|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
9-363 |
4.38e-158 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 447.59 E-value: 4.38e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 9 LANERFFDEYKTKLLETIESGWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKALGLEKNSEIIVPSNTYIAS 88
Cdd:COG0399 4 LSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 89 ILAILHAGLKPVLVEPDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSHGALYKNK 168
Cdd:COG0399 84 ANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 169 KTGTFGEMSGFSFYPTKNLGAlGDAGAVVTDNDLYHDEIRKLRNYGSS--IKYKNDLVGYNSRLDELQATILSIKLKHLD 246
Cdd:COG0399 164 KVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDrdAKYEHVELGYNYRMDELQAAIGLAQLKRLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 247 VMNEHKRSLAKIYLENLK--EDFIKPIVDEEVYDVYHIFNIR---HTKRDDLRDYLLKNGVKTEVHYPIPPHKQIAMKDv 321
Cdd:COG0399 243 EFIARRRAIAARYREALAdlPGLTLPKVPPGAEHVYHLYVIRldeGEDRDELIAALKARGIGTRVHYPIPLHLQPAYRD- 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446497324 322 ILYAEGEFAISEEIHRTTLSLPISTFHTEEDIYKIVEIMNRF 363
Cdd:COG0399 322 LGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
22-359 |
2.19e-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: 394.99 E-value: 2.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 22 LLETIESGWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVL 101
Cdd:cd00616 5 VEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 102 VEPDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGEMSGFSF 181
Cdd:cd00616 85 VDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAGAFSF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 182 YPTKNLGAlGDAGAVVTDNDLYHDEIRKLRNYGSS---IKYKNDLVGYNSRLDELQATILSIKLKHLDVMNEHKRSLAKI 258
Cdd:cd00616 165 HPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDrdrFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 259 YLENLKE--DFIKPIVDEEVYDVYHIFNIRHT-----KRDDLRDYLLKNGVKTEVHYPIPPHKQIAmKDVILYAEGEFAI 331
Cdd:cd00616 244 YKELLADlpGIRLPDVPPGVKHSYHLYVIRLDpeageSRDELIEALKEAGIETRVHYPPLHHQPPY-KKLLGYPPGDLPN 322
|
330 340
....*....|....*....|....*...
gi 446497324 332 SEEIHRTTLSLPISTFHTEEDIYKIVEI 359
Cdd:cd00616 323 AEDLAERVLSLPLHPSLTEEEIDRVIEA 350
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
22-360 |
4.44e-124 |
|
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: 361.22 E-value: 4.44e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 22 LLETIESGWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVL 101
Cdd:pfam01041 11 VREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAKPVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 102 VEPDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGEMSGFSF 181
Cdd:pfam01041 91 VDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAATFSF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 182 YPTKNLgALGDAGAVVTDNDLYHDEIRKLRNYGSS----IKYKNDLVGYNSRLDELQATILSIKLKHLDVMNEHKRSLAK 257
Cdd:pfam01041 171 HPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGMVrkadKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIARRREIAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 258 IY---LENLKEDFIKPIVDEEVYDVYHIFNIR----HTKRDDLRDYLLKNGVKTEVHYPIPPHKQIAMKDVILYAEGEFA 330
Cdd:pfam01041 250 LYqtlLADLPGFTPLTTPPEADVHAWHLFPILvpeeAINRDELVEALKEAGIGTRVHYPIPLHLQPYYRDLFGYAPGDLP 329
|
330 340 350
....*....|....*....|....*....|
gi 446497324 331 ISEEIHRTTLSLPISTFHTEEDIYKIVEIM 360
Cdd:pfam01041 330 NAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
61-363 |
2.48e-45 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 159.23 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 61 DALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVLVepDIR--TYNIDPQKIEEKINFKTKGILIVHLYGKPCE 138
Cdd:PRK11706 57 AALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFV--DIRpdTMNIDETLIEAAITPKTRAIVPVHYAGVACE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 139 MDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGEMSGFSFYPTKNLGAlGDAGA-VVTDNDLYHD-EI--------- 207
Cdd:PRK11706 135 MDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGAlLINDPALIERaEIirekgtnrs 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 208 RKLRnyGSSIKYKNDLVGYNSRLDELQATILSIKLKHLDVMNEHKRSLAKIYLENLKE-----DFIKPIVDEEVYDVYHI 282
Cdd:PRK11706 214 QFFR--GQVDKYTWVDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPlaeagRIELPSIPDDCKHNAHM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 283 FNIR---HTKRDDLRDYLLKNGVKTEVHYpIPPHKQIAMKDVIlYAEGEFAISEEIHRTTLSLPISTFHTEEDIYKIVEI 359
Cdd:PRK11706 292 FYIKlrdLEDRSALINFLKEAGIMAVFHY-IPLHSSPAGERFG-RFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDT 369
|
....
