|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
57-409 |
3.72e-50 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 172.95 E-value: 3.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 57 VLTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVL--IDLNTnHSISLNKIKKHWNANTKAIILTHL 134
Cdd:COG0399 49 VAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAILYVGATPVFvdIDPDT-YNIDPEALEAAITPRTKAIIPVHL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 135 YG--ChdDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNRtiselcdmgEE 211
Cdd:COG0399 128 YGqpA--DMDaIMAIAKKHGLKVIEDAAQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTND---------EE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 212 KKEEVILdYKNHLKTQLAikikKSRVLSLFTNYwrKL-EILPSYNNSKLDSLPEktevINPKRMSIVRslLIDKHLQKTK 290
Cdd:COG0399 197 LAERARS-LRNHGRDRDA----KYEHVELGYNY--RMdELQAAIGLAQLKRLDE----FIARRRAIAA--RYREALADLP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 291 KIleinicnaslcytMLQEIEEKygvkiifsAQNVYlNYFTIIFKESSDRYECSVHLAEKGIQTCWNY-LPLSEIPIFSK 369
Cdd:COG0399 264 GL-------------TLPKVPPG--------AEHVY-HLYVIRLDEGEDRDELIAALKARGIGTRVHYpIPLHLQPAYRD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446372122 370 YATESENI---DYLWPRVLSIPFKYPLVNKDLKYICSQILKYL 409
Cdd:COG0399 322 LGYRPGDLpvaERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
57-405 |
4.34e-45 |
|
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: 159.24 E-value: 4.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 57 VLTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTN-HSISLNKIKKHWNANTKAIILTHLY 135
Cdd:cd00616 37 VAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPVFVDIDPDtYNIDPELIEAAITPRTKAIIPVHLY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 136 GCHDDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNrtiselcDmgEEKKE 214
Cdd:cd00616 117 GNPADMDaIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAGAFSFHPTKNLTTGEGGAVVTN-------D--EELAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 215 EVILdYKNHlktqlaikikksrvlSLFTNYWRKLEILPSYnNSKLDslpektevinpkrmSIVRSLLIDKhLQKTKKILE 294
Cdd:cd00616 188 RARL-LRNH---------------GRDRDRFKYEHEILGY-NYRLS--------------EIQAAIGLAQ-LEKLDEIIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 295 INICNASLCYTMLQEIEekyGVKIIFSAQNVYLNY--FTIIFKESS--DRYECSVHLAEKGIQTCWNYLPLSEIPIFSKY 370
Cdd:cd00616 236 RRREIAERYKELLADLP---GIRLPDVPPGVKHSYhlYVIRLDPEAgeSRDELIEALKEAGIETRVHYPPLHHQPPYKKL 312
|
330 340 350
....*....|....*....|....*....|....*....
gi 446372122 371 ATESE----NIDYLWPRVLSIPFKYPLVNKDLKYICSQI 405
Cdd:cd00616 313 LGYPPgdlpNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
59-405 |
1.10e-38 |
|
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: 142.42 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 59 TNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTN-HSISLNKIKKHWNANTKAIILTHLYGC 137
Cdd:pfam01041 45 VSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAKPVFVDIDPDtYNIDPEAIEAAITPRTKAIIPVHLYGQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 138 HDDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNrtiselcdmgEEKKEEV 216
Cdd:pfam01041 125 PADMDaIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTN----------DPELAEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 217 ILDYKNHlktqlaikikkSRVLSLFTNYWrklEILPSYNNskldslpektevinpkRMSIVRSLLIDKHLQKTKKILEIN 296
Cdd:pfam01041 195 ARVLRNH-----------GMVRKADKRYW---HEVLGYNY----------------RMTEIQAAIGLAQLERLDEFIARR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 297 ICNASLCYTMLQEIEEKYGVKIIFSAQNVYLNYFTIIFKESS-DRYECSVHLAEKGIQTCWNY-LPLSEIPIFSKY---- 370
Cdd:pfam01041 245 REIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPEEAiNRDELVEALKEAGIGTRVHYpIPLHLQPYYRDLfgya 324
|
330 340 350
....*....|....*....|....*....|....*.
