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Conserved domains on  [gi|2665660060|ref|WP_329604259|]
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MULTISPECIES: aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [Dethiosulfovibrio]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 10001360)

DegT/DnrJ/EryC1/StrS family aminotransferase such as Bacillus subtilis 3-oxo-glucose-6-phosphate:glutamate aminotransferase and Saccharopolyspora erythraea erythromycin biosynthesis sensory transduction protein EryC1

EC:  2.6.1.-
Gene Ontology:  GO:0008483
PubMed:  17109392
SCOP:  4000675

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
7-381 1.54e-153

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 437.19  E-value: 1.54e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060   7 RIILSPPHMSGDELGFVHEAFESGWIApLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLT 86
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWLT-LGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  87 FIASVSPVTFMGAKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSA 166
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITP------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 167 EALGADYDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDKAPWYQHSEIGYNYRMSNVLAAI 246
Cdd:COG0399   154 QALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKYEHVELGYNYRMDELQAAI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 247 GRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPDETGTTAMdiwKALGDENIESRPVW- 325
Cdd:COG0399   234 GLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGEDRDELI---AALKARGIGTRVHYp 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2665660060 326 KPMHLQPVFEGCGYASHDDGISvgDRLFENGLCLPSGTSMTEQQQDRVIETVKKAL 381
Cdd:COG0399   311 IPLHLQPAYRDLGYRPGDLPVA--ERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
7-381 1.54e-153

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 437.19  E-value: 1.54e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060   7 RIILSPPHMSGDELGFVHEAFESGWIApLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLT 86
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWLT-LGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  87 FIASVSPVTFMGAKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSA 166
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITP------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 167 EALGADYDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDKAPWYQHSEIGYNYRMSNVLAAI 246
Cdd:COG0399   154 QALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKYEHVELGYNYRMDELQAAI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 247 GRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPDETGTTAMdiwKALGDENIESRPVW- 325
Cdd:COG0399   234 GLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGEDRDELI---AALKARGIGTRVHYp 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2665660060 326 KPMHLQPVFEGCGYASHDDGISvgDRLFENGLCLPSGTSMTEQQQDRVIETVKKAL 381
Cdd:COG0399   311 IPLHLQPAYRDLGYRPGDLPVA--ERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
NHT_00031 TIGR04181
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ...
8-362 6.11e-140

aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar.


Pssm-ID: 275034  Cd Length: 359  Bit Score: 402.31  E-value: 6.11e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060   8 IILSPPHMSGDELGFVHEAFESGWIAPLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTF 87
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  88 IASVSPVTFMGAKPYFVDSDEDTWNMSPRALERAIDDLSSK----------GIKPKAAIVAELYGQAPKWDELMPIFDRH 157
Cdd:TIGR04181  81 VATANAISYLGAEPVFVDVDPDTLGLDPDALEEFLEEEAERkdgvlinketGRRIKACVPVHVFGHPADMDEIMEICDEW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 158 DIPVLEDSAEALGADYDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDKAPW-YQHSEIGYN 236
Cdd:TIGR04181 161 NLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPWeFEHDEVGYN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 237 YRMSNVLAAIGRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPDETGTTAMdiwKALGD 316
Cdd:TIGR04181 241 YRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGVEFLPEPAGARSNYWLNALLLDSKLDRDELL---EALNE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2665660060 317 ENIESRPVWKPMHLQPVFEGCgyasHDDGISVGDRLFENGLCLPSG 362
Cdd:TIGR04181 318 NGIQTRPLWTLMHELPMYRDC----PRDDLPVAENLEERLINLPSS 359
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
19-378 2.50e-137

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 395.37  E-value: 2.50e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  19 ELGFVHEAFESGWIaPLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTFIASVSPVTFMG 98
Cdd:cd00616     1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  99 AKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSAEALGADYDGRKC 178
Cdd:cd00616    80 ATPVFVDIDPDTYNIDPELIEAAITP------RTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 179 GTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDK-APWYQHSEIGYNYRMSNVLAAIGRGQMLHLDER 257
Cdd:cd00616   154 GTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRdRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 258 VEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPdETGTTAMDIWKALGDENIESRPVWKPMHLQPVFEGC 337
Cdd:cd00616   234 IARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDP-EAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKL 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2665660060 338 GYASHDDgISVGDRLFENGLCLPSGTSMTEQQQDRVIETVK 378
Cdd:cd00616   313 LGYPPGD-LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
13-378 1.86e-102

