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Conserved domains on  [gi|628601867|ref|NP_001278764|]
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5-aminolevulinate synthase, non-specific, mitochondrial precursor [Mus musculus]

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) ...
199-604 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: 654.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396

                  ....*.
gi 628601867  599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
2-140 2.92e-53

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: 401101  Cd Length: 114  Bit Score: 178.06  E-value: 2.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867    2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAVHCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867   81 esqmaqtpdgtqLPSGHPSPATSQGSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
Cdd:pfam09029  67 ------------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVR 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
199-604 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: 654.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396

                  ....*.
gi 628601867  599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
245-592 1.17e-177

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: 507.87  E-value: 1.17e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 403
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 404 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 484 LAGALESVRILKSseGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 562
Cdd:cd06454  239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315
                        330       340       350
                 ....*....|....*....|....*....|
gi 628601867 563 PTVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
199-610 1.32e-169

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 489.75  E-value: 1.32e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQ--TERDAHQDRVAALKAKLN 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397
                        410
                 ....*....|..
gi 628601867 599 VGLELKPHSSAE 610
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];
199-600 1.22e-136

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];


Pssm-ID: 223234 [Multi-domain]  Cd Length: 388  Bit Score: 404.71  E-value: 1.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADdytdslitKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:COG0156    1 MDFLSFLRQALQALKAEGLYRGLRALDRRQGLAIRAD--------GRKVLNFCSNDYLGLASHPELIEAAKAAIRRYGVG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:COG0156   73 AGGSRLISGTSDLHVELEEELADFLGAEAALLFSSGFVANLGLLSALLK--KGDLIFSDELNHASIIDGIRLSRAEVRRF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP 436
Cdd:COG0156  151 KHNDLDHLEALLEeaRENGARRKLIVTEGVFSMDGDIAPLPELVELAEKYGALLYVDEAHAVGVLGPNGRGLAEHFGLEP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 437 K-MDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQ 515
Cdd:COG0156  231 EeVDIIVGTLGKALGSSGGYIAGSAALIDYLRNRARPFIFSTALPPAVAAAALAALRILE--EGPERRERLQELAAFFRS 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 516 MLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLVT 595
Cdd:COG0156  309 LLKALGLVLLPSESPIIPVILGDEERALEASRALLEE-GIYVSAIRPPTVPKGTARLRITLTAAHTEED----IDRLAEA 383

                 ....*
gi 628601867 596 WKRVG 600
Cdd:COG0156  384 LSEVG 388
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
250-592 5.41e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 233.35  E-value: 5.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  250 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 321
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  322 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 394
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  395 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDgVMPKMD-IISGTLGKAFGCVG---GYIASTSLLIDTVR 467
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  468 SYAAGFIFTTSLPPMLLAGALESvrILKSSEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICD 547
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 628601867  548 ELMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNFFVEKL 592
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
2-140 2.92e-53

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: 401101  Cd Length: 114  Bit Score: 178.06  E-value: 2.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867    2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAVHCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867   81 esqmaqtpdgtqLPSGHPSPATSQGSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
Cdd:pfam09029  67 ------------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVR 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
199-604 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: 654.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396

                  ....*.
gi 628601867  599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
245-592 1.17e-177

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: 507.87  E-value: 1.17e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 403
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 404 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 484 LAGALESVRILKSseGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 562
Cdd:cd06454  239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315
                        330       340       350
                 ....*....|....*....|....*....|
gi 628601867 563 PTVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
199-610 1.32e-169

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 489.75  E-value: 1.32e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEgrALRRQHQRNVKLLRQMLM 518
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQ--TERDAHQDRVAALKAKLN 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKR 598
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397
                        410
                 ....*....|..
gi 628601867 599 VGLELKPHSSAE 610
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];
199-600 1.22e-136

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];


Pssm-ID: 223234 [Multi-domain]  Cd Length: 388  Bit Score: 404.71  E-value: 1.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADdytdslitKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 278
Cdd:COG0156    1 MDFLSFLRQALQALKAEGLYRGLRALDRRQGLAIRAD--------GRKVLNFCSNDYLGLASHPELIEAAKAAIRRYGVG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 279 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:COG0156   73 AGGSRLISGTSDLHVELEEELADFLGAEAALLFSSGFVANLGLLSALLK--KGDLIFSDELNHASIIDGIRLSRAEVRRF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 359 RHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP 436
Cdd:COG0156  151 KHNDLDHLEALLEeaRENGARRKLIVTEGVFSMDGDIAPLPELVELAEKYGALLYVDEAHAVGVLGPNGRGLAEHFGLEP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 437 K-MDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQ 515
Cdd:COG0156  231 EeVDIIVGTLGKALGSSGGYIAGSAALIDYLRNRARPFIFSTALPPAVAAAALAALRILE--EGPERRERLQELAAFFRS 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 516 MLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLVT 595
Cdd:COG0156  309 LLKALGLVLLPSESPIIPVILGDEERALEASRALLEE-GIYVSAIRPPTVPKGTARLRITLTAAHTEED----IDRLAEA 383

