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Conserved domains on  [gi|29244577|ref|NP_033295|]
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serine palmitoyltransferase 1 isoform 1 [Mus musculus]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

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) ...
 11-472 1.98e-179

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 PLN02822:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 481  Bit Score: 511.21  E-value: 1.98e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   11 VEMVQALYEAPAY-----------HLILEGILILWIIRLVFSKTYKLQERSdLTAKEKEELIEEWQPEPLVPPVSKN--- 76
Cdd:PLN02822  13 LERVTMLLEAPLAravvfgvhiggHLVVEGLLIVVIVFLLSQKSYKPPKRP-LTEKEIDELCDEWTPEPLIPPITEEmrp 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   77 -HPALNYniVSGPPThniVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKF 155
Cdd:PLN02822  92 ePPVLES--AAGPHT---IINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  156 MKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDqknpRKA 235
Cdd:PLN02822 167 LGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN----KRK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  236 RVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVG 315
Cdd:PLN02822 243 KKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEG 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  316 GFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVSGLKVVGESLSPALH 395
Cdd:PLN02822 323 GFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVF 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  396 LQLEESTGSREKDVKLLQAIVDQCMDKG---IALTQARYLDkeeKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVL 472
Cdd:PLN02822 403 LHLEKSTGSAKEDLSLLEHIADRMLKEDsvlVVVSKRSTLD---KCRLPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 11-472 1.98e-179

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 511.21  E-value: 1.98e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   11 VEMVQALYEAPAY-----------HLILEGILILWIIRLVFSKTYKLQERSdLTAKEKEELIEEWQPEPLVPPVSKN--- 76
Cdd:PLN02822  13 LERVTMLLEAPLAravvfgvhiggHLVVEGLLIVVIVFLLSQKSYKPPKRP-LTEKEIDELCDEWTPEPLIPPITEEmrp 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   77 -HPALNYniVSGPPThniVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKF 155
Cdd:PLN02822  92 ePPVLES--AAGPHT---IINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  156 MKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDqknpRKA 235
Cdd:PLN02822 167 LGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN----KRK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  236 RVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVG 315
Cdd:PLN02822 243 KKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEG 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  316 GFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVSGLKVVGESLSPALH 395
Cdd:PLN02822 323 GFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVF 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  396 LQLEESTGSREKDVKLLQAIVDQCMDKG---IALTQARYLDkeeKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVL 472
Cdd:PLN02822 403 LHLEKSTGSAKEDLSLLEHIADRMLKEDsvlVVVSKRSTLD---KCRLPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 84-470 5.19e-77

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: 245.73  E-value: 5.19e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  84 IVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAII 163
Cdd:COG0156  23 VLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALL 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 164 YSYGFSTIASAIPAYSKRGDIIFVDSA--ACfaIQKGLQASRSDIKLFKHNDVADLERLLKEqeiedqknPRKARvtRRF 241
Cdd:COG0156 103 FSSGYAANLGVISALAGRGDLIFSDELnhAS--IIDGARLSGAKVVRFRHNDMDDLERLLKK--------ARAAR--RKL 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 242 IVVEGLY-MnTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISiDDIDLISANMENALASVGGFCCG 320
Cdd:COG0156 171 IVTDGVFsM-DGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAG 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 321 RSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGvSGLKvVGESLSP--ALHLql 398
Cdd:COG0156 249 SKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKE-LGFD-LGPSESPivPVIV-- 324

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29244577 399 eestgsreKDVKLLQAIVDQCMDKGIALTQARYldkeekclppPS-------IRVVVTVEQTEEELQRAASTIREAAQA 470
Cdd:COG0156 325 --------GDAERALALADALLERGIYVSAIRP----------PTvpkgtarLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 98-467 6.17e-76

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: 241.70  E-value: 6.17e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  98 KECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPA 177
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 178 YSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEqeiedqkNPRKARvtRRFIVVEGLYMNTGTICPL 257
Cdd:cd06454  81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLRE-------ARRPYG--KKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 258 PELVKLKYKYKARIFLEESLSFGVLGEHGRGVtEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCF 337
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 338 SASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVsGLKVVGESLSPALHLQLEEStgsrekdvKLLQAIVD 417
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSPSHIIPPLIGDDP--------AKAVAFSD 301

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 29244577 418 QCMDKGIALTQARY----LDKEEkclpppsIRVVVTVEQTEEELQRAASTIREA 467
Cdd:cd06454 302 ALLERGIYVQAIRYptvpRGTAR-------LRISLSAAHTKEDIDRLLEALKEV 348
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
98-464 7.23e-24

