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Conserved domains on  [gi|20138445|sp|Q9XS79|]
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RecName: Full=5-aminolevulinate synthase, non-specific, mitochondrial; Short=ALAS-H; AltName: Full=5-aminolevulinic acid synthase 1; AltName: Full=Delta-ALA synthase 1; AltName: Full=Delta-aminolevulinate synthase 1; Flags: Precursor

Protein Classification

Preseq_ALAS and KBL_like domain-containing protein( domain architecture ID 11181659)

Preseq_ALAS and KBL_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 197-602 0e+00

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member TIGR01821:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 402  Bit Score: 666.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   197 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDYSDSlvTKKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTG 276
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   277 AGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIWNSRVPKYIY 356
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   357 RHNDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKM 436
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   437 DIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEgrVLRRQHQRNVKLMRQMLM 516
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   517 DASLPVVHCPSHIIPVRVADAAKNTEVCNELMSRHNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKR 596
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 20138445   597 VGLELK 602
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-138 5.54e-55

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


:

Pssm-ID: 462658  Cd Length: 114  Bit Score: 182.69  E-value: 5.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445     2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSASAVLCQQVKE-TPPANEKDKTAKAkvqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 20138445    81 gsqqtpdgtqLPSGHPSLAASQGTASKCPFLAAQMSQGGSSVFCKASLELQEDVQEMH 138
Cdd:pfam09029  67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 197-602 0e+00

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 666.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   197 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDYSDSlvTKKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTG 276
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   277 AGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIWNSRVPKYIY 356
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   357 RHNDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKM 436
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   437 DIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEgrVLRRQHQRNVKLMRQMLM 516
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   517 DASLPVVHCPSHIIPVRVADAAKNTEVCNELMSRHNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKR 596
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 20138445   597 VGLELK 602
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 243-588 3.98e-178

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 509.02  E-value: 3.98e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 243 KQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 323 LakMMPGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELLQRSD-PAVPKIVAFETVHSMDGAVCPLEELCDVA 401
Cdd:cd06454  81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 402 HEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPML 481
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 482 LAGALESVRILKSteGRVLRRQHQRNVKLMRQMLMDASLPVVHCPSHIIPVRVAD-AAKNTEVCNELMSRhNIYVQAINY 560
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315

                       330       340
                ....*....|....*....|....*...
gi 20138445 561 PTVRRGEELLRIAPTPHHTPQMMNYFVE 588
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLE 343
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 197-608 5.53e-175

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 503.62  E-value: 5.53e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  197 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDYSDSlvTKKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTG 276
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  277 AGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIWNSRVPKYIY 356
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  357 RHNDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKM 436
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  437 DIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEGRvlRRQHQRNVKLMRQMLM 516
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  517 DASLPVVHCPSHIIPVRVADAAKNTEVCNELMSRHNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKR 596
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 20138445  597 VGLELKPHSSAE 608
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 199-596 2.34e-162

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 470.30  E-value: 2.34e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 199 YDHFFEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDysdslvtkKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAG 278
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 279 GTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIWNSRVPKYIYRH 358
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 359 NDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDI 438
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 439 ISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEGRvlRRQHQRNVKLMRQMLMDA 518
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20138445 519 SLPVVHCPSHIIPVRVADAAKNTEVCNELMSRhNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKR 596
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
248-588 2.09e-67

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 224.11  E-value: 2.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   248 WCSNDYLGMSCHprvcgAVMDTLKQHGtgAGGTRNISGTSKFHVDLEQELADLHG--------KDAALLFSSCFVANDST 319
Cdd:pfam00155   6 LGSNEYLGDTLP-----AVAKAEKDAL--AGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   320 LFTLAKMmPGCEIYSDSGNHASMIQGIWNSRVPKYIYR-------HNDVDHLRELLQRSdpavPKIVAFETVHSMDGAVC 392
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   393 PLEELCDVA---HEFGAITFVDEVHAVGLYGAQGGgIGDRDGVMPKMD-IISGTLGKAFGCVG---GYIASTSSLIDTIR 465
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   466 SYAAGFIFTTSLPPMLLAGALESvrILKSTEGRVLRRQHQRNVKLMRQMLMDASLPVVHCPSHIIPVRVADAAKNTEVCN 545
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 20138445   546 ELMSRHNIYVQAINYPTVrrgEELLRIAPTpHHTPQMMNYFVE 588
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGV---PGWLRITVA-GGTEEELEELLE 349
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-138 5.54e-55