gi 446497324 360 MNRF 363
Cdd:PRK11706 370 ILEF 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
9-363 |
4.38e-158 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 447.59 E-value: 4.38e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 9 LANERFFDEYKTKLLETIESGWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKALGLEKNSEIIVPSNTYIAS 88
Cdd:COG0399 4 LSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 89 ILAILHAGLKPVLVEPDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSHGALYKNK 168
Cdd:COG0399 84 ANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 169 KTGTFGEMSGFSFYPTKNLGAlGDAGAVVTDNDLYHDEIRKLRNYGSS--IKYKNDLVGYNSRLDELQATILSIKLKHLD 246
Cdd:COG0399 164 KVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDrdAKYEHVELGYNYRMDELQAAIGLAQLKRLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 247 VMNEHKRSLAKIYLENLK--EDFIKPIVDEEVYDVYHIFNIR---HTKRDDLRDYLLKNGVKTEVHYPIPPHKQIAMKDv 321
Cdd:COG0399 243 EFIARRRAIAARYREALAdlPGLTLPKVPPGAEHVYHLYVIRldeGEDRDELIAALKARGIGTRVHYPIPLHLQPAYRD- 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446497324 322 ILYAEGEFAISEEIHRTTLSLPISTFHTEEDIYKIVEIMNRF 363
Cdd:COG0399 322 LGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
22-359 |
2.19e-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: 394.99 E-value: 2.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 22 LLETIESGWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVL 101
Cdd:cd00616 5 VEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 102 VEPDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGEMSGFSF 181
Cdd:cd00616 85 VDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAGAFSF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 182 YPTKNLGAlGDAGAVVTDNDLYHDEIRKLRNYGSS---IKYKNDLVGYNSRLDELQATILSIKLKHLDVMNEHKRSLAKI 258
Cdd:cd00616 165 HPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDrdrFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 259 YLENLKE--DFIKPIVDEEVYDVYHIFNIRHT-----KRDDLRDYLLKNGVKTEVHYPIPPHKQIAmKDVILYAEGEFAI 331
Cdd:cd00616 244 YKELLADlpGIRLPDVPPGVKHSYHLYVIRLDpeageSRDELIEALKEAGIETRVHYPPLHHQPPY-KKLLGYPPGDLPN 322
|
330 340
....*....|....*....|....*...