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 102.38  E-value: 7.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577    98 KECVNFASFNFLGLLANPRVKATAFsslkkygVGTCGPRGFYGTFDVHLDLEERLAKFM--------KTEEAIIYSYGFS 169
Cdd:pfam00155   1 TDKINLGSNEYLGDTLPAVAKAEKD-------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   170 TIASAIPAYSK-RGDIIFVDSAACFAIQKGLQASRSDIKLFK-------HNDVADLERLLKEQeiedqknprkarvtRRF 241
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK--------------PKV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   242 IVVEGLYMNTGTICPLPELVKL---KYKYKARIFLEESLSFGVLGEHGRgVTEHYGISiDDIDLISAN-MENALASVG-- 315
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDA-VATRALLA-EGPNLLVVGsFSKAFGLAGwr 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   316 -GFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVsGLKVVGeSLSPAL 394
Cdd:pfam00155 218 vGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA-GLSVLP-SQAGFF 295

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   395 HLQLeestGSREKDVKLLQAIVDQCmdkGIALTQARYldkeekCLPPPSIRVVVTVeQTEEELQRAASTI 464
Cdd:pfam00155 296 LLTG----LDPETAKELAQVLLEEV---GVYVTPGSS------PGVPGWLRITVAG-GTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 11-472 1.98e-179

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 511.21  E-value: 1.98e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   11 VEMVQALYEAPAY-----------HLILEGILILWIIRLVFSKTYKLQERSdLTAKEKEELIEEWQPEPLVPPVSKN--- 76
Cdd:PLN02822  13 LERVTMLLEAPLAravvfgvhiggHLVVEGLLIVVIVFLLSQKSYKPPKRP-LTEKEIDELCDEWTPEPLIPPITEEmrp 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   77 -HPALNYniVSGPPThniVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKF 155
Cdd:PLN02822  92 ePPVLES--AAGPHT---IINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  156 MKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDqknpRKA 235
Cdd:PLN02822 167 LGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN----KRK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  236 RVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVG 315
Cdd:PLN02822 243 KKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEG 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  316 GFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVSGLKVVGESLSPALH 395
Cdd:PLN02822 323 GFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVF 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  396 LQLEESTGSREKDVKLLQAIVDQCMDKG---IALTQARYLDkeeKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVL 472
Cdd:PLN02822 403 LHLEKSTGSAKEDLSLLEHIADRMLKEDsvlVVVSKRSTLD---KCRLPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 101-472 6.81e-115

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 343.42  E-value: 6.81e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  101 VNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSK 180
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  181 RGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPEL 260
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  261 VKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGIS-IDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSA 339
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  340 SLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVS---------GLKVVGESLSPALHLQLEESTGSREKD-V 409
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSShpyalklrnRLVITSDPISPIIYLRLSDQEATRRTDeT 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29244577  410 KLLQAIVDQCMDKGIALTQAR-YLDKEEKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVL 472
Cdd:PLN03227 321 LILDQIAHHSLSEGVAVVSTGgHVKKFLQLVPPPCLRVVANASHTREDIDKLLTVLGEAVEAIL 384
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 84-470 5.19e-77

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: 245.73  E-value: 5.19e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  84 IVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAII 163
Cdd:COG0156  23 VLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALL 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 164 YSYGFSTIASAIPAYSKRGDIIFVDSA--ACfaIQKGLQASRSDIKLFKHNDVADLERLLKEqeiedqknPRKARvtRRF 241
Cdd:COG0156 103 FSSGYAANLGVISALAGRGDLIFSDELnhAS--IIDGARLSGAKVVRFRHNDMDDLERLLKK--------ARAAR--RKL 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 242 IVVEGLY-MnTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISiDDIDLISANMENALASVGGFCCG 320
Cdd:COG0156 171 IVTDGVFsM-DGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAG 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 321 RSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGvSGLKvVGESLSP--ALHLql 398
Cdd:COG0156 249 SKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKE-LGFD-LGPSESPivPVIV-- 324

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29244577 399 eestgsreKDVKLLQAIVDQCMDKGIALTQARYldkeekclppPS-------IRVVVTVEQTEEELQRAASTIREAAQA 470
Cdd:COG0156 325 --------GDAERALALADALLERGIYVSAIRP----------PTvpkgtarLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 98-467 6.17e-76

