQGavgraSWLYKHI---FPFSLIR------ 316
Cdd:cd05927  274 GNVRlmltgsaplsPEV-LEFLRVaLG-CPVLEGYGQTECTAGAT--LTLPG-----DTSVGHVggpLPCAEVKlvdvpe 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 317 --YDVMTGEP-----IRnaqGHCMttspgepgllvapvsqqspFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDE 389
Cdd:cd05927  345 mnYDAKDPNPrgevcIR---GPNV-------------------FSGYYKDPEKTAEALDED----G--WLHTGDIGEWLP 396
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 755503902 390 QGFLHFHDRTGDTFRW-KGENVAttevAEVLETL----DFLQEVNIYG 432
Cdd:cd05927  397 NGTLKIIDRKKNIFKLsQGEYVA----PEKIENIyarsPFVAQIFVYG 440
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
136-476 4.41e-07

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 51.92  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLqCQGFyHLCGVHQ--EDVIYL-ALPLYHMsGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd17636    1 DPVLAIYTAAFSGRPNGALLSHQALL-AQAL-VLAVLQAidEGTVFLnSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVT----VFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGplqileTYGMTE-GNV 287
Cdd:cd17636   78 EEVLELIEAERCThaflLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG------GYGQTEvMGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFNYTGRQ--GAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--FLGYAGAPELA 363
Cdd:cd17636  152 ATFAALGGGaiGGAGRPS-------PLVQVR--------ILDEDGR--EVPDGEVGEIVA----RGPtvMAGYWNRPEVN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 364 KDKlLKDVFWsgdvffNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAG 443
Cdd:cd17636  211 ARR-TRGGWH------HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRW-AQSV 282
                        330       340       350
                 ....*....|....*....|....*....|...
gi 755503902 444 MAALALRPPQALNLVQLYSHVSENLPPYARPRF 476
Cdd:cd17636  283 KAIVVLKPGASVTEAELIEHCRARIASYKKPKS 315
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
138-284 5.35e-07

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 52.09  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 138 CLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLyHMSGSLLGIVGCLGIGATVVLKP---KFSAS 213
Cdd:cd17654  121 AYVIHTSGTTGTPKIVAVPHKCILPnIQHFRSLFNITSEDILFLTSPL-TFDPSVVEIFLSLSSGATLLIVPtsvKVLPS 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWD-DCQKHRVTVFQyigeLCRYLVNQPPSKAECDHKVR-------LAVGSGLRP-DTWERFLRRFGP-LQILETYGMT 283
Cdd:cd17654  200 KLADiLFKRHRITVLQ----ATPTLFRRFGSQSIKSTVLSatsslrvLALGGEPFPsLVILSSWRGKGNrTRIFNIYGIT 275

                 .
gi 755503902 284 E 284
Cdd:cd17654  276 E 276
PRK12316 PRK12316
peptide synthase; Provisional
83-474 1.28e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 51.88  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902   83 LEPDLPALR----------AMGLHLWATGPETNV-AGISNLlseAADQVDEPVPGYLSAPqniMDTCLY-------IFTS 144
Cdd:PRK12316  591 LDPEYPAERlaymledsgvQLLLSQSHLGRKLPLaAGVQVL---DLDRPAAWLEGYSEEN---PGTELNpenlayvIYTS 664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  145 GTTGLPKAARISH--LKVLQC--QGFYHLcGVHQEdviYLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWD 217
Cdd:PRK12316  665 GSTGKPKGAGNRHraLSNRLCwmQQAYGL-GVGDT---VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVE 740
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  218 DCQKHRVTVFQYIGELCRYLVnQPPSKAECDHKVRLAV-GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQ 296
Cdd:PRK12316  741 LINREGVDTLHFVPSMLQAFL-QDEDVASCTSLRRIVCsGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVE 819
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  297 gAVGRAswlykhifpfslirydVMTGEPIRNAQGHCMttspgEPGLLVAPVSQQSPFL--------GYAGAPELAKDKLL 368
Cdd:PRK12316  820 -EGGDS----------------VPIGRPIANLACYIL-----DANLEPVPVGVLGELYlagrglarGYHGRPGLTAERFV 877
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  369 KDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVtvpghEGRAGMAALA 448
Cdd:PRK12316  878 PSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGKQLVGYVV 952
                         410       420
                  ....*....|....*....|....*.
gi 755503902  449 LRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK12316  953 LESEGGDWREALKAHLAASLPEYMVP 978
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
414-479 1.51e-06