gi 446497324 332 SEEIHRTTLSLPISTFHTEEDIYKIVEI 359
Cdd:cd00616 323 AEDLAERVLSLPLHPSLTEEEIDRVIEA 350
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
22-360 |
4.44e-124 |
|
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: 361.22 E-value: 4.44e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 22 LLETIESGWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVL 101
Cdd:pfam01041 11 VREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAKPVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 102 VEPDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGEMSGFSF 181
Cdd:pfam01041 91 VDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAATFSF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 182 YPTKNLgALGDAGAVVTDNDLYHDEIRKLRNYGSS----IKYKNDLVGYNSRLDELQATILSIKLKHLDVMNEHKRSLAK 257
Cdd:pfam01041 171 HPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGMVrkadKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIARRREIAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 258 IY---LENLKEDFIKPIVDEEVYDVYHIFNIR----HTKRDDLRDYLLKNGVKTEVHYPIPPHKQIAMKDVILYAEGEFA 330
Cdd:pfam01041 250 LYqtlLADLPGFTPLTTPPEADVHAWHLFPILvpeeAINRDELVEALKEAGIGTRVHYPIPLHLQPYYRDLFGYAPGDLP 329
|
330 340 350
....*....|....*....|....*....|
gi 446497324 331 ISEEIHRTTLSLPISTFHTEEDIYKIVEIM 360
Cdd:pfam01041 330 NAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
61-363 |
2.48e-45 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 159.23 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 61 DALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVLVepDIR--TYNIDPQKIEEKINFKTKGILIVHLYGKPCE 138
Cdd:PRK11706 57 AALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFV--DIRpdTMNIDETLIEAAITPKTRAIVPVHYAGVACE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 139 MDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGEMSGFSFYPTKNLGAlGDAGA-VVTDNDLYHD-EI--------- 207
Cdd:PRK11706 135 MDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGAlLINDPALIERaEIirekgtnrs 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 208 RKLRnyGSSIKYKNDLVGYNSRLDELQATILSIKLKHLDVMNEHKRSLAKIYLENLKE-----DFIKPIVDEEVYDVYHI 282
Cdd:PRK11706 214 QFFR--GQVDKYTWVDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPlaeagRIELPSIPDDCKHNAHM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 283 FNIR---HTKRDDLRDYLLKNGVKTEVHYpIPPHKQIAMKDVIlYAEGEFAISEEIHRTTLSLPISTFHTEEDIYKIVEI 359
Cdd:PRK11706 292 FYIKlrdLEDRSALINFLKEAGIMAVFHY-IPLHSSPAGERFG-RFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDT 369
|
....
gi 446497324 360 MNRF 363
Cdd:PRK11706 370 ILEF 373
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
13-363 |
3.79e-42 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 152.35 E-value: 3.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 13 RFFDEYKTKLLetIES---GWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKAL--------GLEKNSEIIVP 81
Cdd:PRK15407 40 KVIDAKELQNL--VDAsldFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALtspklgdrALKPGDEVITV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 82 SNTYIASILAILHAGLKPVLVEPDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSH 161
Cdd:PRK15407 118 AAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDAL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 162 GALYKNKKTGTFGEMSGFSFYPTKNLgALGDAGAVVTDNDLYHDEIRKLRNYGSSI------------------------ 217
Cdd:PRK15407 198 GSTYDGRMTGTFGDIATLSFYPAHHI-TMGEGGAVFTNDPLLKKIIESFRDWGRDCwcapgcdntcgkrfgwqlgelpfg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 218 ---KYKNDLVGYNSRLDELQATILSIKLKHLDVMNE-HKRSLAKIY--LENLKEDFIKP---------------IVDEEv 276
Cdd:PRK15407 277 ydhKYTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEaRKANFAYLKegLASLEDFLILPeatpnsdpswfgfpiTVKED- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 277 ydvyHIFNirhtkRDDLRDYLLKNGVKTEVHYPIPPHKQIAMKDVILYAEGEFAISEEIHRTTLSLPISTFHTEEDIYKI 356
Cdd:PRK15407 356 ----AGFT-----RVELVKYLEENKIGTRLLFAGNLTRQPYFKGVKYRVVGELTNTDRIMNDTFWIGVYPGLTEEMLDYV 426
|
....*..
