|
Name |
Accession |
Description |
Interval |
E-value |
| PLP_DesI |
TIGR04427 |
dTDP-4-dehydro-6-deoxyglucose aminotransferase; Members of this family are pyridoxal ... |
1-388 |
0e+00 |
|
dTDP-4-dehydro-6-deoxyglucose aminotransferase; Members of this family are pyridoxal phosphate-dependent aminotransferases that convert TDP-4-keto-6-deoxy-D-glucose to the 4-amino sugar form, TDP-4-amino-4,6-dideoxy-D-glucose. In Streptomyces venezuelae, this enzyme is designated DesI, catalyzing the third of six steps in the biosynthesis of TDP-D-desosamine, a component of a number of different macrolide antibiotics made by that organism. Related proteins, scoring below the trusted cutoff, include sugar aminotranferases in O-antigen biosynthesis regions.
Pssm-ID: 275220 Cd Length: 390 Bit Score: 734.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 1 MKRGVHDLALFGGDAAFLQPLYMGRPNTGDRKRLLDRLEWALDNRWLTNGGPLVREFEQRIADLAGVRNCVATCNATAGL 80
Cdd:TIGR04427 1 MKRALDDLAIFGGPAAFLQPLLVGRPNVGDRARFFERLEWALDNEWLTNGGPLVREFETRIADLAGVRHCVATCNATAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 81 QLLLREAEVTGEVIMPSMTFVATAHAVRWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAI 160
Cdd:TIGR04427 81 QLLLRAAGVTGEVIMPSMTFAATAHAASWLGLEPVFCDVDPDTGCLDPDRVAAAITPRTGAIVGVHLWGRPCPVDELAKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 161 AAEHGLKLFYDAAHALGCTSRQRRLGSFGDAEVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLG--HDGVGAGI 238
Cdd:TIGR04427 161 AAEHGLRLFFDAAHALGCTADGRPVGSFGDAEVFSFHATKVVNSFEGGAVVTDDAELAARLRALHNFGFGldGGVPAGGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 239 NAKMSEAAAAMGLTSLEAFADAVASNRANYELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDAGVTGLHRDLLLTLLR 318
Cdd:TIGR04427 241 NAKMSEASAAMGLTSLDAFAEVVEHNRRNHALYREELRDLPGVRVLDFDPHERNNYQYVIVEIDEAVTGIHRDLLITVLR 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 319 AENVVAQPYFSPGCHQREPYRTEHPVSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIRVAAAHGPRIT 388
Cdd:TIGR04427 321 AEGVVAQPYFSPGCHQMEPYRTEPPVRLPHTERLAAQVLALPTGPAVSSEDIRRVCDIIRLAATRGEEIT 390
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
20-378 |
1.41e-133 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 386.73 E-value: 1.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 20 PLYMGRPNTGDRkrLLDRLEWALDNRWLTNGgPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEVT--GEVIMPS 97
Cdd:COG0399 1 MIPLSRPSIGEE--EIAAVVEVLRSGWLTLG-PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGpgDEVITPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 98 MTFVATAHAVRWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALG 177
Cdd:COG0399 78 FTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 178 CTSRQRRLGSFGDAEVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDG----VGAGINAKMSEAAAAMGLTS 253
Cdd:COG0399 158 ATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAkyehVELGYNYRMDELQAAIGLAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 254 LEAFADAVASNRANYELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDAGVTglhRDLLLTLLRAENVVAQPYFSPGCH 333
Cdd:COG0399 238 LKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGED---RDELIAALKARGIGTRVHYPIPLH 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 5902172 334 QREPYRTEH--PVSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:COG0399 315 LQPAYRDLGyrPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIR 361
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
35-378 |
6.98e-128 |
|
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: 371.87 E-value: 6.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 35 LDRLEWALDNRWLTnGGPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEV--TGEVIMPSMTFVATAHAVRWLGL 112
Cdd:cd00616 2 LEAVEEVLDSGWLT-LGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIgpGDEVIVPSFTFVATANAILLLGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 113 RPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGSFGDAE 192
Cdd:cd00616 81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 193 VFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDGVGA-----GINAKMSEAAAAMGLTSLEAFADAVASNRAN 267
Cdd:cd00616 161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYeheilGYNYRLSEIQAAIGLAQLEKLDEIIARRREI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 268 YELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDaGVTGLHRDLLLTLLRAENVVAQPYFSPGCHQREPYRTEH--PVS 345
Cdd:cd00616 241 AERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLD-PEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLGypPGD 319
|
330 340 350
....*....|....*....|....*....|...