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 306.90  E-value: 1.86e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  13 PHMSGDELGFVHEAFESGWIApLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTFIASVS 92
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLT-TGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  93 PVTFMGAKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSAEALGAD 172
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITP------RTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 173 YDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDKAPW--YQHSEIGYNYRMSNVLAAIGRGQ 250
Cdd:pfam01041 154 YQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADkrYWHEVLGYNYRMTEIQAAIGLAQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 251 MLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKK-GRSSMWLTSITVdpDETGTTAMDIWKALGDENIESRPV-WKPM 328
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEaDVHAWHLFPILV--PEEAINRDELVEALKEAGIGTRVHyPIPL 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2665660060 329 HLQPVFEG-CGYASHDdgISVGDRLFENGLCLPSGTSMTEQQQDRVIETVK 378
Cdd:pfam01041 312 HLQPYYRDlFGYAPGD--LPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
10-331 2.65e-47

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 165.20  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  10 LSPPHMSGDELGFVHEAFESGWIAPlGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTFIA 89
Cdd:PRK11658    7 FSRPAMGDEELAAVKEVLRSGWITT-GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  90 SVSPVTFMGAKPYFVDSDEDTWNMSPRALERAiddlsskgIKPKA-AIVAELYGQAP-KWDELMPIFDRHDIPVLEDSAE 167
Cdd:PRK11658   86 TLNMIVLLGATPVMVDVDRDTLMVTPEAIEAA--------ITPRTkAIIPVHYAGAPaDLDAIRAIGERYGIPVIEDAAH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 168 ALGADYDGRKCGTFGRySVLSYNGNKIITTSGGGMLLLDDVESREK------------AFFWATQARdkAPWYQHSEIGY 235
Cdd:PRK11658  158 AVGTYYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRlrslkfhglgvdAFDRQTQGR--APQAEVLTPGY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 236 NYRMSNVLAAIGRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPDETGTTAMDIWKALG 315
Cdd:PRK11658  235 KYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALK 314
                         330
                  ....*....|....*.
gi 2665660060 316 DENIESRPVWKPMHLQ 331
Cdd:PRK11658  315 ERGIGTGLHFRAAHTQ 330
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
7-381 1.54e-153

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 437.19  E-value: 1.54e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060   7 RIILSPPHMSGDELGFVHEAFESGWIApLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLT 86
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWLT-LGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  87 FIASVSPVTFMGAKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSA 166
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITP------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 167 EALGADYDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDKAPWYQHSEIGYNYRMSNVLAAI 246
Cdd:COG0399   154 QALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKYEHVELGYNYRMDELQAAI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 247 GRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPDETGTTAMdiwKALGDENIESRPVW- 325
Cdd:COG0399   234 GLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGEDRDELI---AALKARGIGTRVHYp 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2665660060 326 KPMHLQPVFEGCGYASHDDGISvgDRLFENGLCLPSGTSMTEQQQDRVIETVKKAL 381
Cdd:COG0399   311 IPLHLQPAYRDLGYRPGDLPVA--ERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
NHT_00031 TIGR04181
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ...
8-362 6.11e-140

aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar.