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 182.69  E-value: 5.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445     2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSASAVLCQQVKE-TPPANEKDKTAKAkvqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 20138445    81 gsqqtpdgtqLPSGHPSLAASQGTASKCPFLAAQMSQGGSSVFCKASLELQEDVQEMH 138
Cdd:pfam09029  67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 197-602 0e+00

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 666.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   197 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDYSDSlvTKKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTG 276
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   277 AGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIWNSRVPKYIY 356
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   357 RHNDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKM 436
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   437 DIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEgrVLRRQHQRNVKLMRQMLM 516
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   517 DASLPVVHCPSHIIPVRVADAAKNTEVCNELMSRHNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKR 596
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 20138445   597 VGLELK 602
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 243-588 3.98e-178

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 509.02  E-value: 3.98e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 243 KQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 323 LakMMPGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELLQRSD-PAVPKIVAFETVHSMDGAVCPLEELCDVA 401
Cdd:cd06454  81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 402 HEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPML 481
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 482 LAGALESVRILKSteGRVLRRQHQRNVKLMRQMLMDASLPVVHCPSHIIPVRVAD-AAKNTEVCNELMSRhNIYVQAINY 560
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315

                       330       340
                ....*....|....*....|....*...
gi 20138445 561 PTVRRGEELLRIAPTPHHTPQMMNYFVE 588
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLE 343
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 197-608 5.53e-175

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 503.62  E-value: 5.53e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  197 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDYSDSlvTKKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTG 276
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  277 AGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIWNSRVPKYIY 356
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  357 RHNDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKM 436
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  437 DIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEGRvlRRQHQRNVKLMRQMLM 516
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  517 DASLPVVHCPSHIIPVRVADAAKNTEVCNELMSRHNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKR 596
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 20138445  597 VGLELKPHSSAE 608
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 199-596 2.34e-162

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 470.30  E-value: 2.34e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 199 YDHFFEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDysdslvtkKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAG 278
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 279 GTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIWNSRVPKYIYRH 358
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 359 NDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDI 438
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 439 ISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEGRvlRRQHQRNVKLMRQMLMDA 518
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20138445 519 SLPVVHCPSHIIPVRVADAAKNTEVCNELMSRhNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKR 596
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 203-590 1.66e-96

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 301.31  E-value: 1.66e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  203 FEKKIDEKKNDHTYRVFKTVNRRAQFFPMADDysdslvtkKQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRN 282
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  283 ISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVD 362
Cdd:PRK05958  79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  363 HLRELLQRSDPAvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIIS-G 441
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILvG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  442 TLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPMLLAGALESVRILKSTEGrvlRRQH-QRNVKLMRQMLMDASL 520
Cdd:PRK05958 236 TLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  521 PVVHCPSHIIPVRVADAAKNTEVCNELmSRHNIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENL 590
Cdd:PRK05958 313 QLMDSQSAIQPLIVGDNERALALAAAL-QEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEAL 381
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 243-581 3.94e-96

8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273303 [Multi-domain]  Cd Length: 360  Bit Score: 299.57  E-value: 3.94e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   243 KQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   323 LAKmmPGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELLQRSDPAVPKIVAFETVHSMDGAVCPLEELCDVAH 402
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   403 EFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIIS-GTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPPML 481
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   482 LAGALESVRILKstEGRVLRRQHQRNVKLMRQMLMDASLPVVHCPSHIIPVRVADAAKNTEVCNELMSRhNIYVQAINYP 561
Cdd:TIGR00858 254 AAAALAALELIQ--EEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ-GIFVGAIRPP 330

                         330       340
                  ....*....|....*....|
gi 20138445   562 TVRRGEELLRIAPTPHHTPQ 581
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPG 350
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 243-602 1.79e-88

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 280.93  E-value: 1.79e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  243 KQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:PRK06939  42 KEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFET 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  323 LakMMPGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELLQ--RSDPAVPKIVAFETVHSMDGAVCPLEELCDV 400
Cdd:PRK06939 122 L--LGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKeaKEAGARHKLIATDGVFSMDGDIAPLPEICDL 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  401 AHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIISGTLGKAF-GCVGGYIASTSSLIDTIRSYAAGFIFTTSLPP 479
Cdd:PRK06939 200 ADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAP 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  480 MLLAGALESVRILKstEGRVLRRQHQRNVKLMRQMLMDASLPVVHCPSHIIPVRVADAAKNTEVCNELMSRhNIYVQAIN 559
Cdd:PRK06939 280 AIVAASIKVLELLE--ESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFS 356