gi 5902172 346 LPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:cd00616 320 LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
30-378 |
8.47e-128 |
|
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: 372.00 E-value: 8.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 30 DRKRLLDRLEWALDNRWLTNGgPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEVT--GEVIMPSMTFVATAHAV 107
Cdd:pfam01041 3 IDEEELAAVREVLKSGWLTTG-PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGpgDEVITPSFTFVATANAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 108 RWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGS 187
Cdd:pfam01041 82 LRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 188 FGDAEVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDGVG------AGINAKMSEAAAAMGLTSLEAFADAV 261
Cdd:pfam01041 162 LGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKrywhevLGYNYRMTEIQAAIGLAQLERLDEFI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 262 ASNRANYELYRQELSGLPGVRLIDYDP-AERNNYHYVIALIDAGvtGLHRDLLLTLLRAENVVAQPYFSPGCHQREPYRT 340
Cdd:pfam01041 242 ARRREIAALYQTLLADLPGFTPLTTPPeADVHAWHLFPILVPEE--AINRDELVEALKEAGIGTRVHYPIPLHLQPYYRD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 5902172 341 EHPV---SLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:pfam01041 320 LFGYapgDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
25-378 |
2.26e-67 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 217.97 E-value: 2.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 25 RPNTGDRKrlLDRLEWALDNRWLTNGgPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEVT--GEVIMPSMTFVA 102
Cdd:PRK11658 9 RPAMGDEE--LAAVKEVLRSGWITTG-PKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGpgDEVITPSLTWVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 103 TAHAVRWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQ 182
Cdd:PRK11658 86 TLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 183 RRLGSFGDAeVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDG--------------VGAGINAKMSEAAAA 248
Cdd:PRK11658 166 RHIGARGTA-IFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAfdrqtqgrapqaevLTPGYKYNLADINAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 249 MGLTSLEAFADAVASNRANYELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDAGVTGLHRDLLLTLLRAENVVAQPYF 328
Cdd:PRK11658 245 IALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGTGLHF 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 5902172 329 SpGCHQREPYRTEHP-VSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:PRK11658 325 R-AAHTQKYYRERFPtLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQ 374
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLP_DesI |
TIGR04427 |
dTDP-4-dehydro-6-deoxyglucose aminotransferase; Members of this family are pyridoxal ... |
1-388 |
0e+00 |
|
dTDP-4-dehydro-6-deoxyglucose aminotransferase; Members of this family are pyridoxal phosphate-dependent aminotransferases that convert TDP-4-keto-6-deoxy-D-glucose to the 4-amino sugar form, TDP-4-amino-4,6-dideoxy-D-glucose. In Streptomyces venezuelae, this enzyme is designated DesI, catalyzing the third of six steps in the biosynthesis of TDP-D-desosamine, a component of a number of different macrolide antibiotics made by that organism. Related proteins, scoring below the trusted cutoff, include sugar aminotranferases in O-antigen biosynthesis regions.