gi 446372122 371 ATESENIDYLWPRVLSIPFkYP-LVNKDLKYICSQI 405
Cdd:pfam01041 325 PGDLPNAEDISSRVLSLPL-YPgLTDEDVDRVVEAV 359
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
58-410 |
1.88e-27 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 112.24 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 58 LTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTNH-SISLNKIKKHWNANTKAIILTHLYG 136
Cdd:PRK11706 51 LTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTmNIDETLIEAAITPKTRAIVPVHYAG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 137 CHDDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNRtiSELCDmgeekKEE 215
Cdd:PRK11706 131 VACEMDtIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLIND--PALIE-----RAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 216 VILDyknhlktqlaikiK---KSRVLSLFTN-Y-WRklEILPSYNNSKLDS------LpEKTEVINPKRMSIVRSLlidk 284
Cdd:PRK11706 204 IIRE-------------KgtnRSQFFRGQVDkYtWV--DIGSSYLPSELQAaylwaqL-EAADRINQRRLALWQRY---- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 285 hlqktkkileinicnaslcYTMLQEIEEKYGVKIIFSAQNVYLNY--FTIIFKESSDRYECSVHLAEKGIQTCWNYLPLS 362
Cdd:PRK11706 264 -------------------YDALAPLAEAGRIELPSIPDDCKHNAhmFYIKLRDLEDRSALINFLKEAGIMAVFHYIPLH 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446372122 363 EIPIFSKYATESENIDY---LWPRVLSIPFKYPLVNKDLKYICSQILKYLE 410
Cdd:PRK11706 325 SSPAGERFGRFHGEDRYttkESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
57-409 |
3.72e-50 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 172.95 E-value: 3.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 57 VLTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVL--IDLNTnHSISLNKIKKHWNANTKAIILTHL 134
Cdd:COG0399 49 VAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAILYVGATPVFvdIDPDT-YNIDPEALEAAITPRTKAIIPVHL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 135 YG--ChdDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNRtiselcdmgEE 211
Cdd:COG0399 128 YGqpA--DMDaIMAIAKKHGLKVIEDAAQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTND---------EE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 212 KKEEVILdYKNHLKTQLAikikKSRVLSLFTNYwrKL-EILPSYNNSKLDSLPEktevINPKRMSIVRslLIDKHLQKTK 290
Cdd:COG0399 197 LAERARS-LRNHGRDRDA----KYEHVELGYNY--RMdELQAAIGLAQLKRLDE----FIARRRAIAA--RYREALADLP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 291 KIleinicnaslcytMLQEIEEKygvkiifsAQNVYlNYFTIIFKESSDRYECSVHLAEKGIQTCWNY-LPLSEIPIFSK 369
Cdd:COG0399 264 GL-------------TLPKVPPG--------AEHVY-HLYVIRLDEGEDRDELIAALKARGIGTRVHYpIPLHLQPAYRD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446372122 370 YATESENI---DYLWPRVLSIPFKYPLVNKDLKYICSQILKYL 409
Cdd:COG0399 322 LGYRPGDLpvaERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
57-405 |
4.34e-45 |
|
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: 159.24 E-value: 4.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 57 VLTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTN-HSISLNKIKKHWNANTKAIILTHLY 135
Cdd:cd00616 37 VAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPVFVDIDPDtYNIDPELIEAAITPRTKAIIPVHLY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 136 GCHDDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNrtiselcDmgEEKKE 214
Cdd:cd00616 117 GNPADMDaIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAGAFSFHPTKNLTTGEGGAVVTN-------D--EELAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 215 EVILdYKNHlktqlaikikksrvlSLFTNYWRKLEILPSYnNSKLDslpektevinpkrmSIVRSLLIDKhLQKTKKILE 294
Cdd:cd00616 188 RARL-LRNH---------------GRDRDRFKYEHEILGY-NYRLS--------------EIQAAIGLAQ-LEKLDEIIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 295 INICNASLCYTMLQEIEekyGVKIIFSAQNVYLNY--FTIIFKESS--DRYECSVHLAEKGIQTCWNYLPLSEIPIFSKY 370
Cdd:cd00616 236 RRREIAERYKELLADLP---GIRLPDVPPGVKHSYhlYVIRLDPEAgeSRDELIEALKEAGIETRVHYPPLHHQPPYKKL 312
|
330 340 350
....*....|....*....|....*....|....*....
