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Conserved domains on  [gi|1085262085|gb|OGU42390|]
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8-amino-7-oxononanoate synthase [Ignavibacteria bacterium GWB2_35_12]

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]; ...
 13-394 0e+00

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: 515.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  13 TRADEVKKLGLYPYFHPIEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNE 92
Cdd:COG0156     7 AELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  93 LESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGI 172
Cdd:COG0156    87 LEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSG---AKVVRFRHNDMDDLERLLKKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 173 PDRAPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFASLG 252
Cdd:COG0156   164 RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 253 GFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPVI 332
Cdd:COG0156   244 GFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVI 323

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085262085 333 VGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVFGMVGRE 394
Cdd:COG0156   324 VGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 13-394 0e+00

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: 515.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  13 TRADEVKKLGLYPYFHPIEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNE 92
Cdd:COG0156     7 AELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  93 LESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGI 172
Cdd:COG0156    87 LEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSG---AKVVRFRHNDMDDLERLLKKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 173 PDRAPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFASLG 252
Cdd:COG0156   164 RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 253 GFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPVI 332
Cdd:COG0156   244 GFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVI 323

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085262085 333 VGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVFGMVGRE 394
Cdd:COG0156   324 VGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 28-388 7.27e-133

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: 385.08  E-value: 7.27e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  28 HPIEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVL 107
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 108 LFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGIPDRAPKLIVSDGVFS 187
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSG---ARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 188 VTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESE-IDLVMGTFSKTFASLGGFVAGKERVINYLK 266
Cdd:TIGR00858 158 MDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpVDIQVGTLSKALGSYGAYVAGSQALIDYLI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 267 HLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPVIVGDVEKAFIFWRKL 346
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1085262085 347 FDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVF 388
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 49-392 1.74e-130

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: 378.83  E-value: 1.74e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  49 GSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGE 128
Cdd:cd06454     7 CSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAGKGD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 129 YVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGIPDRA-PKLIVSDGVFSVTGEIVDLEKMNVVAKKHKA 207
Cdd:cd06454    87 LIISDSLNHASIIDGIRLSG---AKKRIFKHNDMEDLEKLLREARRPYgKKLIVTEGVYSMDGDIAPLPELVDLAKKYGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 208 RILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFASLGGFVAGKERVINYLKHLSPAIIFSASPTPASCAATL 287
Cdd:cd06454   164 ILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 288 KALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPS-KTAIIPVIVGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMS 366
Cdd:cd06454   244 AALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRGTA 323

                         330       340
                  ....*....|....*....|....*.
gi 1085262085 367 MMRTSYMASHEDHHLNRILEVFGMVG 392
Cdd:cd06454   324 RLRISLSAAHTKEDIDRLLEALKEVG 349
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 13-387 7.02e-126

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 368.33  E-value: 7.02e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  13 TRADEVKKLGLYPYFHPIEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNE 92
Cdd:PRK05958    9 AALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  93 LESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGi 172
Cdd:PRK05958   89 LEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSR---ARVRRYPHNDVDALEALLAK- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 173 PDRAPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLV-MGTFSKTFASL 251
Cdd:PRK05958  165 WRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIlVGTLGKALGSS 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 252 GGFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPV 331
Cdd:PRK05958  245 GAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPL 324

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085262085 332 IVGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEV 387
Cdd:PRK05958  325 IVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEA 380
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
43-388 1.49e-51