Pssm-ID: 275220 Cd Length: 390 Bit Score: 734.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 1 MKRGVHDLALFGGDAAFLQPLYMGRPNTGDRKRLLDRLEWALDNRWLTNGGPLVREFEQRIADLAGVRNCVATCNATAGL 80
Cdd:TIGR04427 1 MKRALDDLAIFGGPAAFLQPLLVGRPNVGDRARFFERLEWALDNEWLTNGGPLVREFETRIADLAGVRHCVATCNATAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 81 QLLLREAEVTGEVIMPSMTFVATAHAVRWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAI 160
Cdd:TIGR04427 81 QLLLRAAGVTGEVIMPSMTFAATAHAASWLGLEPVFCDVDPDTGCLDPDRVAAAITPRTGAIVGVHLWGRPCPVDELAKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 161 AAEHGLKLFYDAAHALGCTSRQRRLGSFGDAEVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLG--HDGVGAGI 238
Cdd:TIGR04427 161 AAEHGLRLFFDAAHALGCTADGRPVGSFGDAEVFSFHATKVVNSFEGGAVVTDDAELAARLRALHNFGFGldGGVPAGGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 239 NAKMSEAAAAMGLTSLEAFADAVASNRANYELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDAGVTGLHRDLLLTLLR 318
Cdd:TIGR04427 241 NAKMSEASAAMGLTSLDAFAEVVEHNRRNHALYREELRDLPGVRVLDFDPHERNNYQYVIVEIDEAVTGIHRDLLITVLR 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 319 AENVVAQPYFSPGCHQREPYRTEHPVSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIRVAAAHGPRIT 388
Cdd:TIGR04427 321 AEGVVAQPYFSPGCHQMEPYRTEPPVRLPHTERLAAQVLALPTGPAVSSEDIRRVCDIIRLAATRGEEIT 390
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
20-378 |
1.41e-133 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 386.73 E-value: 1.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 20 PLYMGRPNTGDRkrLLDRLEWALDNRWLTNGgPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEVT--GEVIMPS 97
Cdd:COG0399 1 MIPLSRPSIGEE--EIAAVVEVLRSGWLTLG-PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGpgDEVITPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 98 MTFVATAHAVRWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALG 177
Cdd:COG0399 78 FTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 178 CTSRQRRLGSFGDAEVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDG----VGAGINAKMSEAAAAMGLTS 253
Cdd:COG0399 158 ATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAkyehVELGYNYRMDELQAAIGLAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 254 LEAFADAVASNRANYELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDAGVTglhRDLLLTLLRAENVVAQPYFSPGCH 333
Cdd:COG0399 238 LKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGED---RDELIAALKARGIGTRVHYPIPLH 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 5902172 334 QREPYRTEH--PVSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:COG0399 315 LQPAYRDLGyrPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIR 361
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
35-378 |
6.98e-128 |
|
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: 371.87 E-value: 6.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 35 LDRLEWALDNRWLTnGGPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEV--TGEVIMPSMTFVATAHAVRWLGL 112
Cdd:cd00616 2 LEAVEEVLDSGWLT-LGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIgpGDEVIVPSFTFVATANAILLLGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 113 RPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGSFGDAE 192
Cdd:cd00616 81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 193 VFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDGVGA-----GINAKMSEAAAAMGLTSLEAFADAVASNRAN 267
Cdd:cd00616 161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYeheilGYNYRLSEIQAAIGLAQLEKLDEIIARRREI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 268 YELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDaGVTGLHRDLLLTLLRAENVVAQPYFSPGCHQREPYRTEH--PVS 345
Cdd:cd00616 241 AERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLD-PEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLGypPGD 319
|
330 340 350
....*....|....*....|....*....|...