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 46.00  E-value: 1.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902  414 EVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:pfam13193   1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVF 65
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
141-209 5.87e-06

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 49.10  E-value: 5.87e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755503902 141 IFTSGTTGLPKAArishlkVLQCQGfyHLC---GV------HQEDVIYLALPLYHMSGslLGIV-GCLGIGATVVLKPK 209
Cdd:PRK09029 141 TLTSGSTGLPKAA------VHTAQA--HLAsaeGVlslmpfTAQDSWLLSLPLFHVSG--QGIVwRWLYAGATLVVRDK 209
PLN02736 PLN02736
long-chain acyl-CoA synthetase
60-284 1.08e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 48.17  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  60 AAVRVRSCWPQLgLPTLVEFLeslePDLPALR------AMGLHLWATGPETNV--AGISNLLSEAADQVDEPVPgylSAP 131
Cdd:PLN02736 149 AEVAAIFCVPQT-LNTLLSCL----SEIPSVRlivvvgGADEPLPSLPSGTGVeiVTYSKLLAQGRSSPQPFRP---PKP 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 132 QNIMDTClyiFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMSgSLLGIVGCLGIGATV------ 204
Cdd:PLN02736 221 EDVATIC---YTSGTTGTPKGVVLTHGNlIANVAGSSLSTKFYPSDVHISYLPLAHIY-ERVNQIVMLHYGVAVgfyqgd 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 205 VLKpkfsasqFWDDCQKHRVTVF------------------QYIGELCRYLVN-------------QPPS---------- 243
Cdd:PLN02736 297 NLK-------LMDDLAALRPTIFcsvprlynriydgitnavKESGGLKERLFNaaynakkqalengKNPSpmwdrlvfnk 369
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755503902 244 -KAECDHKVRLaVGSG---LRPDTWErFLRR-FGPlQILETYGMTE 284
Cdd:PLN02736 370 iKAKLGGRVRF-MSSGaspLSPDVME-FLRIcFGG-RVLEGYGMTE 412
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
139-242 1.36e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 48.20  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLalpLYHMS-GSL---LGIVGCLGIGATVVL------K 207
Cdd:PTZ00237 257 LYIlYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVV---FSHSSiGWVsfhGFLYGSLSLGNTFVMfeggiiK 333
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755503902 208 PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPP 242
Cdd:PTZ00237 334 NKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDP 368
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
72-227 3.13e-05

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 46.88  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  72 GLPTLVEFLEslepdLPALRAMGLHLWATGPetNVAGISNLLSEAADQVDEPVPGYLSAPqnimdtcLYI-FTSGTTGLP 150
Cdd:cd05943  199 GLPSLLAVVV-----VPYTVAAGQPDLSKIA--KALTLEDFLATGAAGELEFEPLPFDHP-------LYIlYSSGTTGLP 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 151 KA-------ARISHLKVLQCQgfyhlCGVHQEDVI-YLALPLYHMSGSLlgiVGCLGIGATVVL------KPKFSAsqFW 216
Cdd:cd05943  265 KCivhgaggTLLQHLKEHILH-----CDLRPGDRLfYYTTCGWMMWNWL---VSGLAVGATIVLydgspfYPDTNA--LW 334
                        170
                 ....*....|.
gi 755503902 217 DDCQKHRVTVF 227
Cdd:cd05943  335 DLADEEGITVF 345
PRK07798 PRK07798
acyl-CoA synthetase; Validated
85-302 4.58e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 46.03  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  85 PDLPALRAMGLHLWATGPETNVAGISnLLSEAADQVDEPVPGYLSApqnimDTCLYIFTSGTTGLPKAA--RISHLKVLQ 162
Cdd:PRK07798 119 PRLPKLRTLVVVEDGSGNDLLPGAVD-YEDALAAGSPERDFGERSP-----DDLYLLYTGGTTGMPKGVmwRQEDIFRVL 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 163 CQGFYHLCG--VHQED------------VIYLALPLYHMSGsLLGIVGCLGIGATVVL--KPKFSASQFWDDCQKHRVTV 226
Cdd:PRK07798 193 LGGRDFATGepIEDEEelakraaagpgmRRFPAPPLMHGAG-QWAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 227 FQYIGE-LCRYLVN--QPPSKAECDHKVrlAVGSG---LRPDTWERFLRRFGPLQILETYGMTEgnvATFNYTGRQ--GA 298
Cdd:PRK07798 272 ITIVGDaMARPLLDalEARGPYDLSSLF--AIASGgalFSPSVKEALLELLPNVVLTDSIGSSE---TGFGGSGTVakGA 346