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 175.96  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  43 KEMIMAGSNNYLGLTShPEVKEAAIRAvhkygtGCSGSRYLTGTLDLHNELESRIAKFLG--------YEAVLLFSTGYQ 114
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDA------LAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 115 TSLGTISTLV-TKGEYVISDKENHACIVNACILAKGgfaEFVRFK-------HNDMKDLDKVLtgipDRAPKLIVSDGVF 186
Cdd:pfam00155  74 ANIEALIFLLaNPGDAILVPAPTYASYIRIARLAGG---EVVRYPlydsndfHLDFDALEAAL----KEKPKVVLHTSPH 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 187 SVTGEIV---DLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVsKFKLESEIDL-VMGTFSKTFASLG---GFVAGKE 259
Cdd:pfam00155 147 NPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLlVVGSFSKAFGLAGwrvGYILGNA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 260 RVINYLKHLSPAIIFSaSPTPASCAATL-KALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPVIVGDVEK 338
Cdd:pfam00155 226 AVISQLRKLARPFYSS-THLQAAAAAALsDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPET 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1085262085 339 AFIFWRKLFD-KGIFVNTFIPPGVPPNmsmMRTSyMASHEDHHLNRILEVF 388
Cdd:pfam00155 305 AKELAQVLLEeVGVYVTPGSSPGVPGW---LRIT-VAGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 13-394 0e+00

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: 515.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  13 TRADEVKKLGLYPYFHPIEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNE 92
Cdd:COG0156     7 AELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  93 LESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGI 172
Cdd:COG0156    87 LEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSG---AKVVRFRHNDMDDLERLLKKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 173 PDRAPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFASLG 252
Cdd:COG0156   164 RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 253 GFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPVI 332
Cdd:COG0156   244 GFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVI 323

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085262085 333 VGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVFGMVGRE 394
Cdd:COG0156   324 VGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 28-388 7.27e-133

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: 385.08  E-value: 7.27e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  28 HPIEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVL 107
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 108 LFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGIPDRAPKLIVSDGVFS 187
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSG---ARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 188 VTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESE-IDLVMGTFSKTFASLGGFVAGKERVINYLK 266
Cdd:TIGR00858 158 MDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpVDIQVGTLSKALGSYGAYVAGSQALIDYLI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 267 HLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPVIVGDVEKAFIFWRKL 346
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1085262085 347 FDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVF 388
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 49-392 1.74e-130

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: 378.83  E-value: 1.74e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  49 GSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGE 128
Cdd:cd06454     7 CSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAGKGD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 129 YVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGIPDRA-PKLIVSDGVFSVTGEIVDLEKMNVVAKKHKA 207
Cdd:cd06454    87 LIISDSLNHASIIDGIRLSG---AKKRIFKHNDMEDLEKLLREARRPYgKKLIVTEGVYSMDGDIAPLPELVDLAKKYGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 208 RILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFASLGGFVAGKERVINYLKHLSPAIIFSASPTPASCAATL 287
Cdd:cd06454   164 ILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 288 KALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPS-KTAIIPVIVGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMS 366
Cdd:cd06454   244 AALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRGTA 323

                         330       340
                  ....*....|....*....|....*.
gi 1085262085 367 MMRTSYMASHEDHHLNRILEVFGMVG 392
Cdd:cd06454   324 RLRISLSAAHTKEDIDRLLEALKEVG 349
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 13-387 7.02e-126

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 368.33  E-value: 7.02e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  13 TRADEVKKLGLYPYFHPIEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNE 92
Cdd:PRK05958    9 AALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  93 LESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGi 172
Cdd:PRK05958   89 LEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSR---ARVRRYPHNDVDALEALLAK- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 173 PDRAPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLV-MGTFSKTFASL 251
Cdd:PRK05958  165 WRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIlVGTLGKALGSS 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 252 GGFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPV 331
Cdd:PRK05958  245 GAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPL 324

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085262085 332 IVGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEV 387
Cdd:PRK05958  325 IVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEA 380
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 10-398 1.64e-123