gi 5902172 346 LPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:cd00616 320 LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
30-378 |
8.47e-128 |
|
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: 372.00 E-value: 8.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 30 DRKRLLDRLEWALDNRWLTNGgPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEVT--GEVIMPSMTFVATAHAV 107
Cdd:pfam01041 3 IDEEELAAVREVLKSGWLTTG-PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGpgDEVITPSFTFVATANAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 108 RWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGS 187
Cdd:pfam01041 82 LRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 188 FGDAEVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDGVG------AGINAKMSEAAAAMGLTSLEAFADAV 261
Cdd:pfam01041 162 LGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKrywhevLGYNYRMTEIQAAIGLAQLERLDEFI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 262 ASNRANYELYRQELSGLPGVRLIDYDP-AERNNYHYVIALIDAGvtGLHRDLLLTLLRAENVVAQPYFSPGCHQREPYRT 340
Cdd:pfam01041 242 ARRREIAALYQTLLADLPGFTPLTTPPeADVHAWHLFPILVPEE--AINRDELVEALKEAGIGTRVHYPIPLHLQPYYRD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 5902172 341 EHPV---SLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:pfam01041 320 LFGYapgDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
25-378 |
2.26e-67 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 217.97 E-value: 2.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 25 RPNTGDRKrlLDRLEWALDNRWLTNGgPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEVT--GEVIMPSMTFVA 102
Cdd:PRK11658 9 RPAMGDEE--LAAVKEVLRSGWITTG-PKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGpgDEVITPSLTWVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 103 TAHAVRWLGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQ 182
Cdd:PRK11658 86 TLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 183 RRLGSFGDAeVFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDG--------------VGAGINAKMSEAAAA 248
Cdd:PRK11658 166 RHIGARGTA-IFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAfdrqtqgrapqaevLTPGYKYNLADINAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 249 MGLTSLEAFADAVASNRANYELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDAGVTGLHRDLLLTLLRAENVVAQPYF 328
Cdd:PRK11658 245 IALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGTGLHF 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 5902172 329 SpGCHQREPYRTEHP-VSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:PRK11658 325 R-AAHTQKYYRERFPtLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQ 374
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
41-378 |
1.61e-66 |
|
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: 215.65 E-value: 1.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 41 ALDNRWLTnGGPLVREFEQRIADLAGVRNCVATCNATAGLQLLLREAEV-TG-EVIMPSMTFVATAHAVRWLGLRPVFCD 118
Cdd:TIGR03588 19 VLKSDFLT-QGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVgPGdRVWTTPITFVATANCALYCGAKVDFVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 119 IDPDTGCLDPKLVEAAVT----PRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGS--FGDAE 192
Cdd:TIGR03588 98 IDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNcrYADAT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 193 VFSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFGLGHDG---------------VGAGINAKMSEAAAAMGLTSLEAF 257
Cdd:TIGR03588 178 VFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPllfekqdegpwyyeqQELGFNYRMTDIQAALGLSQLKKL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 258 ADAVASNRANYELYRQELSGLPGVRLIDYDPAERNNYHYVIALIDAgVTGLHRDLLLTLLRAENVVAQPYFSPgCHQREP 337
Cdd:TIGR03588 258 DRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQ-EFGCTRKEVFEALRAAGIGVQVHYIP-VHLQPY 335
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 5902172 338 YRTE-HPVSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:TIGR03588 336 YRQGfGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLR 377
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
35-377 |
2.71e-44 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 157.30 E-value: 2.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 35 LDRLEWALDNRWLTNGGPLVREFEQRIADLAGVRNCVATCNATAGLQL--LLREAEVTGEVIMPSMTFVATAHAVRWLGL 112