Pssm-ID: 275034  Cd Length: 359  Bit Score: 402.31  E-value: 6.11e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060   8 IILSPPHMSGDELGFVHEAFESGWIAPLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTF 87
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  88 IASVSPVTFMGAKPYFVDSDEDTWNMSPRALERAIDDLSSK----------GIKPKAAIVAELYGQAPKWDELMPIFDRH 157
Cdd:TIGR04181  81 VATANAISYLGAEPVFVDVDPDTLGLDPDALEEFLEEEAERkdgvlinketGRRIKACVPVHVFGHPADMDEIMEICDEW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 158 DIPVLEDSAEALGADYDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDKAPW-YQHSEIGYN 236
Cdd:TIGR04181 161 NLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPWeFEHDEVGYN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 237 YRMSNVLAAIGRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPDETGTTAMdiwKALGD 316
Cdd:TIGR04181 241 YRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGVEFLPEPAGARSNYWLNALLLDSKLDRDELL---EALNE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2665660060 317 ENIESRPVWKPMHLQPVFEGCgyasHDDGISVGDRLFENGLCLPSG 362
Cdd:TIGR04181 318 NGIQTRPLWTLMHELPMYRDC----PRDDLPVAENLEERLINLPSS 359
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
19-378 2.50e-137

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 395.37  E-value: 2.50e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  19 ELGFVHEAFESGWIaPLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTFIASVSPVTFMG 98
Cdd:cd00616     1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  99 AKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSAEALGADYDGRKC 178
Cdd:cd00616    80 ATPVFVDIDPDTYNIDPELIEAAITP------RTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 179 GTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDK-APWYQHSEIGYNYRMSNVLAAIGRGQMLHLDER 257
Cdd:cd00616   154 GTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRdRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 258 VEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPdETGTTAMDIWKALGDENIESRPVWKPMHLQPVFEGC 337
Cdd:cd00616   234 IARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDP-EAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKL 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2665660060 338 GYASHDDgISVGDRLFENGLCLPSGTSMTEQQQDRVIETVK 378
Cdd:cd00616   313 LGYPPGD-LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
13-378 1.86e-102

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 306.90  E-value: 1.86e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  13 PHMSGDELGFVHEAFESGWIApLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTFIASVS 92
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLT-TGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  93 PVTFMGAKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSAEALGAD 172
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITP------RTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 173 YDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWATQARDKAPW--YQHSEIGYNYRMSNVLAAIGRGQ 250
Cdd:pfam01041 154 YQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADkrYWHEVLGYNYRMTEIQAAIGLAQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 251 MLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKK-GRSSMWLTSITVdpDETGTTAMDIWKALGDENIESRPV-WKPM 328
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEaDVHAWHLFPILV--PEEAINRDELVEALKEAGIGTRVHyPIPL 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2665660060 329 HLQPVFEG-CGYASHDdgISVGDRLFENGLCLPSGTSMTEQQQDRVIETVK 378
Cdd:pfam01041 312 HLQPYYRDlFGYAPGD--LPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
13-381 1.73e-75

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 238.77  E-value: 1.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  13 PHMSGDELGFVHEAFESGWIAPlGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTFIASVS 92
Cdd:TIGR03588   6 QSIDQDDIDAVVEVLKSDFLTQ-GPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATAN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  93 PVTFMGAKPYFVDSDEDTWNMSPRALERAIddLSSKGIKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSAEALGAD 172
Cdd:TIGR03588  85 CALYCGAKVDFVDIDPDTGNIDEDALEKKL--AAAKGKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 173 YDGRK--CGTFGRYSVLSYNGNKIITTSGGGMLLLDDVESREKAFFWAT----------QARDKAPW-YQHSEIGYNYRM 239
Cdd:TIGR03588 163 YGGKPvgNCRYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRShgitkdpllfEKQDEGPWyYEQQELGFNYRM 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 240 SNVLAAIGRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPdETGTTAMDIWKALGDENI 319
Cdd:TIGR03588 243 TDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQ-EFGCTRKEVFEALRAAGI 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2665660060 320 ESRPVWKPMHLQPVFEGcGYASHDdgISVGDRLFENGLCLPSGTSMTEQQQDRVIETVKKAL 381
Cdd:TIGR03588 322 GVQVHYIPVHLQPYYRQ-GFGDGD--LPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
10-331 2.65e-47