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 362.59  E-value: 1.64e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  10 YNFTRA--DEVKKLGLYPYFHPIEENEGPVVRVE-GKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGT 86
Cdd:PRK06939    6 YAQLREelEEIKAEGLYKEERVITSPQGADITVAdGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  87 LDLHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLD 166
Cdd:PRK06939   86 QDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCK---AKRYRYANNDMADLE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 167 KVLTGIPDRAP--KLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTF 244
Cdd:PRK06939  163 AQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 245 SKTFA-SLGGFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFP 323
Cdd:PRK06939  243 GKALGgASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGP 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085262085 324 SKTAIIPVIVGDVEKAFIFWRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVFGMVGRELGLI 398
Cdd:PRK06939  323 GEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
PLN02483 PLN02483
serine palmitoyltransferase
 49-397 3.62e-67

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 220.79  E-value: 3.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  49 GSNNYLGLTSHPE-VKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKG 127
Cdd:PLN02483  106 GSYNYLGFAAADEyCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 128 EYVISDKENHACIVNAcilAKGGFAEFVRFKHNDMKDLDKVL-TGIPDRAPK--------LIVSDGVFSVTGEIVDLEKM 198
Cdd:PLN02483  186 GLIISDSLNHNSIVNG---ARGSGATIRVFQHNTPSHLEEVLrEQIAEGQPRthrpwkkiIVIVEGIYSMEGELCKLPEI 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 199 NVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLE-SEIDLVMGTFSKTFASLGGFVAGKERVINYLKHLSPAIIFSAS 277
Cdd:PLN02483  263 VAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDpADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATS 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 278 PTPASCAATLKALDIL------EQQPELVTKLIKNSDKMRKGFTEMGFRIFPSK-TAIIPVIVGDVEKAFIFWRKLFDKG 350
Cdd:PLN02483  343 MSPPAVQQVISAIKVIlgedgtNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNdSPVMPIMLYNPAKIPAFSRECLKQN 422

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1085262085 351 IFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVFGMVGRELGL 397
Cdd:PLN02483  423 VAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 5-397 2.96e-61

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 203.16  E-value: 2.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085   5 LFNKCYNFTRA-DEVKKLGLYPYFHPIEENEG--PVVRVEG----KEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGC 77
Cdd:PRK13392    1 MMNYDSYFDAAlAQLHQEGRYRVFADLEREAGrfPRARDHGpdgpRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  78 SGSRYLTGTLDLHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTK--GEYVISDKENHACIVNAciLAKGGfAEFV 155
Cdd:PRK13392   81 GGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEG--IRRSG-AEKQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 156 RFKHNDMKDLDKVLTGIPDRAPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLES 235
Cdd:PRK13392  158 VFRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 236 EIDLVMGTFSKTFASLGGFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFT 315
Cdd:PRK13392  238 RIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 316 EMGFRIFPSKTAIIPVIVGDVEKA-FIFWRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEVFGMVGRE 394
Cdd:PRK13392  318 ANGIPVMPSPSHIVPVMVGDPTLCkAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397


                  ...
gi 1085262085 395 LGL 397
Cdd:PRK13392  398 LEL 400
PLN02822 PLN02822
serine palmitoyltransferase
 30-321 7.79e-58

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 196.12  E-value: 7.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  30 IEENEGPVVRVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVLLF 109
Cdd:PLN02822   96 LESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILY 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 110 STGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGIP---DRAPKL---IVSD 183
Cdd:PLN02822  176 SYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSR---STIVYFKHNDMESLRNTLEKLTaenKRKKKLrryIVVE 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 184 GVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESE-IDLVMGTFSKTFASLGGFVAGKERVI 262
Cdd:PLN02822  253 AIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEkIDIITAAMGHALATEGGFCTGSARVV 332

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 263 NYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEM-GFRI 321
Cdd:PLN02822  333 DHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIpGLSI 392
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 43-376 8.79e-53

