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Conserved domains on  [gi|1092786827|ref|WP_070708181|]
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8-amino-7-oxononanoate synthase [Porphyromonas sp. HMSC077F02]

Protein Classification

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme( domain architecture ID 11414994)

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme similar to 8-amino-7-oxononanoate synthase, which catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide in the biosynthesis of biotin

CATH:  3.40.640.10|3.90.1150.10
EC:  2.3.-.-
Gene Ontology:  GO:0030170|GO:0016747
PubMed:  10800595|10673430

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 2-374 7.13e-148

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: 423.31  E-value: 7.13e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   2 DRYRQALEQCQSEGTYRTLPDIEVR-GKYIDVKGRQLLNLNSNDYLGLLAEPQL---WQRFIEEEGkrrhPSSGSSRLLT 77
Cdd:COG0156     3 DRLEAELAALKAAGLYRYLRVLESPqGPRVTIDGREVLNFSSNDYLGLANHPRVieaAAEALDRYG----TGSGGSRLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  78 GNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRK 157
Cdd:COG0156    79 GTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLER 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 158 ILSRYADqYDTLWLITESLFSMDGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIGTLG 237
Cdd:COG0156   159 LLKKARA-ARRKLIVTDGVFSMDGDIAPLPEIVELAEKY-GALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 238 KALGSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFG---KEMGREF---T 311
Cdd:COG0156   237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFReglKELGFDLgpsE 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092786827 312 SQIIPLIVPGEEQVTKAAEQLCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLANLC 374
Cdd:COG0156   317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 2-374 7.13e-148

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: 423.31  E-value: 7.13e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   2 DRYRQALEQCQSEGTYRTLPDIEVR-GKYIDVKGRQLLNLNSNDYLGLLAEPQL---WQRFIEEEGkrrhPSSGSSRLLT 77
Cdd:COG0156     3 DRLEAELAALKAAGLYRYLRVLESPqGPRVTIDGREVLNFSSNDYLGLANHPRVieaAAEALDRYG----TGSGGSRLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  78 GNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRK 157
Cdd:COG0156    79 GTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLER 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 158 ILSRYADqYDTLWLITESLFSMDGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIGTLG 237
Cdd:COG0156   159 LLKKARA-ARRKLIVTDGVFSMDGDIAPLPEIVELAEKY-GALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 238 KALGSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFG---KEMGREF---T 311
Cdd:COG0156   237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFReglKELGFDLgpsE 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092786827 312 SQIIPLIVPGEEQVTKAAEQLCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLANLC 374
Cdd:COG0156   317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 1-370 2.37e-137

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 396.45  E-value: 2.37e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   1 MDRYRQALEQCQSEGTYRTLPDIE-VRGKYIDVKGRQLLNLNSNDYLGLLAEPQL---WQRFIEEEGkrrhPSSGSSRLL 76
Cdd:PRK05958    4 LDRLEAALAQRRAAGLYRSLRPREgGAGRWLVVDGRRMLNFASNDYLGLARHPRLiaaAQQAARRYG----AGSGGSRLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  77 TGNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLR 156
Cdd:PRK05958   80 TGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 157 KILSRYADQydTLWLITESLFSMDGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREID-LLIGT 235
Cdd:PRK05958  160 ALLAKWRAG--RALIVTESVFSMDGDLAPLAELVALARRH-GAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDvILVGT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 236 LGKALGSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGREF----- 310
Cdd:PRK05958  237 LGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGfqlmd 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092786827 311 -TSQIIPLIVPGEEQVTKAAEQLCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQL 370
Cdd:PRK05958  317 sQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRL 377
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 35-377 1.11e-125

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: 365.73  E-value: 1.11e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  35 RQLLNLNSNDYLGLLAEPQL---WQRFIEEEGkrrhPSSGSSRLLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTG 111
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVieaAKEALDKYG----VGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 112 IPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRYADQYDTLWLITESLFSMDGDIAPLQELVA 191
Cdd:cd06454    77 VLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 192 LKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIGTLGKALGSVGAYSLQSDTLRQLLVSKARSLIFSTALP 271
Cdd:cd06454   157 LAKKY-GAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 272 EVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGR-------EFTSQIIPLIVPGEEQVTKAAEQLCRHGFYIRPIRR 344
Cdd:cd06454   236 PAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKElgfpvggSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1092786827 345 PTVPQGSERLRLSLTAAMTTDEIIQLANLCNSI 377
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEV 348
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 27-372 6.53e-115