gi 446372122 371 ATESE----NIDYLWPRVLSIPFKYPLVNKDLKYICSQI 405
Cdd:cd00616 313 LGYPPgdlpNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
59-405 |
1.10e-38 |
|
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: 142.42 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 59 TNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTN-HSISLNKIKKHWNANTKAIILTHLYGC 137
Cdd:pfam01041 45 VSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAKPVFVDIDPDtYNIDPEAIEAAITPRTKAIIPVHLYGQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 138 HDDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNrtiselcdmgEEKKEEV 216
Cdd:pfam01041 125 PADMDaIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTN----------DPELAEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 217 ILDYKNHlktqlaikikkSRVLSLFTNYWrklEILPSYNNskldslpektevinpkRMSIVRSLLIDKHLQKTKKILEIN 296
Cdd:pfam01041 195 ARVLRNH-----------GMVRKADKRYW---HEVLGYNY----------------RMTEIQAAIGLAQLERLDEFIARR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 297 ICNASLCYTMLQEIEEKYGVKIIFSAQNVYLNYFTIIFKESS-DRYECSVHLAEKGIQTCWNY-LPLSEIPIFSKY---- 370
Cdd:pfam01041 245 REIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPEEAiNRDELVEALKEAGIGTRVHYpIPLHLQPYYRDLfgya 324
|
330 340 350
....*....|....*....|....*....|....*.
gi 446372122 371 ATESENIDYLWPRVLSIPFkYP-LVNKDLKYICSQI 405
Cdd:pfam01041 325 PGDLPNAEDISSRVLSLPL-YPgLTDEDVDRVVEAV 359
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
58-410 |
1.88e-27 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 112.24 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 58 LTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTNH-SISLNKIKKHWNANTKAIILTHLYG 136
Cdd:PRK11706 51 LTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTmNIDETLIEAAITPKTRAIVPVHYAG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 137 CHDDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSIGGGALLLNRtiSELCDmgeekKEE 215
Cdd:PRK11706 131 VACEMDtIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLIND--PALIE-----RAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 216 VILDyknhlktqlaikiK---KSRVLSLFTN-Y-WRklEILPSYNNSKLDS------LpEKTEVINPKRMSIVRSLlidk 284
Cdd:PRK11706 204 IIRE-------------KgtnRSQFFRGQVDkYtWV--DIGSSYLPSELQAaylwaqL-EAADRINQRRLALWQRY---- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 285 hlqktkkileinicnaslcYTMLQEIEEKYGVKIIFSAQNVYLNY--FTIIFKESSDRYECSVHLAEKGIQTCWNYLPLS 362
Cdd:PRK11706 264 -------------------YDALAPLAEAGRIELPSIPDDCKHNAhmFYIKLRDLEDRSALINFLKEAGIMAVFHYIPLH 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446372122 363 EIPIFSKYATESENIDY---LWPRVLSIPFKYPLVNKDLKYICSQILKYLE 410
Cdd:PRK11706 325 SSPAGERFGRFHGEDRYttkESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
38-194 |
3.62e-14 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 73.52 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 38 PNDSKLKKSLQALYPDAEIVLTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNT-NHSISLN 116
Cdd:PRK11658 33 PKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLNMIVLLGATPVMVDVDRdTLMVTPE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446372122 117 KIKKHWNANTKAIILTHLYGCHDDLDII-DWARENNIYIIDDAAQAMFSYQNGKPVGSLGdIGILSFGGTKPIPSIGGG 194
Cdd:PRK11658 113 AIEAAITPRTKAIIPVHYAGAPADLDAIrAIGERYGIPVIEDAAHAVGTYYKGRHIGARG-TAIFSFHAIKNITCAEGG 190
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
57-182 |
2.31e-12 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 68.37 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 57 VLTNSGTSALVVGLKYL--------KVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLN-TNHSISLNKIKKHWNANTK 127
Cdd:PRK15407 82 LLVNSGSSANLLAFSALtspklgdrALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVElPTYNIDASLLEAAVSPKTK 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446372122 128 AIILTHLYGCHDDLDII-DWARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSF 182
Cdd:PRK15407 162 AIMIAHTLGNPFDLAAVkAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSF 217
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
51-186 |
2.36e-10 |
|