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 165.20  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  10 LSPPHMSGDELGFVHEAFESGWIAPlGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLTFIA 89
Cdd:PRK11658    7 FSRPAMGDEELAAVKEVLRSGWITT-GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  90 SVSPVTFMGAKPYFVDSDEDTWNMSPRALERAiddlsskgIKPKA-AIVAELYGQAP-KWDELMPIFDRHDIPVLEDSAE 167
Cdd:PRK11658   86 TLNMIVLLGATPVMVDVDRDTLMVTPEAIEAA--------ITPRTkAIIPVHYAGAPaDLDAIRAIGERYGIPVIEDAAH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 168 ALGADYDGRKCGTFGRySVLSYNGNKIITTSGGGMLLLDDVESREK------------AFFWATQARdkAPWYQHSEIGY 235
Cdd:PRK11658  158 AVGTYYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRlrslkfhglgvdAFDRQTQGR--APQAEVLTPGY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 236 NYRMSNVLAAIGRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLTSITVDPDETGTTAMDIWKALG 315
Cdd:PRK11658  235 KYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALK 314
                         330
                  ....*....|....*.
gi 2665660060 316 DENIESRPVWKPMHLQ 331
Cdd:PRK11658  315 ERGIGTGLHFRAAHTQ 330
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
7-382 3.71e-44

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 156.53  E-value: 3.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060   7 RIILSPPHMSGDELGFVHEAFESGWIAPLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLGVETGDVVLCSSLT 86
Cdd:PRK11706    1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  87 FIASVSPVTFMGAKPYFVDSDEDTWNMSPRALERAIDDlsskgiKPKaAIVAELY-GQAPKWDELMPIFDRHDIPVLEDS 165
Cdd:PRK11706   81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITP------KTR-AIVPVHYaGVACEMDTIMALAKKHNLFVVEDA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 166 AEALGADYDGRKCGTFGRYSVLSYNGNKIITTSGGGMLLLDD---VES----REK-----AFFwatqaR---DKAPWyqh 230
Cdd:PRK11706  154 AQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDpalIERaeiiREKgtnrsQFF-----RgqvDKYTW--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 231 SEIGYNYRMSNVLAAIGRGQMLHLDERVEAKRAVYKRYEKAFSDIpgialmpeAKKGRssmwLTSITVDPDETGTTAM-- 308
Cdd:PRK11706  226 VDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPL--------AEAGR----IELPSIPDDCKHNAHMfy 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 309 ----------DIWKALGDENIESRPVWKPMHLQPVFEGCGYASHDDGISvgDRLFENGLCLPSGTSMTEQQQDRVIETVK 378
Cdd:PRK11706  294 iklrdledrsALINFLKEAGIMAVFHYIPLHSSPAGERFGRFHGEDRYT--TKESERLLRLPLFYNLTDVEQRTVIDTIL 371

                  ....
gi 2665660060 379 KALK 382
Cdd:PRK11706  372 EFFS 375
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
30-383 5.55e-38

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 141.56  E-value: 5.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  30 GWIApLGPQVDAFERETSDYIGRPQALALSSGTAALHLGLR-----LLG---VETGDVVLCSSLTFIASVSPVTFMGAKP 101
Cdd:PRK15407   57 FWLT-TGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSaltspKLGdraLKPGDEVITVAAGFPTTVNPIIQNGLVP 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 102 YFVDSDEDTWNMSPRALERAIDDlsskgiKPKAAIVAELYGQAPKWDELMPIFDRHDIPVLEDSAEALGADYDGRKCGTF 181
Cdd:PRK15407  136 VFVDVELPTYNIDASLLEAAVSP------KTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTF 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 182 GRYSVLSYNGNKIITTSGGGMLLLDD------VES-RE----------------KAFFWatQARDKAPWYQH----SEIG 234
Cdd:PRK15407  210 GDIATLSFYPAHHITMGEGGAVFTNDpllkkiIESfRDwgrdcwcapgcdntcgKRFGW--QLGELPFGYDHkytySHLG 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060 235 YNYRMSNVLAAIGRGQMLHLDERVEAKRAVYKRYEKAFSDIPGIALMPEAKKGRSSMWLT-SITVDPDeTGTTAMDIWKA 313
Cdd:PRK15407  288 YNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLEDFLILPEATPNSDPSWFGfPITVKED-AGFTRVELVKY 366
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2665660060 314 LGDENIESRPVW-----KpmhlQPVFEGCGYASHDDgISVGDRLFENGLCLPSGTSMTEQQQDRVIETVKKALKR 383
Cdd:PRK15407  367 LEENKIGTRLLFagnltR----QPYFKGVKYRVVGE-LTNTDRIMNDTFWIGVYPGLTEEMLDYVIEKIEEFFGL 436
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
51-203 7.30e-11