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: 338.47  E-value: 6.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  27 GKYIDVKGRQLLNLNSNDYLGLLAEPQLWQRFIEeeGKRRHPS-SGSSRLLTGNSPVAQQFESELANAYGLGSALLWDSG 105
Cdd:TIGR00858   8 GPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQ--GAEQYGAgSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 106 YHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRyADQYDTLWLITESLFSMDGDIAP 185
Cdd:TIGR00858  86 YLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEK-NRGERRKLIVTDGVFSMDGDIAP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 186 LQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTRE-IDLLIGTLGKALGSVGAYSLQSDTLRQLLVSKARSL 264
Cdd:TIGR00858 165 LPQLVALAERY-GAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 265 IFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGR-EFT-----SQIIPLIVPGEEQVTKAAEQLCRHGFY 338
Cdd:TIGR00858 244 IFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEAlGFTlmpscTPIVPVIIGDNASALALAEELQQQGIF 323

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1092786827 339 IRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLAN 372
Cdd:TIGR00858 324 VGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAE 357
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
35-377 2.74e-42

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 150.92  E-value: 2.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  35 RQLLNLNSNDYLGLLAEpqlwqrFIEEEGKRRHpsSGSSRLLTGNSPVAQQFESELANAYGLGSALLWD--------SGY 106
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP------AVAKAEKDAL--AGGTRNLYGPTDGHPELREALAKFLGRSPVLKLDreaavvfgSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 107 HAN-TGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYR-------HNDLSHLRKILSRyadqyDTLWLITESLFS 178
Cdd:pfam00155  73 GANiEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE-----KPKVVLHTSPHN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 179 MDGDIAP---LQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGlAAEMGVTREIDLLI-GTLGKALGSVG---AYSLQSD 251
Cdd:pfam00155 148 PTGTVATleeLEKLLDLAKEH-NILLLVDEAYAGFVFGSPDAV-ATRALLAEGPNLLVvGSFSKAFGLAGwrvGYILGNA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 252 TLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGRE----FTSQ--IIPLIVPGEEQV 325
Cdd:pfam00155 226 AVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAglsvLPSQagFFLLTGLDPETA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1092786827 326 TKAAEQLC-RHGFYIRPIRRPTVPqgsERLRLSLtAAMTTDEiiqLANLCNSI 377
Cdd:pfam00155 306 KELAQVLLeEVGVYVTPGSSPGVP---GWLRITV-AGGTEEE---LEELLEAI 351
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 2-374 7.13e-148

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: 423.31  E-value: 7.13e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   2 DRYRQALEQCQSEGTYRTLPDIEVR-GKYIDVKGRQLLNLNSNDYLGLLAEPQL---WQRFIEEEGkrrhPSSGSSRLLT 77
Cdd:COG0156     3 DRLEAELAALKAAGLYRYLRVLESPqGPRVTIDGREVLNFSSNDYLGLANHPRVieaAAEALDRYG----TGSGGSRLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  78 GNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRK 157
Cdd:COG0156    79 GTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLER 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 158 ILSRYADqYDTLWLITESLFSMDGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIGTLG 237
Cdd:COG0156   159 LLKKARA-ARRKLIVTDGVFSMDGDIAPLPEIVELAEKY-GALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 238 KALGSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFG---KEMGREF---T 311
Cdd:COG0156   237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFReglKELGFDLgpsE 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092786827 312 SQIIPLIVPGEEQVTKAAEQLCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLANLC 374
Cdd:COG0156   317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 1-370 2.37e-137

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 396.45  E-value: 2.37e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   1 MDRYRQALEQCQSEGTYRTLPDIE-VRGKYIDVKGRQLLNLNSNDYLGLLAEPQL---WQRFIEEEGkrrhPSSGSSRLL 76
Cdd:PRK05958    4 LDRLEAALAQRRAAGLYRSLRPREgGAGRWLVVDGRRMLNFASNDYLGLARHPRLiaaAQQAARRYG----AGSGGSRLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  77 TGNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLR 156
Cdd:PRK05958   80 TGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 157 KILSRYADQydTLWLITESLFSMDGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREID-LLIGT 235
Cdd:PRK05958  160 ALLAKWRAG--RALIVTESVFSMDGDLAPLAELVALARRH-GAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDvILVGT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 236 LGKALGSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGREF----- 310
Cdd:PRK05958  237 LGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGfqlmd 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092786827 311 -TSQIIPLIVPGEEQVTKAAEQLCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQL 370
Cdd:PRK05958  317 sQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRL 377
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 35-377 1.11e-125