                 ....*
gi 628601867 596 WKRVG 600
Cdd:COG0156  384 LSEVG 388
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
205-592 1.02e-95

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 299.38  E-value: 1.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 205 FEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRN 284
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 285 ISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVN 364
Cdd:PRK05958  79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 365 HLRELLQRSDPSvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGG-GIGDRDGVMPKMDIISG 443
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRgLAAEAGLAGEPDVILVG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 444 TLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSSEGralRRQH-QRNVKLLRQMLMDAGL 522
Cdd:PRK05958 236 TLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 523 PVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:PRK05958 313 QLMDSQSAIQPLIVGDNERALALAAALQEQ-GFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEAL 381
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
245-592 1.02e-95

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: 298.41  E-value: 1.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  325 LAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAH 404
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  405 EFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIIS-GTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  484 LAGALESVRILKssEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYP 563
Cdd:TIGR00858 254 AAAALAALELIQ--EEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ-QQGIFVGAIRPP 330
                         330       340
                  ....*....|....*....|....*....
gi 628601867  564 TVPRGEELLRIAPTPHHTPQMMNFFVEKL 592
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
204-604 3.44e-90

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 285.17  E-value: 3.44e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 204 FFEKKIDEKKNDHTY---RVFKTVNRrAQIfpmaddytdSLITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 280
Cdd:PRK06939   8 QLREELEEIKAEGLYkeeRVITSPQG-ADI---------TVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 281 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 360
Cdd:PRK06939  78 SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 361 NDVNHLRELLQRSDPSVP--KIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 438
Cdd:PRK06939 156 NDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 439 DIISGTLGKAF-GCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQML 517
Cdd:PRK06939 236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE--ESDELRDRLWENARYFREGM 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 518 MDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLVTWK 597
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFE 388

                 ....*..
gi 628601867 598 RVGLELK 604
Cdd:PRK06939 389 KVGKELG 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
250-592 5.41e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 233.35  E-value: 5.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  250 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 321
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  322 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 394
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  395 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDgVMPKMD-IISGTLGKAFGCVG---GYIASTSLLIDTVR 467
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867  468 SYAAGFIFTTSLPPMLLAGALESvrILKSSEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICD 547
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 628601867  548 ELMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNFFVEKL 592
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
2-140 2.92e-53

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: 401101  Cd Length: 114  Bit Score: 178.06  E-value: 2.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867    2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAVHCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867   81 esqmaqtpdgtqLPSGHPSPATSQGSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
Cdd:pfam09029  67 ------------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVR 114
PLN02483 PLN02483
serine palmitoyltransferase
252-566 2.04e-46

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 171.10  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 252 SNDYLGMSRHPRVCGA-VMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMP 330
Cdd:PLN02483 107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 331 GCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--------RSDPSVPKI-VAFETVHSMDGAVCPLEELCD 401
Cdd:PLN02483 185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGELCKLPEIVA 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 402 VAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPK-MDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLP 480
Cdd:PLN02483 265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 481 PMLLAGALESVRIL----KSSEGRALRRQHQRNVKLLRQMLMDAGLPVI-HCPSHIIPVRVADAAKNTEICDELMTRhNI 555
Cdd:PLN02483 345 PPAVQQVISAIKVIlgedGTNRGAQKLAQIRENSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-NV 423
                        330
                 ....*....|.
gi 628601867 556 YVQAINYPTVP 566
Cdd:PLN02483 424 AVVVVGFPATP 434
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
245-594 4.75e-44

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 164.46  E-value: 4.75e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 245 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 L--------AKMMP----GCEIYSDSGNHASMIQGIR----NSRVPKYIFRHNDVNHLRELLQRSDPSvPKIVAFETVHS 388
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 389 MDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRS 468
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 469 YAAGFIFTTSLPPMLLAGALESVRILKSSEGRalRRQHQRNVKLLRQMlmdAGLPVihcPSHIIPVRVADAAKNTEICDE 548
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 628601867 549 LMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffVEKLLV 594
Cdd:PLN02955 413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTED----VKKLIT 453
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
252-605 3.93e-43