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 182.57  E-value: 8.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  43 KEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVLLFSTGY------QTS 116
Cdd:PLN02955  102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFaanmaaMVA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 117 LGTISTLVT------KGEYV--ISDKENHACIVNACILA-KGGFAEFVRFKHNDMKDLDKVLTGIPDRApKLIVSDGVFS 187
Cdd:PLN02955  182 IGSVASLLAasgkplKNEKVaiFSDALNHASIIDGVRLAeRQGNVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDSLFS 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 188 VTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFASLGGFVAGKERVINYLKH 267
Cdd:PLN02955  261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 268 LSPAIIFS-ASPTPAScAATLKALdILEQQPELVTKLIKNSDKMRKGFTEMgfrifPSKTAIIPVIVGDVEKAFIFWRKL 346
Cdd:PLN02955  341 RGRSFIFStAIPVPMA-AAAYAAV-VVARKEKWRRKAIWERVKEFKALSGV-----DISSPIISLVVGNQEKALKASRYL 413

                         330       340       350
                  ....*....|....*....|....*....|
gi 1085262085 347 FDKGIFVNTFIPPGVPPNMSMMRTSYMASH 376
Cdd:PLN02955  414 LKSGFHVMAIRPPTVPPNSCRLRVTLSAAH 443
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
43-388 1.49e-51

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 175.96  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  43 KEMIMAGSNNYLGLTShPEVKEAAIRAvhkygtGCSGSRYLTGTLDLHNELESRIAKFLG--------YEAVLLFSTGYQ 114
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDA------LAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 115 TSLGTISTLV-TKGEYVISDKENHACIVNACILAKGgfaEFVRFK-------HNDMKDLDKVLtgipDRAPKLIVSDGVF 186
Cdd:pfam00155  74 ANIEALIFLLaNPGDAILVPAPTYASYIRIARLAGG---EVVRYPlydsndfHLDFDALEAAL----KEKPKVVLHTSPH 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 187 SVTGEIV---DLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVsKFKLESEIDL-VMGTFSKTFASLG---GFVAGKE 259
Cdd:pfam00155 147 NPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLlVVGSFSKAFGLAGwrvGYILGNA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 260 RVINYLKHLSPAIIFSaSPTPASCAATL-KALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIFPSKTAIIPVIVGDVEK 338
Cdd:pfam00155 226 AVISQLRKLARPFYSS-THLQAAAAAALsDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPET 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1085262085 339 AFIFWRKLFD-KGIFVNTFIPPGVPPNmsmMRTSyMASHEDHHLNRILEVF 388
Cdd:pfam00155 305 AKELAQVLLEeVGVYVTPGSSPGVPGW---LRIT-VAGGTEEELEELLEAI 351
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 50-332 7.68e-50

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 172.78  E-value: 7.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  50 SNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLTGTLDLHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEY 129
Cdd:PLN03227    5 THDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKRGDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 130 VISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVLTGI--PDRAPKL--------IVSDGVFSVTGEIVDLEKMN 199
Cdd:PLN03227   85 LVVDRGVNEALLVGVSLSR---ANVRWFRHNDMKDLRRVLEQVraQDVALKRkptdqrrfLVVEGLYKNTGTLAPLKELV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 200 VVAKKHKARILIDDAHGIGVIGNGGRGTVSKF--KLESEIDLVMGTFSKTFASLGGFVAGKERVINYLKHLSPAIIFSAS 277
Cdd:PLN03227  162 ALKEEFHYRLILDESFSFGTLGKSGRGSLEHAglKPMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSAS 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085262085 278 PTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFT--------EMGFRIFPSKTAIIPVI 332
Cdd:PLN03227  242 APPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTnsshpyalKLRNRLVITSDPISPII 304
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
32-387 1.45e-46