                 ....
gi 755503902 299 VGRA 302
Cdd:PRK07798 347 VHTG 350
PRK05691 PRK05691
peptide synthase; Validated
117-284 4.59e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 46.70  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  117 ADQVDEPVPgYLSAPQNimdTCLYIFTSGTTGLPKAARISHLKV-LQCQGFYHLCGVHQEDViylALPLYHM-----SGS 190
Cdd:PRK05691 2319 AAYSDAPLP-FLSLPQH---QAYLIYTSGSTGKPKGVVVSHGEIaMHCQAVIERFGMRADDC---ELHFYSInfdaaSER 2391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  191 LLGIVGClgiGATVVLKpkfsASQFWDD---CQ---KHRVTVF----QYIGELCRYLVNQPPSKAecdhkVRLAV--GSG 258
Cdd:PRK05691 2392 LLVPLLC---GARVVLR----AQGQWGAeeiCQlirEQQVSILgftpSYGSQLAQWLAGQGEQLP-----VRMCItgGEA 2459
                         170       180
                  ....*....|....*....|....*.
gi 755503902  259 LRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:PRK05691 2460 LTGEHLQRIRQAFAPQLFFNAYGPTE 2485
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
108-437 5.70e-05

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 45.91  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 108 GISNL---LSEAADQvdepvpGYLSAPQnIMDTCLYIFTSGTTGLPKAARISH-LKVLQCQGFYHLCGVHQEDVIYLALP 183
Cdd:cd05910   62 GRKNLkqcLQEAEPD------AFIGIPK-ADEPAAILFTSGSTGTPKGVVYRHgTFAAQIDALRQLYGIRPGEVDLATFP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 184 LYHMSGSLLGIvgclgigATVV-----LKPKFSASQF-WDDCQKHRVT-------VFQYIGELCRYLVNQPPSkaecdhk 250
Cdd:cd05910  135 LFALFGPALGL-------TSVIpdmdpTRPARADPQKlVGAIRQYGVSivfgspaLLERVARYCAQHGITLPS------- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 251 VR--LAVGSGLRPDTWERFLRRFGP-LQILETYGMTE-------GNVATFNYTGRQGAVGRASWLyKHIFPFSLIRYDVM 320
Cdd:cd05910  201 LRrvLSAGAPVPIALAARLRKMLSDeAEILTPYGATEalpvssiGSRELLATTTAATSGGAGTCV-GRPIPGVRVRIIEI 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 321 TGEPIRNAQG-HCMttSPGEPGLLVAPVSQQSP-FLGYAGAPELAKDKLLKDVFWSgdvffNTGDLLVCDEQGFLHFHDR 398
Cdd:cd05910  280 DDEPIAEWDDtLEL--PRGEIGEITVTGPTVTPtYVNRPVATALAKIDDNSEGFWH-----RMGDLGYLDDEGRLWFCGR 352
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 755503902 399 TGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPG 437
Cdd:cd05910  353 KAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG 391
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
139-478 5.89e-05

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 46.02  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAarishlkVLQCQGFYhLCGV----------HQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL- 206
Cdd:cd05966  234 LFIlYTSGSTGKPKG-------VVHTTGGY-LLYAattfkyvfdyHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMf 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 --KPKF-SASQFWDDCQKHRVTVFqY-----IGELCRYlVNQPPSKaeCDHK-VRL--AVGSGLRPDTWERFLRRFGP-- 273
Cdd:cd05966  306 egTPTYpDPGRYWDIVEKHKVTIF-YtaptaIRALMKF-GDEWVKK--HDLSsLRVlgSVGEPINPEAWMWYYEVIGKer 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEgnvatfnyTG------RQGAV----GRASwlykhiFPFSLIRYDVM--TGEPIRNAQGhcmttspgepG 341
Cdd:cd05966  382 CPIVDTWWQTE--------TGgimitpLPGATplkpGSAT------RPFFGIEPAILdeEGNEVEGEVE----------G 437
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 342 LLVAPVSQQSPFLGYAGAPElakdkLLKDVFWS--GDVFFnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:cd05966  438 YLVIKRPWPGMARTIYGDHE-----RYEDTYFSkfPGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL 511
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755503902 420 ETLDFLQEVNIYGVTvpgHE--GRAGMAALALRP--PQALNLVQ-LYSHVSENLPPYARPRFLR 478
Cdd:cd05966  512 VAHPAVAEAAVVGRP---HDikGEAIYAFVTLKDgeEPSDELRKeLRKHVRKEIGPIATPDKIQ 572
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
142-417 6.90e-05