gi 446497324 357 VEIMNRF 363
Cdd:PRK15407 427 IEKIEEF 433
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
24-315 |
3.13e-40 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 145.94 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 24 ETIESGWYILGKEVSNFESQFAEYNGNRYCIGVGNGLDALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVLVE 103
Cdd:PRK11658 22 EVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLNMIVLLGATPVMVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 104 PDIRTYNIDPQKIEEKINFKTKGILIVHLYGKPCEMDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGeMSGFSFYP 183
Cdd:PRK11658 102 VDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHIGARG-TAIFSFHA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 184 TKNLgALGDAGAVVTDNDLYHDEIRKLRNYGSSI----------KYKNDLV--GYNSRLDELQATILSIKLKHLDVMNEH 251
Cdd:PRK11658 181 IKNI-TCAEGGLVVTDDDELADRLRSLKFHGLGVdafdrqtqgrAPQAEVLtpGYKYNLADINAAIALVQLAKLEALNAR 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446497324 252 KRSLAKIYLENLKEDFIKPIV--DEEVYDVYHIFNIRHTK------RDDLRDYLLKNGVKTEVHYpIPPHKQ 315
Cdd:PRK11658 260 RREIAARYLQALADLPFQPLSlpAWPHQHAWHLFIIRVDEercgisRDALMEALKERGIGTGLHF-RAAHTQ 330
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
53-156 |
1.49e-06 |
|
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: 49.65 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 53 CIGVGNGLDALILALkalgLEKNSEIIVPSNTYIASILAILHAGLKPVLVEPDI-RTYNIDPQKIEEKINFKTKGILIV- 130
Cdd:cd00609 65 TNGAQEALSLLLRAL----LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEeGGFLLDLELLEAAKTPKTKLLYLNn 140
|
90 100 110
....*....|....*....|....*....|..
gi 446497324 131 ------HLYGKPcEMDSILKIKEKNNLFLVED 156
Cdd:cd00609 141 pnnptgAVLSEE-ELEELAELAKKHGILIISD 171
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
40-163 |
2.30e-06 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 48.84 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 40 FESQFAEYNGNRYCIG--------VGNGLDALILALKALGLEKNSEIIVPSNTYIASILAILHAGLKPVLVE-PDIRTYN 110
Cdd:pfam00155 44 LREALAKFLGRSPVLKldreaavvFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlYDSNDFH 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446497324 111 IDPQKIEEKINFKTKGILI--VHlygKPC-------EMDSILKIKEKNNLFLVEDCAQSHGA 163
Cdd:pfam00155 124 LDFDALEAALKEKPKVVLHtsPH---NPTgtvatleELEKLLDLAKEHNILLLVDEAYAGFV 182
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
59-156 |
6.06e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 47.54 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 59 GLDALILALKALgLEKNSEIIVPSNTYI--ASILAILHAGLKPVL--VEPDIRTYNIDpqKIEEKINFKTKGILIVH--- 131
Cdd:PRK07568 97 GSEAILFAMMAI-CDPGDEILVPEPFYAnyNGFATSAGVKIVPVTtkIEEGFHLPSKE--EIEKLITPKTKAILISNpgn 173
|
90 100
....*....|....*....|....*....
gi 446497324 132 ----LYGKPcEMDSILKIKEKNNLFLVED 156
Cdd:PRK07568 174 ptgvVYTKE-ELEMLAEIAKKHDLFLISD 201
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
62-129 |
3.01e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 45.57 E-value: 3.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446497324 62 ALILALKALgLEKNSEIIVPSNTYIASILAILHAGLKPVLVEPDIRTYNIDPQKIEEKINFKTKGILI 129
Cdd:PRK06836 108 ALNVALKAI-LNPGDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVII 174
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
41-163 |
5.89e-05 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 44.16 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 41 ESQ--FAEYNGNRYCI----GVGNGLDALILALkalgLEKNSEIIVPSNTYIASILAILHAGLKPVLVEPDIRTYN---- 110