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: 365.73  E-value: 1.11e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  35 RQLLNLNSNDYLGLLAEPQL---WQRFIEEEGkrrhPSSGSSRLLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTG 111
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVieaAKEALDKYG----VGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 112 IPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRYADQYDTLWLITESLFSMDGDIAPLQELVA 191
Cdd:cd06454    77 VLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 192 LKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIGTLGKALGSVGAYSLQSDTLRQLLVSKARSLIFSTALP 271
Cdd:cd06454   157 LAKKY-GAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 272 EVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGR-------EFTSQIIPLIVPGEEQVTKAAEQLCRHGFYIRPIRR 344
Cdd:cd06454   236 PAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKElgfpvggSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1092786827 345 PTVPQGSERLRLSLTAAMTTDEIIQLANLCNSI 377
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEV 348
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 27-372 6.53e-115

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: 338.47  E-value: 6.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  27 GKYIDVKGRQLLNLNSNDYLGLLAEPQLWQRFIEeeGKRRHPS-SGSSRLLTGNSPVAQQFESELANAYGLGSALLWDSG 105
Cdd:TIGR00858   8 GPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQ--GAEQYGAgSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 106 YHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRyADQYDTLWLITESLFSMDGDIAP 185
Cdd:TIGR00858  86 YLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEK-NRGERRKLIVTDGVFSMDGDIAP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 186 LQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTRE-IDLLIGTLGKALGSVGAYSLQSDTLRQLLVSKARSL 264
Cdd:TIGR00858 165 LPQLVALAERY-GAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 265 IFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGR-EFT-----SQIIPLIVPGEEQVTKAAEQLCRHGFY 338
Cdd:TIGR00858 244 IFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEAlGFTlmpscTPIVPVIIGDNASALALAEELQQQGIF 323

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1092786827 339 IRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLAN 372
Cdd:TIGR00858 324 VGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAE 357
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 4-372 1.43e-73

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: 234.24  E-value: 1.43e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   4 YRQALEQCQSEGTYRTLPDIE-VRGKY-----IDVKGRQLLNL-NSNDYLGLLAEPQLWQ---RFIEEEGKrrhpSSGSS 73
Cdd:TIGR01821   7 FNKEIDKLHLEGRYRVFADLErQAGEFpfaqwHRPDGAKDVTVwCSNDYLGMGQHPEVLQamhETLDKYGA----GAGGT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  74 RLLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLA--LPNTLFIADKLVHASIIDGLRLSGAPFQRYRHND 151
Cdd:TIGR01821  83 RNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAkiIPGCVIFSDELNHASMIEGIRHSGAEKFIFRHND 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 152 LSHLRKILSRYADQYDTLwLITESLFSMDGDIAPLQELVALKEEYPHLyIYVDEAHAVGLFGPKGLGLAAEMGVTREIDL 231
Cdd:TIGR01821 163 VAHLEKLLQSVDPNRPKI-IAFESVYSMDGDIAPIEEICDLADKYGAL-TYLDEVHAVGLYGPRGGGIAERDGLMHRIDI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 232 LIGTLGKALGSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWS----RFLFHAIQEMDDRRQHLKDLVTLFgKEMG 307
Cdd:TIGR01821 241 IEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAtasiRHLKESQDLRRAHQENVKRLKNLL-EALG 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092786827 308 REFT---SQIIPLIVPGEEQVTKAAEQLC-RHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLAN 372
Cdd:TIGR01821 320 IPVIpnpSHIVPVIIGDAALCKKVSDLLLnKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVE 388
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 2-367 8.15e-72