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 160.17  E-value: 3.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 252 SNDYLGMSRHPRVCGAVMETVKQHGAG----AGGTRNISGTSKFhvelEQALADLHGKDAALLFSSCFVANDSTLFTLAK 327
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 328 mmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSvpkIVAFETVHSMDGAVCPLEELCDVAHEFG 407
Cdd:PRK07179 137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFG 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 408 AITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVR--SYAAgfIFTTSLPPMLLA 485
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 486 GALESVRILKSSEGRalRRQHQRNVKLLRQMLMDAGLPvIHCPSHIIPVrVADAAKNTEIC-DELMTRhNIYVQAINYPT 564
Cdd:PRK07179 290 GLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCAPA 364
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 628601867 565 VPRGEELLRIAPTPHHTPQMMNFFVEKLLVTWKRVGLELKP 605
Cdd:PRK07179 365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
249-555 4.33e-31

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 125.40  E-value: 4.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 249 VWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKM 328
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 329 mpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELL----------QRSDPSVPKIVAFETVHSMDGAVCPLEE 398
Cdd:PLN03227  82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 399 LCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP--KMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFT 476
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 477 TSLPPMLLAGALESVRILKSSEgRALRRQHQrNVKLLRQMLMDAGLPVIHCP-----------SHIIPVRVADAAKnTEI 545
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316
                        330
                 ....*....|
gi 628601867 546 CDELMTRHNI 555
Cdd:PLN03227 317 TDETLILDQI 326
PLN02822 PLN02822
serine palmitoyltransferase
242-519 1.06e-27

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 116.76  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 242 ITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDST 321
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 322 LFTLAKMmpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ-------RSDPSVPKIVAfETVHSMDGAVC 394
Cdd:PLN02822 186 IPAFCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenkRKKKLRRYIVV-EAIYQNSGQIA 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 395 PLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP-KMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGF 473
Cdd:PLN02822 263 PLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIeKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGY 342
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 628601867 474 IFTTSLPPMLLAGALESVRILKssEGRALRRQHQRNVKLLRQMLMD 519
Cdd:PLN02822 343 VFSASLPPYLASAAITAIDVLE--DNPSVLAKLKENIALLHKGLSD 386
PRK07505 PRK07505
hypothetical protein; Provisional
251-583 5.08e-27

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 113.54  E-value: 5.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 251 CSNDYLGMSRHPRVCGAVMETVKqhgagAGGTRNISgTSKFHV------ELEQALADLHGKDAaLLFSSCFVANDSTLFT 324
Cdd:PRK07505  52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LAK--MMPGCEIYS--DSGNHASM--IQGIRNSRVPKYIFRHNDVNHLRELLQRSdpsvpKIVAF--ETVHSMdGAVCPL 396
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSM-GGIAPV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 397 EELCDVAHEFGAITFVDEVHAVGLYGargggIGDRDGVMPKMD-------IISGTLGKAFGCVGGYIA-STSLLIDTVRS 468
Cdd:PRK07505 199 KELLRLQEKYGLFLYIDDAHGLSIYG-----KNGEGYVRSELDyrlnertIIAASLGKAFGASGGVIMlGDAEQIELILR 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 469 YAAGFIFTTSLPPMLLAGALESVRILKSSEGRALRRQHQRNVKLLRQMLMD--AGLPVihcpshiiPVRVA---DAAKNT 543
Cdd:PRK07505 274 YAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAI 345
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 628601867 544 EICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 583
Cdd:PRK07505 346 KAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
252-544 1.24e-21

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 97.16  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 252 SNDYLGMSRHPRVCGAVMETVKQH-------GAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 325 LAKMMPgcEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDV 402
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscRQRSFGRIFIFVCSVYSFKGTLAPLEQIIAL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 403 AHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISgTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPM 482
Cdd:PRK05937 169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 483 LLAGALESVRILkSSEGRALRRQ--------HQR-----------------NVKLLRQMLMDAGLPV-IHCPSHIIPVRV 536
Cdd:PRK05937 248 LLISIQVAYDFL-SQEGELARKQlfrlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPFLRV 326

                 ....*...
gi 628601867 537 ADAAKNTE 544
Cdd:PRK05937 327 NLHAFNTE 334
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
291-454 1.64e-12