Cdd:PRK11706 14 LDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMaaLLLDIQPGDEVIMPSYTFVSTANAFVLRGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 113 RPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGSFGDAE 192
Cdd:PRK11706 94 KIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 193 VFSFHATKVVNSFEGGGIVTDDDT---RAERLRalhnfglgHDG----------------VGAGINAKMSEAAAAMGLTS 253
Cdd:PRK11706 174 CFSFHETKNYTAGEGGALLINDPAlieRAEIIR--------EKGtnrsqffrgqvdkytwVDIGSSYLPSELQAAYLWAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 254 LEAFADAVASNRANYELYRQELSGLPGVRLID--YDPAE-RNNYH-YVIALIDAGvtglHRDLLLTLLRAENVVAqpYF- 328
Cdd:PRK11706 246 LEAADRINQRRLALWQRYYDALAPLAEAGRIElpSIPDDcKHNAHmFYIKLRDLE----DRSALINFLKEAGIMA--VFh 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 5902172 329 ------SP-GchqrEPYRTEHPvSLPHTEHLAEQVIALPTGPAVSREDIRRVCDII 377
Cdd:PRK11706 320 yiplhsSPaG----ERFGRFHG-EDRYTTKESERLLRLPLFYNLTDVEQRTVIDTI 370
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
41-378 |
1.42e-27 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 113.05 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 41 ALDNrWLTNGgPLVREFEQRIADLAGVRNCVaTCNA--TAGL---------QLLLREAEVTGEVIMPSMTFVATAHAVRW 109
Cdd:PRK15407 54 SLDF-WLTTG-RFNDAFEKKLAEFLGVRYAL-LVNSgsSANLlafsaltspKLGDRALKPGDEVITVAAGFPTTVNPIIQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 110 LGLRPVFCDIDPDTGCLDPKLVEAAVTPRTGAILGVHLWGRPSRVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGSFG 189
Cdd:PRK15407 131 NGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 190 DAEVFSF----HATkvvnSFEGGGIVTDDD---TRAERLR---------------ALHNFG--LG-------HDGVGA-- 236
Cdd:PRK15407 211 DIATLSFypahHIT----MGEGGAVFTNDPllkKIIESFRdwgrdcwcapgcdntCGKRFGwqLGelpfgydHKYTYShl 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 237 GINAKMSEAAAAMGLTSLEAFADAVASNRANYELYRQELSGLPGVrLIDYDPAERNN---YHYVIALI-DAGVTGL---- 308
Cdd:PRK15407 287 GYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLEDF-LILPEATPNSDpswFGFPITVKeDAGFTRVelvk 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5902172 309 HRDLLLTLLR---AENVVAQPYFSpgchqREPYRTEHpvSLPHTEHLAEQVIALPTGPAVSREDIRRVCDIIR 378
Cdd:PRK15407 366 YLEENKIGTRllfAGNLTRQPYFK-----GVKYRVVG--ELTNTDRIMNDTFWIGVYPGLTEEMLDYVIEKIE 431
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
20-284 |
1.67e-11 |
|
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: 65.06 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 20 PLYMGRPNTGDRKRLLDRLEWALDNRWLTNGGPLV--REFEQRIADLAGVRNCVA--------TCNATAGLQLLLRE-AE 88
Cdd:cd00609 2 DLSIGEPDFPPPPEVLEALAAAALRAGLLGYYPDPglPELREAIAEWLGRRGGVDvppeeivvTNGAQEALSLLLRAlLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 89 VTGEVIMPSMTFVATAHAVRWLGLRPVFCDIDPDTGCL-DPKLVEAAVTPRTGAIL--------GVhLWGRpSRVDELAA 159
Cdd:cd00609 82 PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLlDLELLEAAKTPKTKLLYlnnpnnptGA-VLSE-EELEELAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 160 IAAEHGLKLFYDAAHA-LGCTSRQRRLGSFGDAEVFSFhatkVVNSFE---------GGGIVTDDDTRAERLRALHNFGL 229
Cdd:cd00609 160 LAKKHGILIISDEAYAeLVYDGEPPPALALLDAYERVI----VLRSFSktfglpglrIGYLIAPPEELLERLKKLLPYTT 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 5902172 230 GHdgvgagiNAKMSEAAAAMGLTSLEAFADAVASN-RANYELYRQELSGLPGVRLI 284
Cdd:cd00609 236 SG-------PSTLSQAAAAAALDDGEEHLEELRERyRRRRDALLEALKELGPLVVV 284
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
56-213 |
4.53e-07 |
|
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: 49.30 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 56 EFEQRIADLAGVRNCVA------TCnATAGLQLLLREAEvtGEVIMPSMTFVA-TAHAVRWLGLRPVFCDIDPDT-GCLD 127
Cdd:cd01494 4 ELEEKLARLLQPGNDKAvfvpsgTG-ANEAALLALLGPG--DEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGyGGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 128 PKLVEAAVTPRTGAILGVHLWGRPS----RVDELAAIAAEHGLKLFYDAAHALGCTSRQRRLGSFGDAEVFSFHATKVVN 203
Cdd:cd01494 81 VAILEELKAKPNVALIVITPNTTSGgvlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLG 160
|
170
....*....|
gi 5902172 204 SFEGGGIVTD 213
Cdd:cd01494 161 GEGGGVVIVK 170
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
92-171 |
4.69e-07 |
|
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: 51.28 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 92 EVIMPSMTFVATAHAVRWLGLRPVFCDIDPDTG-CLDPKLVEAAVTPRTGAIL--------GVhLWGRpSRVDELAAIAA 162
Cdd:COG0436 116 EVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENGfLPDPEALEAAITPRTKAIVlnspnnptGA-VYSR-EELEALAELAR 193
|
....*....