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 229.31  E-value: 8.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   2 DRYRQALEQCQSEGTYRTL--------PDIEVRGkyidvkGRQLLNLNSNDYLGLLAEPQLwqrfIE--EEGKRRHP-SS 70
Cdd:PRK06939    7 AQLREELEEIKAEGLYKEErvitspqgADITVAD------GKEVINFCANNYLGLANHPEL----IAaaKAALDSHGfGM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  71 GSSRLLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHN 150
Cdd:PRK06939   77 ASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 151 DLSHLRKILsRYADQYD--TLWLITESLFSMDGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTRE 228
Cdd:PRK06939  157 DMADLEAQL-KEAKEAGarHKLIATDGVFSMDGDIAPLPEICDLADKY-DALVMVDDSHAVGFVGENGRGTVEHFGVMDR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 229 IDLLIGTLGKAL-GSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMG 307
Cdd:PRK06939  235 VDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMT 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092786827 308 RE-FT-----SQIIPLIVpGEEQVTKA-AEQLCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEI 367
Cdd:PRK06939  315 AAgFTlgpgeHPIIPVML-GDAKLAQEfADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQL 380
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 2-371 1.77e-69

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 223.96  E-value: 1.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827   2 DRYRQALEQCQSEGTYRTLPDIE-VRGKYIDVK------GRQLLNLNSNDYLGLLAEPQLWQRFIEEeGKRRHPSSGSSR 74
Cdd:PRK13392    6 SYFDAALAQLHQEGRYRVFADLErEAGRFPRARdhgpdgPRRVTIWCSNDYLGMGQHPDVIGAMVDA-LDRYGAGAGGTR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  75 LLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLA--LPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDL 152
Cdd:PRK13392   85 NISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGklLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 153 SHLRKILSRyADQYDTLWLITESLFSMDGDIAPLQELVALKEEYPHLyIYVDEAHAVGLFGPKGLGLAAEMGVTREIDLL 232
Cdd:PRK13392  165 ADLEEQLAS-VDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNAL-TYVDEVHAVGLYGARGGGIAERDGLMDRIDMI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 233 IGTLGKALGSVGAYSLQSDTLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGRE--- 309
Cdd:PRK13392  243 QGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANgip 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092786827 310 ---FTSQIIPLIVPGEEQVTKAAEQLCR-HGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLA 371
Cdd:PRK13392  323 vmpSPSHIVPVMVGDPTLCKAISDRLMSeHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALV 388
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 33-370 3.14e-56

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 191.04  E-value: 3.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  33 KGRQLLNLNSNDYLGLLAEPQLWQ---RFIEEEGKrrhpSSGSSRLLTGNSPVAQQFESELANAYGLGSALLWDSGYHAN 109
Cdd:PLN02955  100 RFKKLLLFSGNDYLGLSSHPTISNaaaNAAKEYGM----GPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAAN 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 110 TGIPPVLALPNTLFIA--------------DKLVHASIIDGLRLS----GAPFQRYRHNDLSHLRKILSRYADQYDTLwl 171
Cdd:PLN02955  176 MAAMVAIGSVASLLAAsgkplknekvaifsDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKMKRKVV-- 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 172 ITESLFSMDGDIAPLQELVALKEEYPHLYIyVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIGTLGKALGSVGAYSLQSD 251
Cdd:PLN02955  254 VTDSLFSMDGDFAPMEELSQLRKKYGFLLV-IDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSK 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 252 TLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGREFTSQIIPLIVPGEEQVTKAAEQ 331
Cdd:PLN02955  333 KWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKALSGVDISSPIISLVVGNQEKALKASRY 412

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1092786827 332 LCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQL 370
Cdd:PLN02955  413 LLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKL 451
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
27-377 2.29e-49

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 171.35  E-value: 2.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  27 GKYIdVKGRQ----LLNLNSNDYLGLLAEPQLWQRFIEEEGKRRHPSSGSSRLLTGNSPvAQQFESELANAYGLGSALLW 102
Cdd:PRK07179   43 GKHL-VLGKTpgpdAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSP-KPQFEKKLAAFTGFESCLLC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 103 DSGYHANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRYADQYdtlwLITESLFSMDGD 182
Cdd:PRK07179  121 QSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPGI----IVVDSVYSTTGT 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 183 IAPLQELVALKEEYPHLYIyVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIGTLGKALGSVGAYSLQSDTLRQLLVSKAR 262
Cdd:PRK07179  197 IAPLADIVDIAEEFGCVLV-VDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSY 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 263 SLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHL----KDLVTLFgKEMGREF--TSQIIPLiVPGEEQVTKAA-EQLCRH 335
Cdd:PRK07179  276 PAIFSSTLLPHEIAGLEATLEVIESADDRRARLhanaRFLREGL-SELGYNIrsESQIIAL-ETGSERNTEVLrDALEER 353