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 20138445  560 YPTVRRGEELLRIAPTPHHTPQMmnyfVENLLATWKRVGLELK 602
Cdd:PRK06939 357 FPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFEKVGKELG 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
248-588 2.09e-67

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 224.11  E-value: 2.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   248 WCSNDYLGMSCHprvcgAVMDTLKQHGtgAGGTRNISGTSKFHVDLEQELADLHG--------KDAALLFSSCFVANDST 319
Cdd:pfam00155   6 LGSNEYLGDTLP-----AVAKAEKDAL--AGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   320 LFTLAKMmPGCEIYSDSGNHASMIQGIWNSRVPKYIYR-------HNDVDHLRELLQRSdpavPKIVAFETVHSMDGAVC 392
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   393 PLEELCDVA---HEFGAITFVDEVHAVGLYGAQGGgIGDRDGVMPKMD-IISGTLGKAFGCVG---GYIASTSSLIDTIR 465
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445   466 SYAAGFIFTTSLPPMLLAGALESvrILKSTEGRVLRRQHQRNVKLMRQMLMDASLPVVHCPSHIIPVRVADAAKNTEVCN 545
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 20138445   546 ELMSRHNIYVQAINYPTVrrgEELLRIAPTpHHTPQMMNYFVE 588
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGV---PGWLRITVA-GGTEEELEELLE 349
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-138 5.54e-55

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 182.69  E-value: 5.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445     2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSASAVLCQQVKE-TPPANEKDKTAKAkvqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 20138445    81 gsqqtpdgtqLPSGHPSLAASQGTASKCPFLAAQMSQGGSSVFCKASLELQEDVQEMH 138
Cdd:pfam09029  67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 243-581 2.97e-45

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 167.54  E-value: 2.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  243 KQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  323 L--------AKMMP----GCEIYSDSGNHASMIQGIW----NSRVPKYIYRHNDVDHLRELLQrSDPAVPKIVAFETVHS 386
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLS-SCKMKRKVVVTDSLFS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  387 MDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTIRS 466
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  467 YAAGFIFTTSLPPMLLAGALESVRILKSTEGRvlRRQHQRNVKLMRQMlmdASLPVvhcPSHIIPVRVADAAKNTEVCNE 546
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 20138445  547 LMsRHNIYVQAINYPTVRRGEELLRIAPTPHHTPQ 581
Cdd:PLN02955 413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
PLN02483 PLN02483
serine palmitoyltransferase
 250-563 2.76e-44

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 165.32  E-value: 2.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  250 SNDYLGMS-----CHPRVcgavMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLa 324
Cdd:PLN02483 107 SYNYLGFAaadeyCTPRV----IESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  325 kMMPGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELLQ--------RSDPAVPKI-VAFETVHSMDGAVCPLE 395
Cdd:PLN02483 182 -IGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGELCKLP 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  396 ELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPK-MDIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFT 474
Cdd:PLN02483 261 EIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYA 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  475 TSLPPMLLAGALESVRILKSTEG-----RVLRRQHQrNVKLMRQMLMDASLPVV-HCPSHIIPVRVADAAKNTEVCNELM 548
Cdd:PLN02483 341 TSMSPPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECL 419

                        330
                 ....*....|....*
gi 20138445  549 SRhNIYVQAINYPTV 563
Cdd:PLN02483 420 KQ-NVAVVVVGFPAT 433
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
250-603 3.70e-44

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 162.87  E-value: 3.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  250 SNDYLGMSCHPRVCGAVMDTLKQHGtgaggtRNISGTSKFHVD------LEQELADLHGKDAALLFSSCFVANDSTLFTL 323
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEG------DSLVMSAVFLHDdspkpqFEKKLAAFTGFESCLLCQSGWAANVGLLQTI 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  324 AKmmPGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELLQRSDPAvpkIVAFETVHSMDGAVCPLEELCDVAHE 403
Cdd:PRK07179 135 AD--PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEE 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  404 FGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTIR--SYAAgfIFTTSLPPML 481
Cdd:PRK07179 210 FGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHE 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  482 LAGALESVRILKSTEGRvlRRQHQRNVKLMRQMLMDASLPvVHCPSHIIPVrVADAAKNTEVCNELMSRHNIYVQAINYP 561
Cdd:PRK07179 288 IAGLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLRDALEERNVFGAVFCAP 363

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 20138445  562 TVRRGEELLRIAPTPHHTPQMMNYFVENLLATWKRVGLELKP 603
Cdd:PRK07179 364 ATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 247-553 1.65e-33

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 132.34  E-value: 1.65e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  247 VWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFTLAKM 326
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  327 mpGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELL----------QRSDPAVPKIVAFETVHSMDGAVCPLEE 396
Cdd:PLN03227  82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  397 LCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMP--KMDIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFT 474
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  475 TSLPPMLLAGALESVRILKSTEgRVLRRQHQrNVKLMRQMLMDASLPVVHCP-----------SHIIPVRVADAAKnTEV 543
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316

                        330
                 ....*....|
gi 20138445  544 CNELMSRHNI 553
Cdd:PLN03227 317 TDETLILDQI 326
PLN02822 PLN02822
serine palmitoyltransferase
 243-517 5.17e-32

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 129.86  E-value: 5.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  243 KQVSVWCSNDYLGMSCHPRVCGAVMDTLKQHGTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:PLN02822 109 KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPA 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  323 LAKMmpGCEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLR---ELLQRSDPAVPKI---VAFETVHSMDGAVCPLEE 396
Cdd:PLN02822 189 FCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRntlEKLTAENKRKKKLrryIVVEAIYQNSGQIAPLDE 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  397 LCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMP-KMDIISGTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTT 475
Cdd:PLN02822 267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIeKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSA 346

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 20138445  476 SLPPMLLAGALESVRILKSTEGrVLRRQHQrNVKLMRQMLMD 517
Cdd:PLN02822 347 SLPPYLASAAITAIDVLEDNPS-VLAKLKE-NIALLHKGLSD 386
PRK07505 PRK07505
hypothetical protein; Provisional
 249-590 2.03e-29

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 120.85  E-value: 2.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  249 CSNDYLGMSCHPRVCGAVMDTLKqhgtgAGGTRNISgTSKFHV------DLEQELADLHGKDAaLLFSSCFVANDSTLFT 322
Cdd:PRK07505  52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  323 LAK--MMPGCEIYS--DSGNHASM--IQGIWNSRVPKYIYRHNDVDHLRELLQRSdpavpKIVAF--ETVHSMdGAVCPL 394
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSM-GGIAPV 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  395 EELCDVAHEFGAITFVDEVHAVGLYGAQGGG--IGDRDGVMPKMDIISGTLGKAFGCVGGYIA-STSSLIDTIRSYAAGF 471
Cdd:PRK07505 199 KELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPL 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  472 IFTTSLPPMLLAGALESVRILKSTEGRVLRRQHQRNVKLMRQmLMDASLPVVHCPSHIIPVRVADAAKNTevCNELMSRh 551
Cdd:PRK07505 279 AFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDS-LIPTEQSGSFLPIRLIYIGDEDTAIKA--AKQLLDR- 354

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 20138445  552 NIYVQAINYPTVRRGEELLRIAPTPHHTPQMMNYFVENL 590
Cdd:PRK07505 355 GFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLL 393
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 250-503 7.33e-22

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 97.93  E-value: 7.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  250 SNDYLGMSCHPRVCGAVMDTLKQH-------GTGAGGTRNISGTSKFHVDLEQELADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  323 LAKMMPgcEIYSDSGNHASMIQGIWNSRVPKYIYRHNDVDHLRELLQrSDPAVPKIVAF---ETVHSMDGAVCPLEELCD 399
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLE-SCRQRSFGRIFifvCSVYSFKGTLAPLEQIIA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  400 VAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGVMPKMDIISgTLGKAFGCVGGYIASTSSLIDTIRSYAAGFIFTTSLPP 479
Cdd:PRK05937 168 LSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPP 246

                        250       260
                 ....*....|....*....|....
gi 20138445  480 MLLAGALESVRILkSTEGRVLRRQ 503
Cdd:PRK05937 247 HLLISIQVAYDFL-SQEGELARKQ 269
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 289-452 1.38e-13