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 45.54  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQEDVIyLALPLYH-----------MSGSLLGIVG-------CLG 199
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHrslyLQSLSLRTTDSLAVTHGESFL-CCVPIYHvlswgvplaafMSGTPLVFPGpdlsaptLAK 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 200 IGATVVLKPKFSASQFWddcqkhrvtvfqyIGELCRYLVNqPPSKAECdhKVRLAVGSGLRP---DTWERflrRFGpLQI 276
Cdd:PRK05620 267 IIATAMPRVAHGVPTLW-------------IQLMVHYLKN-PPERMSL--QEIYVGGSAVPPiliKAWEE---RYG-VDV 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 LETYGMTE----GNVATfnytGRQGAVGRASWLYKHI---FPFSLiRYDVMTgepirnaQGHCMTTS---PGE---PGLL 343
Cdd:PRK05620 327 VHVWGMTEtspvGTVAR----PPSGVSGEARWAYRVSqgrFPASL-EYRIVN-------DGQVMESTdrnEGEiqvRGNW 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 344 VAPVSQQSPFLGYAGAPELAKDKLLKDV--FWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKG--------EN--VA 411
Cdd:PRK05620 395 VTASYYHSPTEEGGGAASTFRGEDVEDAndRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGewiysaqlENyiMA 474

                 ....*.
gi 755503902 412 TTEVAE 417
Cdd:PRK05620 475 APEVVE 480
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
139-475 9.46e-05

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 45.14  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYIFTSGTTGLPKAARISHLKVLQC-QGFYHLCGVHQEDVIYLA-LPLYHMSGSLLgIVGCLGIGATVVLKPKFSASQFW 216
Cdd:cd17632  227 LLIYTSGSTGTPKGAMYTERLVATFwLKVSSIQDIRPPASITLNfMPMSHIAGRIS-LYGTLARGGTAYFAAASDMSTLF 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 217 DDCQKHRVT-----------VFQ-YIGELCRYLVN-------QPPSKAECDHKV---RLA---VGSGLRPDTWERFLRRF 271
Cdd:cd17632  306 DDLALVRPTelflvprvcdmLFQrYQAELDRRSVAgadaetlAERVKAELRERVlggRLLaavCGSAPLSAEMKAFMESL 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 272 GPLQILETYGMTEGNVATFNytgrqGAVGRASWL-YKHIfpfsliryDVmtgePirnAQGHCMTTSPGEPGLLVapVSQQ 350
Cdd:cd17632  386 LDLDLHDGYGSTEAGAVILD-----GVIVRPPVLdYKLV--------DV----P---ELGYFRTDRPHPRGELL--VKTD 443
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 351 SPFLGYAGAPELAkdkllKDVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRW-KGENVATTEVAEVLETLDFLQEVN 429
Cdd:cd17632  444 TLFPGYYKRPEVT-----AEVF-DEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIF 517
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 430 IYG---------VTVPGHEGRAGMAALALRPPQALNLVQLYShvSENLPPYARPR 475
Cdd:cd17632  518 VYGnserayllaVVVPTQDALAGEDTARLRAALAESLQRIAR--EAGLQSYEIPR 570
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
263-475 1.10e-04