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: 60.47  E-value: 7.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  51 GRPQALALSSGTAALHLGLRLLgVETGDVVLCSSLTFIAS-VSPVTFMGAKPYFVDSDEDTwnmsprALERAIDDLS-SK 128
Cdd:cd01494    16 GNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRyWVAAELAGAKPVPVPVDDAG------YGGLDVAILEeLK 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2665660060 129 GIKPKAAIVAE----LYGQAPKWDELMPIFDRHDIPVLEDSAEALGADYDGRKCGTFGRYSVLSYNGNKIITTSGGGML 203
Cdd:cd01494    89 AKPNVALIVITpnttSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGVV 167
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
59-166 7.13e-07

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 50.80  E-value: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  59 SSGTAALHLGLRLLgVETGDVVLCSSLTFIASVSPVTFMGAKPYFVDSDEDTWNMSPRALERAIddlssKGIKPKAAIVA 138
Cdd:cd00609    66 NGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAA-----KTPKTKLLYLN 139
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2665660060 139 elYGQAP--------KWDELMPIFDRHDIPVLEDSA 166
Cdd:cd00609   140 --NPNNPtgavlseeELEELAELAKKHGILIISDEA 173
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
40-171 2.63e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 45.76  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  40 DAFERETSDYIGRPQALAL--------SSGTAALHLGLRLLGVETGDVVLCSSLTFiASVSP-VTFMGAKPYFVD-SDED 109
Cdd:pfam00155  42 PELREALAKFLGRSPVLKLdreaavvfGSGAGANIEALIFLLANPGDAILVPAPTY-ASYIRiARLAGGEVVRYPlYDSN 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2665660060 110 TWNMSPRALERAIDDlsskgiKPKAAIVAELY---GQAP---KWDELMPIFDRHDIPVLEDSAEALGA 171
Cdd:pfam00155 121 DFHLDFDALEAALKE------KPKVVLHTSPHnptGTVAtleELEKLLDLAKEHNILLLVDEAYAGFV 182
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
37-166 4.33e-05

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 44.90  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2665660060  37 PQVDAFERETSDYIGRPQALALSSGTAALHLGLRLLgVETGDVVLC---SSLTFIASVSPVTFMGAKPYFVDSDEDTwNM 113
Cdd:pfam01212  32 PTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICgepAHIHFDETGGHAELGGVQPRPLDGDEAG-NM 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2665660060 114 SPRALERAIDDLSSKGIKPKAAIVAE-----LYGQAPKWDELMPIF---DRHDIPVLEDSA 166
Cdd:pfam01212 110 DLEDLEAAIREVGADIFPPTGLISLEnthnsAGGQVVSLENLREIAalaREHGIPVHLDGA 170
PucR pfam07905
Purine catabolism regulatory protein-like family; The bacterial proteins found in this family ...
111-163 2.78e-03

Purine catabolism regulatory protein-like family; The bacterial proteins found in this family are similar to the purine catabolism regulatory protein expressed by Bacillus subtilis (PucR). PucR is thought to be a transcriptional activator involved in the induction of the purine degradation pathway, and may contain a LysR-like DNA-binding domain. It is similar to LysR-type regulators in that it represses its own expression. The other members of this family are also annotated as being putative regulatory proteins.


Pssm-ID: 462312 [Multi-domain]  Cd Length: 117  Bit Score: 37.44  E-value: 2.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2665660060 111 WNMSPRALERAIDDLSSKGIkpkAAIVAELYGQAPkwDELMPIFDRHDIPVLE 163
Cdd:pfam07905  52 LKDDPEALAELVRELAEAGV---AGLGIKLGREIP--EELIEAADELGLPLIE 99
 
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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