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 68.95  E-value: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 289 FHVDLEQELADL--HGKDAALLFSSCFVANDSTLFTLAkmMPGCEIYSDSGNHAS-------MIQGIWNS-RVPKYIYRH 358
Cdd:cd01494   1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSrywvaaeLAGAKPVPvPVDDAGYGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 359 NDVDHLRELLqRSDPavPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGAQGGGIGDRDGvmpkmDI 438
Cdd:cd01494  79 LDVAILEELK-AKPN--VALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA-----DV 150

                       170
                ....*....|....
gi 20138445 439 ISGTLGKAFGCVGG 452
Cdd:cd01494 151 VTFSLHKNLGGEGG 164
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 293-411 1.15e-06

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 51.05  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 293 LEQELADLHGKDAALLFSSCFVANDSTLFTLAK-----MMPGCeIYSDSGNHASMIQGIWNSRVpkyiyRHNDVDHLREL 367
Cdd:cd00614  45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERLLPKLGIEV-----TFVDPDDPEAL 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 20138445 368 LQRSDPAVpKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVD 411
Cdd:cd00614 119 EAAIKPET-KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
360-417 2.10e-06

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 50.52  E-value: 2.10e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20138445 360 DVDHLRELLqrsDPAVpKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 417
Cdd:COG0520 143 DLEALEALL---TPRT-KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 394-555 3.86e-05

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 46.18  E-value: 3.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 394 LEELCDVAHEFGAITFVDEVHA----VGLYGAQGGGIGDRDGVmpkmdIISGTLGKAFGCVG---GYIASTSSLIdtIRS 466
Cdd:cd00609 154 LEELAELAKKHGILIISDEAYAelvyDGEPPPALALLDAYERV-----IVLRSFSKTFGLPGlriGYLIAPPEEL--LER 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 467 YAAGFIFTTSLPPMLLAGALEsvRILKSTEGRV--LRRQHQRNVKLMRQMLMDASLPVVHCPS---HI-IPVRVADAAkn 540
Cdd:cd00609 227 LKKLLPYTTSGPSTLSQAAAA--AALDDGEEHLeeLRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE-- 302

                       170
                ....*....|....*
gi 20138445 541 tEVCNELMSRHNIYV 555
Cdd:cd00609 303 -EFLERLLLEAGVVV 316
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 360-425 1.62e-03

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 41.30  E-value: 1.62e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20138445 360 DVDHLRELLQRSdpavPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDevhavglyGAQGGG 425
Cdd:cd06453 128 DLEALEKLLTER----TKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVD--------GAQSAG 181
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
394-573 2.07e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 40.89  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  394 LEELCDVAHEFGA-----IT---FVDEVHAVGLYGaqgggigdrdgvmPKMDIISGTLGKAFGCVG---GYIASTSSLID 462
Cdd:PRK06225 179 IKEFAEIARDNDAfllhdCTyrdFAREHTLAAEYA-------------PEHTVTSYSFSKIFGMAGlriGAVVATPDLIE 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445  463 TIRSYAAGFIFTTSLPPmllAGALESVRILKSTEGRVLR--RQHQRNVKLMRQMLMDASLPVVhcPSH--IIPVRVADAA 538
Cdd:PRK06225 246 VVKSIVINDLGTNVIAQ---EAAIAGLKVKDEWIDRIRRttFKNQKLIKEAVDEIEGVFLPVY--PSHgnMMVIDISEAG 320

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 20138445  539 KNTEVCNELMSRHNIYVQAINYPTVRRGEELLRIA 573
Cdd:PRK06225 321 IDPEDLVEYLLERKIFVRQGTYTSKRFGDRYIRVS 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 360-417 2.15e-03

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 40.69  E-value: 2.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 20138445   360 DVDHLRELLqrsDPAvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 417
Cdd:pfam00266 128 DLDELEKLI---TPK-TKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 295-414 9.36e-03

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 38.38  E-value: 9.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138445 295 QEL-ADLHGKDAAllfssCFVANDSTLFTLAKMM----PGCEIYSDSGNHASMIQGIWNSR-VPKYI--YRHN------- 359
Cdd:cd00615  65 QELaARAFGAKHT-----FFLVNGTSSSNKAVILavcgPGDKILIDRNCHKSVINGLVLSGaVPVYLkpERNPyygiagg 139

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20138445 360 -DVDHLRELLQRSDPAVPKIVafeTVHSMDGAVCPLEELCDVAHEFGAITFVDEVH 414
Cdd:cd00615 140 iPPETFKKALIEHPDAKAAVI---TNPTYYGICYNLRKIVEEAHHRGLPVLVDEAH 192
 
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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