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 164.41  E-value: 1.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  32 ENEGPVV--RVEGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGTGCSGSRYLtgtldLHNE-----LESRIAKFLGYE 104
Cdd:PRK07179   41 WNGKHLVlgKTPGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVF-----LHDDspkpqFEKKLAAFTGFE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 105 AVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKggfAEFVRFKHNDMKDLDKVltgIPDRAPKLIVSDG 184
Cdd:PRK07179  116 SCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAG---AQAHPFRHNDVDHLRRQ---IERHGPGIIVVDS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 185 VFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFASLGGFVAGKERVINY 264
Cdd:PRK07179  190 VYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEY 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 265 LKHLS-PAiIFSASPTPASCAATLKALDILEQQPELVTKLIKNSDKMRKGFTEMGFRIfPSKTAIIPVIVGDVEKAFIFW 343
Cdd:PRK07179  270 VPFVSyPA-IFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNI-RSESQIIALETGSERNTEVLR 347

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1085262085 344 RKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHEDHHLNRILEV 387
Cdd:PRK07179  348 DALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEV 391
PRK07505 PRK07505
hypothetical protein; Provisional
 41-378 1.37e-27

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 112.77  E-value: 1.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  41 EGKEMIMAGSNNYLGLTSHPEVKEAAIRAVHKYGT---GCSGSRYLTGTLDlhnELESRIAKFLGYEaVLLFSTGYQTSL 117
Cdd:PRK07505   44 DGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlhlSSSRTRVRSQILK---DLEEALSELFGAS-VLTFTSCSAAHL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 118 GTI----STLVTKGE--YVISDKENHACI-VNACILAKggFAEFVRFKHNDMKDLDKvltgIPDRAPKLI-VSDGVFSvT 189
Cdd:PRK07505  120 GILpllaSGHLTGGVppHMVFDKNAHASLnILKGICAD--ETEVETIDHNDLDALED----ICKTNKTVAyVADGVYS-M 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 190 GEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKfKLESEID---LVMGTFSKTFASLGGFVA-GKERVINYL 265
Cdd:PRK07505  193 GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVRS-ELDYRLNertIIAASLGKAFGASGGVIMlGDAEQIELI 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 266 KHLSPAIIFSASPTPASCAATLKALDI--LEQQPELVTKLIKNSdkmrKGF-TEMGFRIFPSKTAIIPVIVGDVEKAFIF 342
Cdd:PRK07505  272 LRYAGPLAFSQSLNVAALGAILASAEIhlSEELDQLQQKLQNNI----ALFdSLIPTEQSGSFLPIRLIYIGDEDTAIKA 347

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1085262085 343 WRKLFDKGIFVNTFIPPGVPPNMSMMRTSYMASHED 378
Cdd:PRK07505  348 AKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTN 383
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 76-306 4.86e-20

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 90.61  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  76 GCSGSRYLTGTLDLHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKGgfaEFV 155
Cdd:PRK05937   44 GYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISG---WHQ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 156 RFKHNDMKDLDKVLTGIPDRAPK--LIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGRGTVSKFKL 233
Cdd:PRK05937  121 SFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085262085 234 ESeIDLVMGTFSKTFASLGGFVAGKERVINYLKHLSPAIIFSASPTPASCAATLKALDILEQQPELVTKLIKN 306
Cdd:PRK05937  201 EN-FYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPHLLISIQVAYDFLSQEGELARKQLFR 272
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 194-363 3.00e-09

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 58.12  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 194 DLEKMNVVAKKHKARILIDDAHGiGVIGNGGRGTVSKFKLESEIDLVMGTFSKTFAS----LGGFVAGKERVINYLKHLS 269
Cdd:cd00609   153 ELEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLpglrIGYLIAPPEELLERLKKLL 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 270 PAIIFSASPTPAscAATLKALDILEQQ-PELVTKLIKNSDKMRKGFTEMGF--RIFPSKT--AIIPVIVGDVEKAfiFWR 344
Cdd:cd00609   232 PYTTSGPSTLSQ--AAAAAALDDGEEHlEELRERYRRRRDALLEALKELGPlvVVKPSGGffLWLDLPEGDDEEF--LER 307

                         170
                  ....*....|....*....
gi 1085262085 345 KLFDKGIFVNTFIPPGVPP 363
Cdd:cd00609   308 LLLEAGVVVRPGSAFGEGG 326
Cys_Met_Meta_PP pfam01053
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ...
 80-212 1.11e-06

Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.