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: 241.70  E-value: 6.17e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  98 KECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPA 177
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 178 YSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEqeiedqkNPRKARvtRRFIVVEGLYMNTGTICPL 257
Cdd:cd06454  81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLRE-------ARRPYG--KKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 258 PELVKLKYKYKARIFLEESLSFGVLGEHGRGVtEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCF 337
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577 338 SASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVsGLKVVGESLSPALHLQLEEStgsrekdvKLLQAIVD 417
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSPSHIIPPLIGDDP--------AKAVAFSD 301

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 29244577 418 QCMDKGIALTQARY----LDKEEkclpppsIRVVVTVEQTEEELQRAASTIREA 467
Cdd:cd06454 302 ALLERGIYVQAIRYptvpRGTAR-------LRISLSAAHTKEDIDRLLEALKEV 348
PLN02483 PLN02483
serine palmitoyltransferase
 96-471 4.35e-55

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 191.13  E-value: 4.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   96 NGKECVNFASFNFLGLLA-----NPRVkataFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFST 170
Cdd:PLN02483  98 KTRRCLNLGSYNYLGFAAadeycTPRV----IESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYAT 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  171 IASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQknPRKARVTRRFIV-VEGLYM 249
Cdd:PLN02483 174 NSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQ--PRTHRPWKKIIViVEGIYS 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  250 NTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQR 329
Cdd:PLN02483 252 MEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLK 331

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  330 LSGQGYCFSASL-PPLLAAAAIEALNIM-EENPDIFAvlkKKCQNIHKS-------LQGVsGLKVVGESLSPALHLQLEE 400
Cdd:PLN02483 332 RTCPAHLYATSMsPPAVQQVISAIKVILgEDGTNRGA---QKLAQIRENsnffrseLQKM-GFEVLGDNDSPVMPIMLYN 407

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29244577  401 STG----SREkdvkllqaivdqCMDKGIALTQARYldkeeKCLPP--PSIRVVVTVEQTEEELQRAASTIREAAQAV 471
Cdd:PLN02483 408 PAKipafSRE------------CLKQNVAVVVVGF-----PATPLllARARICISASHSREDLIKALEVISEVGDLV 467
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 84-468 2.69e-47

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 167.64  E-value: 2.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   84 IVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAII 163
Cdd:PRK05958  25 PREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  164 YSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLkeqeiedqknpRKARVTRRFIV 243
Cdd:PRK05958 105 FSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALL-----------AKWRAGRALIV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  244 VEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGIsIDDIDLIS-ANMENALASVGGFCCGRS 322
Cdd:PRK05958 174 TESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGL-AGEPDVILvGTLGKALGSSGAAVLGSE 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  323 FVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP-------DIFAVLKKKCQNIHKSLqgvsglkvvGESLSPALH 395
Cdd:PRK05958 253 TLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPerrerlaALIARLRAGLRALGFQL---------MDSQSAIQP 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  396 LQLeestGSREKDVKLLQAivdqCMDKGIALTqaryldkeekCLPPPS-------IRVVVTVEQTEEELQRAASTIREAA 468
Cdd:PRK05958 324 LIV----GDNERALALAAA----LQEQGFWVG----------AIRPPTvpagtsrLRITLTAAHTEADIDRLLEALAEAL 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 94-471 1.26e-46

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 166.14  E-value: 1.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   94 VVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIAS 173
Cdd:PRK06939  38 VADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  174 AIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQeiedqknpRKARVTRRFIVVEGLYMNTGT 253
Cdd:PRK06939 118 LFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEA--------KEAGARHKLIATDGVFSMDGD 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  254 ICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISiDDIDLISANMENALA-SVGGFCCGRSFVVDHQRLSG 332
Cdd:PRK06939 190 IAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVM-DRVDIITGTLGKALGgASGGYTAGRKEVIDWLRQRS 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  333 QGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKslqgvsGLKVVGESLSPALHLQLEESTGsrekDVKLL 412
Cdd:PRK06939 269 RPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFRE------GMTAAGFTLGPGEHPIIPVMLG----DAKLA 338

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29244577  413 QAIVDQCMDKGIALT----------QARyldkeekclpppsIRVVVTVEQTEEELQRAASTIREAAQAV 471
Cdd:PRK06939 339 QEFADRLLEEGVYVIgfsfpvvpkgQAR-------------IRTQMSAAHTKEQLDRAIDAFEKVGKEL 394
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 98-343 4.53e-31