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440205 [Multi-domain] Cd Length: 387 Bit Score: 61.68 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 51 YPDAEIVLTNSGTSALVVGLKYLkVAKGDEVILSN--FncPNVIEAILTVGAKPVLIDLN--TNHSISLNKIKKHWNANT 126
Cdd:COG0436 88 LDPDEILVTNGAKEALALALLAL-LNPGDEVLVPDpgY--PSYRAAVRLAGGKPVPVPLDeeNGFLPDPEALEAAITPRT 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446372122 127 KAIILT-------HLYGcHDDLD-IIDWARENNIYIIDDAAQAMFSYQNGKPVgslgdiGILSFGGTK 186
Cdd:COG0436 165 KAIVLNspnnptgAVYS-REELEaLAELAREHDLLVISDEIYEELVYDGAEHV------SILSLPGLK 225
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
42-170 |
3.77e-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: 57.74 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 42 KLKKSLQALYPDAEIVLTNSGTSALVVGLKYLkVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDL--NTNHSISLNKIK 119
Cdd:cd00609 48 WLGRRGGVDVPPEEIVVTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLdeEGGFLLDLELLE 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446372122 120 KHWNANTKAIILTHlygCH---------DDL-DIIDWARENNIYIIDDAAQAMFSYQNGKP 170
Cdd:cd00609 127 AAKTPKTKLLYLNN---PNnptgavlseEELeELAELAKKHGILIISDEAYAELVYDGEPP 184
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
42-196 |
4.36e-08 |
|
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: 52.38 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 42 KLKKSLQALYPDAE--IVLTNSGTSALVVGLKYLkVAKGDEVILSNFNCPNVIEAILTV-GAKPVLIDLNTNHSISLN-- 116
Cdd:cd01494 4 ELEEKLARLLQPGNdkAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGGLDva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 117 -KIKKHWNANTKAIILTH---LYGCHDDLDIIDW-ARENNIYIIDDAAQAMFSYQNGKPVGSLGDIGILSFGGTKPIPSI 191
Cdd:cd01494 83 iLEELKAKPNVALIVITPnttSGGVLVPLKEIRKiAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGE 162
|
....*
gi 446372122 192 GGGAL 196
Cdd:cd01494 163 GGGVV 167
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
42-161 |
8.39e-08 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 53.99 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 42 KLKKSLQALYPDaEIVLTNSGTSA--LVV-GLKYLKvaKGDEVILSNFNCPNVI----EAILTVGAKPVLIDLNTNHSIS 114
Cdd:COG0520 67 KVARFIGAASPD-EIIFTRGTTEAinLVAyGLGRLK--PGDEILITEMEHHSNIvpwqELAERTGAEVRVIPLDEDGELD 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446372122 115 LNKIKKHWNANTKAIILTHL---YGC-HDDLDIIDWARENNIYIIDDAAQA 161
Cdd:COG0520 144 LEALEALLTPRTKLVAVTHVsnvTGTvNPVKEIAALAHAHGALVLVDGAQS 194
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
55-177 |
4.80e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 48.40 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 55 EIVLTNSGTSALVVGLKYLkVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTNH---SISLNKIKKHWNANTKAIIL 131
Cdd:PRK06108 86 RIAVTSSGVQALMLAAQAL-VGPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFGGggwTLDLDRLLAAITPRTRALFI 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446372122 132 ------THLYGCHDDL-DIIDWARENNIYIIDDAAQAMFSYQNGKPVGSLGDI 177
Cdd:PRK06108 165 nspnnpTGWTASRDDLrAILAHCRRHGLWIVADEVYERLYYAPGGRAPSFLDI 217
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
52-196 |
1.12e-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: 47.24 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 52 PDAEIVLTNSGTSAL---VVGLKYlKVAKGDEVILSNFNCPNVIEAIL----TVGAKPVLIDLNTNHSISLNKIKKHWNA 124
Cdd:pfam00266 60 SNDEIIFTSGTTEAInlvALSLGR-SLKPGDEIVITEMEHHANLVPWQelakRTGARVRVLPLDEDGLLDLDELEKLITP 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446372122 125 NTKAIILTH---LYGCHDDL-DIIDWARENNIYIIDDAAQAMFSyqngKPVgSLGDIGI--LSFGGTKPIPSIGGGAL 196
Cdd:pfam00266 139 KTKLVAITHvsnVTGTIQPVpEIGKLAHQYGALVLVDAAQAIGH----RPI-DVQKLGVdfLAFSGHKLYGPTGIGVL 211
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
77-157 |
7.05e-05 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 44.73 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 77 KGDEVILSN--FNC-PNVIEAiltVGAKPVLIDLN--TNHSISLNKIKKHWNANTKAIILT-------HLYGcHDDL-DI 143
Cdd:PRK05764 114 PGDEVIIPApyWVSyPEMVKL---AGGVPVFVPTGeeNGFKLTVEQLEAAITPKTKALILNspsnptgAVYS-PEELeAI 189
|
90
....*....|....