Cdd:cd00615 63 EAQelAARAFGAKHTFflvnGTSSSNKAVILAV----CGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiag 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446497324 111 -IDPQKIEEKI--NFKTKGILIVH--LYGKPCEMDSILKIKEKNNLFLVEDCAqsHGA 163
Cdd:cd00615 139 gIPPETFKKALieHPDAKAAVITNptYYGICYNLRKIVEEAHHRGLPVLVDEA--HGA 194
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
37-265 |
6.69e-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: 44.50 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 37 VSNFESQFAEYNGNRYCIGVGNGLDALILALKALgLEKNSEIIVPSNTY------IASILAILhaGLKPVLVEPDirtyn 110
Cdd:cd00614 42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYggtyrlFERLLPKL--GIEVTFVDPD----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 111 iDPQKIEEKINFKTKGILI---VHLYGKPCEMDSILKIKEKNNLFLVEDcaqshgalyknkktGTFgeMSGFSFYP---- 183
Cdd:cd00614 114 -DPEALEAAIKPETKLVYVespTNPTLKVVDIEAIAELAHEHGALLVVD--------------NTF--ATPYLQRPlelg 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 184 --------TKNLGALGD--AGAVVTDNDLYHDEIRKLRNYgssikykndlVGYNsrLDELQATILSIKLKHLDV-MNEHK 252
Cdd:cd00614 177 adivvhsaTKYIGGHSDviAGVVVGSGEALIQRLRFLRLA----------LGTI--LSPFDAWLLLRGLKTLPLrMERHS 244
|
250
....*....|....*
gi 446497324 253 RSLAKI--YLENLKE 265
Cdd:cd00614 245 ENALKVaeFLEKHPK 259
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
33-156 |
3.34e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 42.40 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 33 LGKEVSNFESQFAEYN-GNRYCIGVGNGLDALILALKALgLEKNSEIIVPSNTYIASILAILHAGLKPVLVEpdirTY-- 109
Cdd:PRK06348 71 LIEEIIKYYSKNYDLSfKRNEIMATVGACHGMYLALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILE----TYee 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446497324 110 ---NIDPQKIEEKINFKTKGILI------VHLYGKPCEMDSILKIKEKNNLFLVED 156
Cdd:PRK06348 146 dgfQINVKKLEALITSKTKAIILnspnnpTGAVFSKETLEEIAKIAIEYDLFIISD 201
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
62-130 |
6.23e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 41.60 E-value: 6.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446497324 62 ALILALKALGleknSEIIVPSNTYIASILAILHAGLKPVLVEPDiRTYNIDPQKIEEKINFKTKGILIV 130
Cdd:PRK05957 104 NAILAITDPG----DEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIVTI 167
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
48-199 |
3.09e-03 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 38.13 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 48 NGNRYCIGVGNGLDALILALKALgLEKNSEIIVPSNTYIASILAILH-AGLKPVLVEPDIRTYN-IDPQKIEEKINFKTK 125
Cdd:cd01494 15 PGNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAElAGAKPVPVPVDDAGYGgLDVAILEELKAKPNV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446497324 126 GILIVHLYGKPC----EMDSILKIKEKNNLFLVEDCAQSHGALYKNKKTGTFGEMSGFSFYPTKNLGALGdAGAVVTD 199
Cdd:cd01494 94 ALIVITPNTTSGgvlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEG-GGVVIVK 170
|
|
| PRK13355 |
PRK13355 |
bifunctional HTH-domain containing protein/aminotransferase; Provisional |
54-156 |
5.01e-03 |
|
bifunctional HTH-domain containing protein/aminotransferase; Provisional
Pssm-ID: 237361 [Multi-domain] Cd Length: 517 Bit Score: 38.56 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497324 54 IGVGNGLDALI-LALKALgLEKNSEIIVPSNTYIASILAILHAGLKPVLV--------EPDIrtynidpQKIEEKINFKT 124
Cdd:PRK13355 211 IYTGNGVSELInLSMSAL-LDDGDEVLIPSPDYPLWTACVNLAGGTAVHYrcdeqsewYPDI-------DDIRSKITSRT 282
|
90 100 110
....*....|....*....|....*....|....*....
gi 446497324 125 KGILIVH-------LYGKPCeMDSILKIKEKNNLFLVED 156
Cdd:PRK13355 283 KAIVIINpnnptgaLYPREV-LQQIVDIAREHQLIIFSD 320
|
|
| |