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1092786827 336 GFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLANLCNSI 377
Cdd:PRK07179  354 NVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREA 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
35-377 2.74e-42

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 150.92  E-value: 2.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  35 RQLLNLNSNDYLGLLAEpqlwqrFIEEEGKRRHpsSGSSRLLTGNSPVAQQFESELANAYGLGSALLWD--------SGY 106
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP------AVAKAEKDAL--AGGTRNLYGPTDGHPELREALAKFLGRSPVLKLDreaavvfgSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 107 HAN-TGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYR-------HNDLSHLRKILSRyadqyDTLWLITESLFS 178
Cdd:pfam00155  73 GANiEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE-----KPKVVLHTSPHN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 179 MDGDIAP---LQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGlAAEMGVTREIDLLI-GTLGKALGSVG---AYSLQSD 251
Cdd:pfam00155 148 PTGTVATleeLEKLLDLAKEH-NILLLVDEAYAGFVFGSPDAV-ATRALLAEGPNLLVvGSFSKAFGLAGwrvGYILGNA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 252 TLRQLLVSKARSLIFSTALPEVNVAWSRFLFHAIQEMDDRRQHLKDLVTLFGKEMGRE----FTSQ--IIPLIVPGEEQV 325
Cdd:pfam00155 226 AVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAglsvLPSQagFFLLTGLDPETA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1092786827 326 TKAAEQLC-RHGFYIRPIRRPTVPqgsERLRLSLtAAMTTDEiiqLANLCNSI 377
Cdd:pfam00155 306 KELAQVLLeEVGVYVTPGSSPGVP---GWLRITV-AGGTEEE---LEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
 33-276 2.90e-41

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 151.45  E-value: 2.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  33 KGRQLLNLNSNDYLGLLAEPQLWQRFIEEEGKRRHPSSGSSRLLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTGI 112
Cdd:PLN02483   98 KTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTI 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 113 PPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKIL--------SRYADQYDTLWLITESLFSMDGDIA 184
Cdd:PLN02483  178 IPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLreqiaegqPRTHRPWKKIIVIVEGIYSMEGELC 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 185 PLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGV-TREIDLLIGTLGKALGSVGAYSLQSDTLRQLLVSKARS 263
Cdd:PLN02483  258 KLPEIVAVCKKY-KAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPA 336

                         250
                  ....*....|...
gi 1092786827 264 LIFSTALPEVNVA 276
Cdd:PLN02483  337 HLYATSMSPPAVQ 349
PRK07505 PRK07505
hypothetical protein; Provisional
 26-373 2.91e-39

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 143.97  E-value: 2.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  26 RGKYIDV-KGRQLLNLNSNDYLGLLAEPQLWQ---RFIEEEGKRRHPSSgSSRLltgNSPVAQQFESELANAYGlGSALL 101
Cdd:PRK07505   36 EGILITLaDGHTFVNFVSCSYLGLDTHPAIIEgavDALKRTGSLHLSSS-RTRV---RSQILKDLEEALSELFG-ASVLT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 102 WDSGYHANTGIPPVLA---LPNT---LFIADKLVHAS--IIDGLRLSGAPFQRYRHNDLSHLRKIlsryADQYDTLWLIT 173
Cdd:PRK07505  111 FTSCSAAHLGILPLLAsghLTGGvppHMVFDKNAHASlnILKGICADETEVETIDHNDLDALEDI----CKTNKTVAYVA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 174 ESLFSMdGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLA-AEMGVT-REIDLLIGTLGKALGSVGAYSL--- 248
Cdd:PRK07505  187 DGVYSM-GGIAPVKELLRLQEKY-GLFLYIDDAHGLSIYGKNGEGYVrSELDYRlNERTIIAASLGKAFGASGGVIMlgd 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 249 --QSDTLRQLLVSKARSLIFSTALPEVNVAWSRFlfHAIQEMDDRRQHLKDLVTLFGKEMGREFTSQIIP--LIVPG-EE 323
Cdd:PRK07505  265 aeQIELILRYAGPLAFSQSLNVAALGAILASAEI--HLSEELDQLQQKLQNNIALFDSLIPTEQSGSFLPirLIYIGdED 342

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092786827 324 QVTKAAEQLCRHGFYIRPIRRPTVPQGSERLRLSLTAAMTTDEIIQLANL 373
Cdd:PRK07505  343 TAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSL 392
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 42-376 2.60e-36