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 44.99  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 263 TWERFLR--RFGPLQILETYGMTE--GNVATfnytgrqgavgraswlykhIFPFSLIRYDVMTGEPIRNAQghcMTTSPG 338
Cdd:PRK07445 242 AWPSLLEqaRQLQLRLAPTYGMTEtaSQIAT-------------------LKPDDFLAGNNSSGQVLPHAQ---ITIPAN 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 339 EPGLLVapVSQQSPFLGYAgaPElakdkllkdvFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEV 418
Cdd:PRK07445 300 QTGNIT--IQAQSLALGYY--PQ----------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAA 365
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 419 LETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQaLNLVQLYSHVSENLPPYARPR 475
Cdd:PRK07445 366 ILATGLVQDVCVLGLPDP-HWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPK 420
PRK03584 PRK03584
acetoacetate--CoA ligase;
139-227 1.63e-04

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 44.40  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKA-------ARISHLKVLQcqgfYHlCGVHQEDVI-YLALPLYHMSGSLlgiVGCLGIGATVVL--- 206
Cdd:PRK03584 266 LWIlYSSGTTGLPKCivhghggILLEHLKELG----LH-CDLGPGDRFfWYTTCGWMMWNWL---VSGLLVGATLVLydg 337
                         90       100
                 ....*....|....*....|....
gi 755503902 207 ---KPKFSAsqFWDDCQKHRVTVF 227
Cdd:PRK03584 338 spfYPDPNV--LWDLAAEEGVTVF 359
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
136-284 1.95e-04

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 44.13  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYH-LCGVHQEDVIYLA-LPLYH-----------MSGSLLG-------- 193
Cdd:cd17639   89 DLACIMYTSGSTGNPKGVMLTHGNLVAgIAGLGDrVPELLGPDDRYLAyLPLAHifelaaenvclYRGGTIGygsprtlt 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 194 ---IVGCLgiGATVVLKPKFSAS--QFWDDCQK-----------HRVTVFQYIGELCRYLVNQPPSKAECD----HKVRL 253
Cdd:cd17639  169 dksKRGCK--GDLTEFKPTLMVGvpAIWDTIRKgvlaklnpmggLKRTLFWTAYQSKLKALKEGPGTPLLDelvfKKVRA 246
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755503902 254 AVGSGLR----------PDTwERFLRRF-GPlqILETYGMTE 284
Cdd:cd17639  247 ALGGRLRymlsggaplsADT-QEFLNIVlCP--VIQGYGLTE 285
PRK08162 PRK08162
acyl-CoA synthetase; Validated
142-419 2.05e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 44.17  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHL-KVLQCQGFYHLCGVHQEDViYL-ALPLYHMSGSLLGIVGCLGIGATVVLKpKFSASQFWDDC 219
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRgAYLNALSNILAWGMPKHPV-YLwTLPMFHCNGWCFPWTVAARAGTNVCLR-KVDPKLIFDLI 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 220 QKHRVTvfqyigELC------RYLVNQPPS-KAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE--GNV--- 287
Cdd:PRK08162 267 REHGVT------HYCgapivlSALINAPAEwRAGIDHPVHAMVAGAAPPAAVIAKMEEIG-FDLTHVYGLTEtyGPAtvc 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 --------------ATFNytGRQGavgraswlykhifpfslIRY---------DVMTGEPIrNAQGHCMttspGE---PG 341
Cdd:PRK08162 340 awqpewdalplderAQLK--ARQG-----------------VRYplqegvtvlDPDTMQPV-PADGETI----GEimfRG 395
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 342 LLVAPvsqqspflGYagapeLAKDKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK08162 396 NIVMK--------GY-----LKNPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
PRK05691 PRK05691
peptide synthase; Validated
76-455 2.50e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 44.39  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902   76 LVEFLESLEPDL--------PALRAMGLHLWATGPEtnVAGISNLLSEAADQVDEP-VPGylsapqniMDTCLYIFTSGT 146
Cdd:PRK05691  108 LLSIIADAEPRLlltvadlrDSLLQMEELAAANAPE--LLCVDTLDPALAEAWQEPaLQP--------DDIAFLQYTSGS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  147 TGLPKAARISHL-----KVLQCQGFYhlCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLkpkFSASQFWDDCQK 221
Cdd:PRK05691  178 TALPKGVQVSHGnlvanEQLIRHGFG--IDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL---MSPAYFLERPLR 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  222 HRVTVFQYIG----------ELCRYLVNQPPSKAECDHKVRLAVgSG---LRPDTWERFLRRFG-----PLQILETYGMT 283
Cdd:PRK05691  253 WLEAISEYGGtisggpdfayRLCSERVSESALERLDLSRWRVAY-SGsepIRQDSLERFAEKFAacgfdPDSFFASYGLA 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  284 EgnvATFNYTGRQGAVGRASwLYKHIFPFSLIRYDVMTGEPIRNaqghCMTTSPGEPGLLVAPVSQQ------------- 350
Cdd:PRK05691  332 E---ATLFVSGGRRGQGIPA-LELDAEALARNRAEPGTGSVLMS----CGRSQPGHAVLIVDPQSLEvlgdnrvgeiwas 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902  351 --SPFLGYAGAPElAKDKLLkdVFWSGDVFFNTGDLLVCDEqGFLHFHDRTGDTFRWKGENVATTEVAEVLET-LDFLQE 427
Cdd:PRK05691  404 gpSIAHGYWRNPE-ASAKTF--VEHDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEReVEVVRK 479
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 755503902  428 --VNIYGVTVPGHEGrAGMAALALR------PPQAL 455
Cdd:PRK05691  480 grVAAFAVNHQGEEG-IGIAAEISRsvqkilPPQAL 514
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
139-475 2.81e-04