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 123.81  E-value: 4.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   98 KECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGF-------ST 170
Cdd:PRK13392  46 RRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYvsndaalST 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  171 IASAIPayskrGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKnprkarvtrrFIVVEGLYMN 250
Cdd:PRK13392 126 LGKLLP-----GCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPK----------LIAFESVYSM 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  251 TGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGIsIDDIDLISANMENALASVGGFCCGRSFVVDHQRL 330
Cdd:PRK13392 191 DGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRS 269

                        250
                 ....*....|...
gi 29244577  331 SGQGYCFSASLPP 343
Cdd:PRK13392 270 FAPGFIFTTALPP 282
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
98-464 7.23e-24

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 102.38  E-value: 7.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577    98 KECVNFASFNFLGLLANPRVKATAFsslkkygVGTCGPRGFYGTFDVHLDLEERLAKFM--------KTEEAIIYSYGFS 169
Cdd:pfam00155   1 TDKINLGSNEYLGDTLPAVAKAEKD-------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   170 TIASAIPAYSK-RGDIIFVDSAACFAIQKGLQASRSDIKLFK-------HNDVADLERLLKEQeiedqknprkarvtRRF 241
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK--------------PKV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   242 IVVEGLYMNTGTICPLPELVKL---KYKYKARIFLEESLSFGVLGEHGRgVTEHYGISiDDIDLISAN-MENALASVG-- 315
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDA-VATRALLA-EGPNLLVVGsFSKAFGLAGwr 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   316 -GFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVsGLKVVGeSLSPAL 394
Cdd:pfam00155 218 vGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA-GLSVLP-SQAGFF 295

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   395 HLQLeestGSREKDVKLLQAIVDQCmdkGIALTQARYldkeekCLPPPSIRVVVTVeQTEEELQRAASTI 464
Cdd:pfam00155 296 LLTG----LDPETAKELAQVLLEEV---GVYVTPGSS------PGVPGWLRITVAG-GTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
97-320 1.03e-17

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 85.06  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   97 GKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFS------- 169
Cdd:PRK07179  53 GPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAanvgllq 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  170 TIASA-IPAYskrgdiifVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLkeqeiedqknprkarvtRRF----IVV 244
Cdd:PRK07179 133 TIADPnTPVY--------IDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQI-----------------ERHgpgiIVV 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29244577  245 EGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISiDDIDLISANMENALASVGGFCCG 320
Cdd:PRK07179 188 DSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAFAGRAGIITC 262
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 130-294 1.22e-16

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 81.37  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  130 VGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLF 209
Cdd:PRK05937  43 LGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSF 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  210 KHNDVADLERLLKEQeiedqknpRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGV 289
Cdd:PRK05937 123 RHNDLDHLESLLESC--------RQRSFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGF 194


                 ....*
gi 29244577  290 TEHYG 294
Cdd:PRK05937 195 CHSLG 199
PRK07505 PRK07505
hypothetical protein; Provisional
 97-317 4.11e-16

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 80.02  E-value: 4.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   97 GKECVNFASFNFLGLLANPRVKATAFSSLKKYGV-GTCGPRGFYgTFDVHLDLEERLAKFMkTEEAIIYSYGFST----- 170
Cdd:PRK07505  45 GHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRV-RSQILKDLEEALSELF-GASVLTFTSCSAAhlgil 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  171 --IASAIPAYSKRGDIIFVDSA-ACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEiedqknprkarvtRRFIVVEGL 247
Cdd:PRK07505 123 plLASGHLTGGVPPHMVFDKNAhASLNILKGICADETEVETIDHNDLDALEDICKTNK-------------TVAYVADGV 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29244577  248 YmNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRG-VTEHYGISIDDIDLISANMENALASVGGF 317
Cdd:PRK07505 190 Y-SMGGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRLNERTIIAASLGKAFGASGGV 259
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 98-342 2.29e-15

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 78.18  E-value: 2.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577   98 KECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFS-------- 169
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAanmaamva 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  170 --TIASAIPAYSK----RGDIIFVDSAACFAIQKGLQ-ASR---SDIKLFKHNDVADLERLLKEQEIEdqknprkarvtR 239
Cdd:PLN02955 182 igSVASLLAASGKplknEKVAIFSDALNHASIIDGVRlAERqgnVEVFVYRHCDMYHLNSLLSSCKMK-----------R 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244577  240 RFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISiDDIDLISANMENALASVGGF-- 317
Cdd:PLN02955 251 KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFia 329

                        250       260
                 ....*....|....*....|....*
gi 29244577  318 CCGRSFVVDHQRlsGQGYCFSASLP 342
Cdd:PLN02955 330 CSKKWKQLIQSR--GRSFIFSTAIP 352
 
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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