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 135.68  E-value: 2.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  42 SNDYLGLLAEPQL-------WQRFIEEEGKRRHPSSGSsRLLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPP 114
Cdd:PRK05937   11 TNDFLGFSRSDTLvhevekrYRLYCRQFPHAQLGYGGS-RAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 115 VLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRY-ADQYDTLWLITESLFSMDGDIAPLQELVALK 193
Cdd:PRK05937   90 HLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCrQRSFGRIFIFVCSVYSFKGTLAPLEQIIALS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 194 EEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTREIDLLIgTLGKALGSVGAYSLQSDTLRQLLVSKARSLIFSTALP-- 271
Cdd:PRK05937  170 KKY-HAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPph 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 272 ---EVNVAWSrflfHAIQEMDDRRQHLKDLVTLFGKEMGREFTSQIIPLIVPG---EEQVTKAAEQLCRHGFyIRPIRRP 345
Cdd:PRK05937  248 lliSIQVAYD----FLSQEGELARKQLFRLKEYFAQKFSSAAPGCVQPIFLPGiseQELYSKLVETGIRVGV-VCFPTGP 322

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1092786827 346 TvpqgserLRLSLTAAMTTDEIIQLANLCNS 376
Cdd:PRK05937  323 F-------LRVNLHAFNTEDEVDILVSVLAT 346
PLN02822 PLN02822
serine palmitoyltransferase
 27-271 4.97e-26

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 108.68  E-value: 4.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  27 GKYIDVKGRQLLNLNSNDYLGLLAEPQLWQRFIEEEGKRRHPSSGSsRLLTGNSPVAQQFESELANAYGLGSALLWDSGY 106
Cdd:PLN02822  101 GPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGP-RGFYGTIDVHLDCETKIAKFLGTPDSILYSYGL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 107 HANTGIPPVLALPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRYADQYDTL-----WLITESLFSMDG 181
Cdd:PLN02822  180 STIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKRKkklrrYIVVEAIYQNSG 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 182 DIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGVTRE-IDLLIGTLGKALGSVGAYSLQSDTL--RQLLV 258
Cdd:PLN02822  260 QIAPLDEIVRLKEKY-RFRVLLDESNSFGVLGKSGRGLSEHFGVPIEkIDIITAAMGHALATEGGFCTGSARVvdHQRLS 338

                         250
                  ....*....|...
gi 1092786827 259 SKArsLIFSTALP 271
Cdd:PLN02822  339 SSG--YVFSASLP 349
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 38-298 3.45e-25

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 105.37  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827  38 LNLNSNDYLGLLAEPQLWQRfIEEEGKRRHPSSGSSRLLTGNSPVAQQFESELANAYGLGSALLWDSGYHANTGIPPVLA 117
Cdd:PLN03227    1 LNFATHDFLSTSSSPTLRQT-ALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 118 LPNTLFIADKLVHASIIDGLRLSGAPFQRYRHNDLSHLRKILSRYADQYDTL---------WLITESLFSMDGDIAPLQE 188
Cdd:PLN03227   80 KRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALkrkptdqrrFLVVEGLYKNTGTLAPLKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 189 LVALKEEYpHLYIYVDEAHAVGLFGPKGLGLAAEMGV--TREIDLLIGTLGKALGSVGAYSLQSDTLRQLLVSKARSLIF 266
Cdd:PLN03227  160 LVALKEEF-HYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCF 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1092786827 267 STALPEVNVAWSrflFHAIQEMDDRRQHLKDL 298
Cdd:PLN03227  239 SASAPPFLAKAD---ATATAGELAGPQLLNRL 267
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 104-245 7.69e-03

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: 36.98  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092786827 104 SGYHANTGIPPVLALPNTLFIADKLVHASII-DGLRLSGAPFQRYRHNDLSHLR---KILSRYADQYDTLWLITESLFSM 179
Cdd:cd01494    25 SGTGANEAALLALLGPGDEVIVDANGHGSRYwVAAELAGAKPVPVPVDDAGYGGldvAILEELKAKPNVALIVITPNTTS 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092786827 180 DGDIAPLQELVALKEEYpHLYIYVDEAHAVGLFGPKGLglaaEMGVTReIDLLIGTLGKALGSVGA 245
Cdd:cd01494   105 GGVLVPLKEIRKIAKEY-GILLLVDAASAGGASPAPGV----LIPEGG-ADVVTFSLHKNLGGEGG 164
 
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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