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 43.84  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAarishlkVLQCQGFY---------HLCGVHQEDVIYlalplyhmSGSLLGIV--------GCLGI 200
Cdd:cd05967  233 LYIlYTSGTTGKPKG-------VVRDNGGHavalnwsmrNIYGIKPGDVWW--------AASDVGWVvghsyivyGPLLH 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 201 GATVVL---KPKFS--ASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE---CD---HKVRLAVGSGLRPDTWErFLR 269
Cdd:cd05967  298 GATTVLyegKPVGTpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikkYDlssLRTLFLAGERLDPPTLE-WAE 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 270 RFGPLQILETYGMTE-GNVATFNYTG------RQGAVGRaswlykhifpfSLIRYDVM----TGEPIR-NAQGHCMTTSP 337
Cdd:cd05967  377 NTLGVPVIDHWWQTEtGWPITANPVGleplpiKAGSPGK-----------PVPGYQVQvldeDGEPVGpNELGNIVIKLP 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 338 GEPGLLvapvsqqspflgyagaPELAK-DKLLKDVFWSGDV-FFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEV 415
Cdd:cd05967  446 LPPGCL----------------LTLWKnDERFKKLYLSKFPgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEM 509
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 416 AEVLETLDFLQEVNIYGVtvpgHEGRAGMAALAL--------RPPQALnLVQLYSHVSENLPPYARPR 475
Cdd:cd05967  510 EESVLSHPAVAECAVVGV----RDELKGQVPLGLvvlkegvkITAEEL-EKELVALVREQIGPVAAFR 572
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
141-480 3.70e-04

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 43.01  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIylaLPLYHMS--GSLLGIVGCLGIGATVVLKPK---FSASQ 214
Cdd:cd17652   99 IYTSGSTGRPKGVVVTHRGLANlAAAQIAAFDVGPGSRV---LQFASPSfdASVWELLMALLAGATLVLAPAeelLPGEP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVfqyigelcrylVNQPPS-----KAECDHKVRLAVGSGLRP-----DTWERFlRRFgplqiLETYGMTE 284
Cdd:cd17652  176 LADLLREHRITH-----------VTLPPAalaalPPDDLPDLRTLVVAGEACpaelvDRWAPG-RRM-----INAYGPTE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 gnvATFNYTGRQGAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMTTS-----PGEPG-LLVApvsqqSPFL--GY 356
Cdd:cd17652  239 ---TTVCATMAGPLPGGGV---------------PPIGRPVPGTRVYVLDARlrpvpPGVPGeLYIA-----GAGLarGY 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLKDVF-WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEvniygVTV 435
Cdd:cd17652  296 LNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-----AVV 370
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 755503902 436 PGHEGRAGMAALAL----RPPQALNLVQLYSHVSENLPPYARPR-FLRLQ 480
Cdd:cd17652  371 VVRDDRPGDKRLVAyvvpAPGAAPTAAELRAHLAERLPGYMVPAaFVVLD 420
PRK08308 PRK08308
acyl-CoA synthetase; Validated
371-474 3.91e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 43.10  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 371 VFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYgvtvPGHEGRAG-MAALAL 449
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY----RGKDPVAGeRVKAKV 360
                         90       100
                 ....*....|....*....|....*
gi 755503902 450 RPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQHLAPYQVP 385
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
133-204 5.37e-04