Pssm-ID: 395837 [Multi-domain]  Cd Length: 376  Bit Score: 50.31  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  80 SRYLTGTldlHNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNAC--ILAKGGfaefVRF 157
Cdd:pfam01053  42 SRSGNPT---RDVLEERIAALEGGAAALAFSSGMAAITAAILALLKAGDHIVATDDLYGGTYRLFnkVLPRFG----IEV 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1085262085 158 KHNDMKDLDKVLTGIPDRaPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILID 212
Cdd:pfam01053 115 TFVDTSDPEDLEAAIKPN-TKAVYLETPTNPLLKVVDIEAIAKLAKKHGILVVVD 168
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 89-258 2.78e-06

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: 46.99  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  89 LHNELESRIAKFL--GYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNACILAKGgfAEFVRFKHNDMKDLD 166
Cdd:cd01494     1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAG--AKPVPVPVDDAGYGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 167 KVLTGIPDRA----PKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAHGIGVIGNGGrgtvsKFKLESEIDLVMG 242
Cdd:cd01494    79 LDVAILEELKakpnVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPG-----VLIPEGGADVVTF 153

                         170
                  ....*....|....*..
gi 1085262085 243 TFSKTF-ASLGGFVAGK 258
Cdd:cd01494   154 SLHKNLgGEGGGVVIVK 170
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 239-353 4.58e-06

Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439849 [Multi-domain]  Cd Length: 341  Bit Score: 48.20  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 239 LVMGTFSKTFAsLG----GFVAGKERVINYL-KHLSPaiiFSASpTPAsCAATLKALDILEQQPELVTKLIKNSDKMRKG 313
Cdd:COG0079   198 VVLRTFSKAYG-LAglrlGYAIASPELIAALrRVRGP---WNVN-SLA-QAAALAALEDRAYLEETRARLRAERERLAAA 271

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1085262085 314 FTEMGFRIFPSKTAIipVIVGDVEKAFIFWRKLFDKGIFV 353
Cdd:COG0079   272 LRALGLTVYPSQANF--VLVRVPEDAAELFEALLERGILV 309
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 65-218 1.98e-05

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


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 46.09  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  65 AAIRAVHKYGTgcsgsrYLTgtlDLHNELESRIAKFLG----YEAVLLFSTGYQTSL---GTISTLVTKGEYVISDKENH 137
Cdd:pfam00266  29 NVHRGVHTLGK------EAT---QAYEEAREKVAEFINapsnDEIIFTSGTTEAINLvalSLGRSLKPGDEIVITEMEHH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 138 ACIVNACILAKGGFAEFVRFKHNDMK--DLDKVLTGIPDRaPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDDAH 215
Cdd:pfam00266 100 ANLVPWQELAKRTGARVRVLPLDEDGllDLDELEKLITPK-TKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQ 178


                  ...
gi 1085262085 216 GIG 218
Cdd:pfam00266 179 AIG 181
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 90-212 4.79e-05

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


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 44.89  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  90 HNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVNAC--ILAKGGfaefVRFKHNDMKDLDK 167
Cdd:cd00614    42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASDDLYGGTYRLFerLLPKLG----IEVTFVDPDDPEA 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1085262085 168 VLTGIPDRApKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILID 212
Cdd:cd00614   118 LEAAIKPET-KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 128-212 1.04e-04

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 43.97  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 128 EYVISDKENHACIVNACILA--KGGFAEFVRFKHNDMKDLDKvLTGIPDRAPKLIVSDGVFSVTGEIVDLEKMNVVAKKH 205
Cdd:PLN02855  124 EVILSVAEHHSNIVPWQLVAqkTGAVLKFVGLTPDEVLDVEQ-LKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAV 202