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: 65.87  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 291 FHVELEQALADL--HGKDAALLFSSCFVANDSTLFTLAkmMPGCEIYSDSGNHAS--MIQGIRNSRVPKYIFRHNDVNHL 366
Cdd:cd01494    1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSryWVAAELAGAKPVPVPVDDAGYGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 367 RELLQRSD---PSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRdgvmpKMDIISG 443
Cdd:cd01494   79 LDVAILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG-----GADVVTF 153
                        170
                 ....*....|.
gi 628601867 444 TLGKAFGCVGG 454
Cdd:cd01494  154 SLHKNLGGEGG 164
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
254-419 4.01e-08

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


Pssm-ID: 223594 [Multi-domain]  Cd Length: 405  Bit Score: 55.78  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 254 DYLGMSRHPRVC-GAVMETVKQHGAGAGgtrniSGTSKFHVELEQALADLHGKDAALLFSS-----CFVANDST-LFTLA 326
Cdd:COG0520   27 DNAATSQKPQAVlDAVAEYYRRYNANVH-----RGAHTLAEEATDLYEAAREAVARFLNADssdeiVFTRGTTEaLNLVA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 327 KMM-----PGCEIYSDSGNHASMI---------QGIRNSRVPkyiFRHNDVNHLRELLQRSDPSvPKIVAFETVHSMDGA 392
Cdd:COG0520  102 RGLgrslkPGDEIVVSDLEHHSNIvpwqelakrTGAKVRVIP---LDDDGLLDLDALEKLITPK-TKLVALSHVSNVTGT 177
                        170       180
                 ....*....|....*....|....*..
gi 628601867 393 VCPLEELCDVAHEFGAITFVDEVHAVG 419
Cdd:COG0520  178 VNPVKEIAELAHEHGALVLVDAAQAAG 204
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
292-413 2.73e-07

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: 52.97  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 292 HVELEQALADLHGKDAALLFSSCFVANDSTLFTLAK-----MMPGCeIYSDSGNHASMIQ---GIRNSRVPKyifrhNDV 363
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERLLpklGIEVTFVDP-----DDP 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 628601867 364 NHLRELLQRSdpsvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVD 413
Cdd:cd00614  116 EALEAAIKPE----TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
396-575 6.01e-07

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: 51.96  E-value: 6.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 396 LEELCDVAHEFGAITFVDEVHAvGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVG---GY-IASTSLLIDTVRSYAa 471
Cdd:cd00609  154 LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLL- 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 472 gfIFTTSLPPMLLAGALESVRILKSSEGRALRRQHQRNVKLLRQMLMDAGLPVIHCPS---HI-IPVRVADAAkntEICD 547
Cdd:cd00609  232 --PYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLE 306
                        170       180
                 ....*....|....*....|....*...
gi 628601867 548 ELMTRHNIYVQAINYPtVPRGEELLRIA 575
Cdd:cd00609  307 RLLLEAGVVVRPGSAF-GEGGEGFVRLS 333
HemL COG0001
Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism];
357-524 2.66e-04

Glutamate-1-semialdehyde aminotransferase [Coenzyme transport and metabolism];


Pssm-ID: 223080 [Multi-domain]  Cd Length: 432  Bit Score: 43.72  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 357 IFRHNDVNHLRELLQRSDPSVPKIVaFETVHSMDGAVCP----LEELCDVAHEFGAITFVDEVH---------AVGLYGa 423
Cdd:COG0001  181 VLPYNDLEALEEAFEEYGDDIAAVI-VEPVAGNMGVVPPepgfLEGLRELTEEHGALLIFDEVItgfrvalggAQGYYG- 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601867 424 rgggigdrdgVMPkmDIIsgTLGKA------FGCVGGYIASTSLLIDTVRSYAAGfifTTSLPPMLLAGALESVRILKSS 497
Cdd:COG0001  259 ----------VEP--DLT--TLGKIiggglpIGAFGGRAEIMEQLAPLGPVYQAG---TLSGNPLAMAAGLATLEELMTE 321
                        170       180
                 ....*....|....*....|....*....
gi 628601867 498 EG--RALRRQHQRNVKLLRQMLMDAGLPV 524
Cdd:COG0001  322 EGvyERLDALGERLAEGLRAAAERHGIPL 350
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
378-419 7.01e-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: 39.15  E-value: 7.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 628601867  378 PKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 419
Cdd:pfam00266 140 TKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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