gi 446372122 144 IDWARENNIYIIDD 157
Cdd:PRK05764 190 ADVAVEHDIWVLSD 203
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
52-174 |
3.69e-04 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 42.51 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 52 PDaEIVLTNSGTSALVVGLKYLkVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLnTNHSISLNKIKKHWNA-NTKAII 130
Cdd:COG1167 170 PD-QILITSGAQQALDLALRAL-LRPGDTVAVESPTYPGALAALRAAGLRLVPVPV-DEDGLDLDALEAALRRhRPRAVY 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446372122 131 LT--HLY--GC--HDD--LDIIDWARENNIYIIDDAAQAMFSYQnGKPVGSL 174
Cdd:COG1167 247 VTpsHQNptGAtmSLErrRALLELARRHGVPIIEDDYDSELRYD-GRPPPPL 297
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
55-161 |
4.57e-04 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 42.07 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 55 EIVLTNSGTSAL-VVGLKYLK-VAKGDEVILSnfncpnVIE-----------AILTvGAKPVLIDLNTNHSISLNKIKKH 121
Cdd:cd06453 63 EIIFTRNTTEAInLVAYGLGRaNKPGDEIVTS------VMEhhsnivpwqqlAERT-GAKLKVVPVDDDGQLDLEALEKL 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446372122 122 WNANTKAIILTHL---YGC-HDDLDIIDWARENNIYIIDDAAQA 161
Cdd:cd06453 136 LTERTKLVAVTHVsnvLGTiNPVKEIGEIAHEAGVPVLVDGAQS 179
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
78-178 |
4.84e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 41.98 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 78 GDEVILsnfNCP---NVIEAILTVGAKPVLIDLNTNHSISLNKIKKHWNANTKAIIL------THLYGCHDDLDIID-WA 147
Cdd:PRK05957 113 GDEIIL---NTPyyfNHEMAITMAGCQPILVPTDDNYQLQPEAIEQAITPKTRAIVTispnnpTGVVYPEALLRAVNqIC 189
|
90 100 110
....*....|....*....|....*....|.
gi 446372122 148 RENNIYIIDDAAQAMFSYqNGKPVGSLGDIG 178
Cdd:PRK05957 190 AEHGIYHISDEAYEYFTY-DGVKHFSPGSIP 219
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
57-172 |
1.07e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 40.75 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 57 VLTNSGTSALVVGLKYLKVAKGDEVILSNFNCPNVIEAILTVGAKPVLIDLNT--NHSISLNKIKKHWNANTKAIILThl 134
Cdd:pfam00155 66 VVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDsnDFHLDFDALEAALKEKPKVVLHT-- 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446372122 135 yGCH---------DDL-DIIDWARENNIYIIDDAAQAMFSYQNGKPVG 172
Cdd:pfam00155 144 -SPHnptgtvatlEELeKLLDLAKEHNILLLVDEAYAGFVFGSPDAVA 190
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
52-176 |
2.53e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 39.71 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 52 PDAEIVLTNSGTSALVVGLKYLKVAkGDEVILSNFNCPNVIEAILTVGAKPVLIDLNTNHSI----SLNKIKKHWNANTK 127
Cdd:PRK07309 90 PENEILVTIGATEALSASLTAILEP-GDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVltpeMLEKAILEQGDKLK 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446372122 128 AIILTH-------LYGCHDDLDIIDWARENNIYIIDDAAQAMFSYqNGKPVGSLGD 176
Cdd:PRK07309 169 AVILNYpanptgvTYSREQIKALADVLKKYDIFVISDEVYSELTY-TGEPHVSIAE 223
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
55-177 |
5.95e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 38.68 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372122 55 EIVLTNSGTSALVVGLkyLKVA-KGDEVIL-----SNFNCpnvIEAILTVGAKPVLIDLNTNHSI-SLNKIKKHWNANTK 127
Cdd:PRK07568 90 EILITNGGSEAILFAM--MAICdPGDEILVpepfyANYNG---FATSAGVKIVPVTTKIEEGFHLpSKEEIEKLITPKTK 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446372122 128 AIILTH-------LYGCHDDLDIIDWARENNIYIIDDAAQAMFSYqNGKPVGSLGDI 177
Cdd:PRK07568 165 AILISNpgnptgvVYTKEELEMLAEIAKKHDLFLISDEVYREFVY-DGLKYTSALSL 220
|
|
| |