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 42.73  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 133 NIMDT------CLYIFTSGTTGLPKAARISHLKVL-----QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIG 201
Cdd:cd05933  142 AIISSqkpnqcCTLIYTSGTTGMPKGVMLSHDNITwtakaASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVG 221

                 ...
gi 755503902 202 ATV 204
Cdd:cd05933  222 GQV 224
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
142-419 1.04e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 41.80  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHLKVLQ--CQGFYHLcGVHQEDVIY-LALPLYhMSGSLLGIVGCLGIGAT-VVLKPKFSASQFWD 217
Cdd:PRK04319 212 YTSGSTGKPKGVLHVHNAMLQhyQTGKYVL-DLHEDDVYWcTADPGW-VTGTSYGIFAPWLNGATnVIDGGRFSPERWYR 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 218 DCQKHRVTVFQYIGELCRYLVNQPPSKAEC-DHK-VR--LAVGSGLRPD--TWERflRRFGpLQILETYGMTE-GNVATF 290
Cdd:PRK04319 290 ILEDYKVTVWYTAPTAIRMLMGAGDDLVKKyDLSsLRhiLSVGEPLNPEvvRWGM--KVFG-LPIHDNWWMTEtGGIMIA 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 NYTG---RQGAVGRaswlykhifPFSLIRYDVMTgepiRNAQGhcmtTSPGEPGLLVAPVSQQSPFLGYAGAPElakdkL 367
Cdd:PRK04319 367 NYPAmdiKPGSMGK---------PLPGIEAAIVD----DQGNE----LPPNRMGNLAIKKGWPSMMRGIWNNPE-----K 424
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755503902 368 LKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK04319 425 YESYFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKL 474
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
141-288 1.86e-03

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 41.03  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQ-----CQGFyhlcGVhQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKfsasqf 215
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSftnwmLEDF----AL-PEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPK------ 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 wddcqkhrvTVFQYIGELCRYLVNQP-------PSKAE-C--------DHKVRLAV----GSGLRPDTWERFLRRFGPLQ 275
Cdd:PRK04813 218 ---------DMTANFKQLFETLPQLPinvwvstPSFADmClldpsfneEHLPNLTHflfcGEELPHKTAKKLLERFPSAT 288
                        170
                 ....*....|...
gi 755503902 276 ILETYGMTEGNVA 288
Cdd:PRK04813 289 IYNTYGPTEATVA 301
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
103-432 1.86e-03

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 40.88  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 103 ETNVAGISNLLSEAADQVD-EPVPGYLSA------PQNIMDTCLYI---FTSGTTGLPKAARISHlkvlqcQGFY---HL 169
Cdd:cd05915  111 EAIRGELKTVQHFVVMDEKaPEGYLAYEEalgeeaDPVRVPERAACgmaYTTGTTGLPKGVVYSH------RALVlhsLA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 170 CGVHQEDV-----IYL-ALPLYHMSG-SLLGIVGCLGiGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPP 242
Cdd:cd05915  185 ASLVDGTAlsekdVVLpVVPMFHVNAwCLPYAATLVG-AKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLE 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 243 S-KAECDHKVRLAVGSGLRPDTWERfLRRFGPLQILETYGMTEGNvatfnytgrqgAVGRAS-WL--YKHIFPFSLIRYD 318
Cdd:cd05915  264 StGHRLKTLRRLVVGGSAAPRSLIA-RFERMGVEVRQGYGLTETS-----------PVVVQNfVKshLESLSEEEKLTLK 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 319 VMTG-----EPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYagapelAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFL 393
Cdd:cd05915  332 AKTGlpiplVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGY------YGNEEATRSALTPDGFFRTGDIAVWDEEGYV 405
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 755503902 394 HFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYG 432
Cdd:cd05915  406 EIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
129-170 7.18e-03

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 39.06  E-value: 7.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755503902 129 SAPQNIMdtclY-IFTSGTTGLPKAARISHLKVlqCQGFYHLC 170
Cdd:cd05918  103 SSPSDAA----YvIFTSGSTGKPKGVVIEHRAL--STSALAHG 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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