                  ....*..
gi 1085262085 206 KARILID 212
Cdd:PLN02855  203 GAKVLVD 209
PRK06767 PRK06767
methionine gamma-lyase; Provisional
 93-213 2.60e-04

methionine gamma-lyase; Provisional


Pssm-ID: 180685 [Multi-domain]  Cd Length: 386  Bit Score: 42.91  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  93 LESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACIVnacilakgGFAEFVRFKHN------DMKDLD 166
Cdd:PRK06767   66 FEERMAVLEGGEEALAFGSGMAAISATLIGFLKAGDHIICSNGLYGCTY--------GFLEVLEEKFMithsfcDMETEA 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1085262085 167 KVLTGIPDRApKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILIDD 213
Cdd:PRK06767  138 DIENKIRPNT-KLIFVETPINPTMKLIDLKQVIRVAKRNGLLVIVDN 183
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
130-220 4.40e-04

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 42.05  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 130 VISDKENHACIVNACILAKGGFAEFVRFKHN-----DMKDLDKVLTgipDRaPKLIVSDGVFSVTGEIVDLEKMNVVAKK 204
Cdd:COG0520   107 LITEMEHHSNIVPWQELAERTGAEVRVIPLDedgelDLEALEALLT---PR-TKLVAVTHVSNVTGTVNPVKEIAALAHA 182

                          90
                  ....*....|....*.
gi 1085262085 205 HKARILIDDAHGIGVI 220
Cdd:COG0520   183 HGALVLVDGAQSVPHL 198
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
 64-259 6.68e-04

Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.


Pssm-ID: 99745  Cd Length: 361  Bit Score: 41.61  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  64 EAAIRAVHKYGTGCSGSRYLTGTLDLH-----NELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHA 138
Cdd:cd06452    15 PEARKALIEWGDGYSVCDFCRGRLDEIekppiKDFHHDLAEFLGMDEARVTPGAREGKFAVMHSLCEKGDWVVVDGLAHY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 139 CIVNACILAKGGFAEFVRFKHNDMK-DLDKVLTGIPD------RAPKLIVSDGVFSVTGEIVDLEKMNVVAKKHKARILI 211
Cdd:cd06452    95 TSYVAAERAGLNVREVPNTGHPEYHiTPEGYAEVIEEvkdefgKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1085262085 212 DDAHGIGVIGNGGRgtvskfklESEIDLVMGTFSKTFASLG--GFVAGKE 259
Cdd:cd06452   175 NGAYTVGRMPVSGK--------ELGADFIVGSGHKSMAASApiGVLATTE 216
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
91-268 2.13e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 39.51  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  91 NELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEYVISDKENHACI--VNACILAKGGFAEFVRFKHNDMKDLDKV 168
Cdd:pfam01212  35 NRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFdeTGGHAELGGVQPRPLDGDEAGNMDLEDL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085 169 LTGIPDRAPKLIVSDGVFSVT-------GEIVDLEKMNVV---AKKHKARILIDDAH------GIGVIgnggrgtVSkfK 232
Cdd:pfam01212 115 EAAIREVGADIFPPTGLISLEnthnsagGQVVSLENLREIaalAREHGIPVHLDGARfanaavALGVI-------VK--E 185

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1085262085 233 LESEIDLVMGTFSKT-FASLGGFVAGKERVINYLKHL 268
Cdd:pfam01212 186 ITSYADSVTMCLSKGlGAPVGSVLAGSDDFIAKAIRQ 222
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 50-140 6.44e-03

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 38.47  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085262085  50 SNNYLGltSHPEVKEAAIRAVhkYGTGCSGSRYLTgtldlhNELESRIAKFLGYEAVLLFSTGYQTSLGTISTLVTKGEY 129
Cdd:cd06502     4 SDTVTG--PTPEMLEAMAAAN--VGDDVYGEDPTT------AKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGS 73

                          90
                  ....*....|.
gi 1085262085 130 VISDKENHACI 140
Cdd:cd06502    74 VICHETAHIYT 84
 
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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