gi 5902172 163 EHGLKLFYD 171
Cdd:COG0436 194 EHDLLVISD 202
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
50-293 |
5.22e-07 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 50.68 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 50 GGPLVREFEQRIADLAGVRNCVATCNATAGLQLLLRE-AEVTGEVIM--PSMTFVATAHAVRWL-GLRPVFCDIDPDtGC 125
Cdd:pfam01212 30 GDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAhCQRGDEVICgePAHIHFDETGGHAELgGVQPRPLDGDEA-GN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 126 LDPKLVEAAVTPRTGAIL---GV--------HLWGRPSRVDELAAIAA---EHGLKLFYD------AAHALGCTSRQrrL 185
Cdd:pfam01212 109 MDLEDLEAAIREVGADIFpptGLislenthnSAGGQVVSLENLREIAAlarEHGIPVHLDgarfanAAVALGVIVKE--I 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 186 GSFGDaeVFSFHATKVVNSFEGGGIVTDDD--TRAERLRALHNFGLGHDGVgaginakmseaAAAMGLTSLEafaDAVAS 263
Cdd:pfam01212 187 TSYAD--SVTMCLSKGLGAPVGSVLAGSDDfiAKAIRQRKYLGGGLRQAGV-----------LAAAGLRALE---EGVAR 250
|
250 260 270
....*....|....*....|....*....|
gi 5902172 264 NRANYELYRQELSGLPGVRLIDYDPAERNN 293
Cdd:pfam01212 251 LARDHATARRLAEGLELLRLAIPRRVYTNT 280
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
92-174 |
5.80e-07 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 51.28 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 92 EVIMPSMTFVATAHAVRWLGLRPVFCDIDPDTG-CLDPKLVEAAVTPRT------------GAILGvhlwgrPSRVDELA 158
Cdd:PRK05764 117 EVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENGfKLTVEQLEAAITPKTkalilnspsnptGAVYS------PEELEAIA 190
|
90 100
....*....|....*....|....*
gi 5902172 159 AIAAEHGL---------KLFYDAAH 174
Cdd:PRK05764 191 DVAVEHDIwvlsdeiyeKLVYDGAE 215
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
71-175 |
8.54e-05 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 44.34 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 71 VATCNATAGLQLLLREAEVTG-EVIMPSMTFVATAHAVRWLGLRPVFCDIDPDTGC-LDPKLVEAAVTPRTGAIL----- 143
Cdd:PRK07682 85 IVTVGASQALDVAMRAIINPGdEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENEFkVQPAQIEAAITAKTKAILlcspn 164
|
90 100 110
....*....|....*....|....*....|....*
gi 5902172 144 ---GVHLwgRPSRVDELAAIAAEHGLKLFYDAAHA 175
Cdd:PRK07682 165 nptGAVL--NKSELEEIAVIVEKHDLIVLSDEIYA 197
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
56-265 |
1.11e-04 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 43.83 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 56 EFEQRIADLAGVRN----------CVATCnATAGLQLLLREAEVTG-EVIMPSMTFVATAHAVRWLGLRPVFCDI-DPDT 123
Cdd:pfam00155 43 ELREALAKFLGRSPvlkldreaavVFGSG-AGANIEALIFLLANPGdAILVPAPTYASYIRIARLAGGEVVRYPLyDSND 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 124 GCLDPKLVEAAVTPRTGAIL--------GVHLwgRPSRVDELAAIAAEHGLKLFYDAAHALGCtsrqrrLGSFGDAEVFS 195
Cdd:pfam00155 122 FHLDFDALEAALKEKPKVVLhtsphnptGTVA--TLEELEKLLDLAKEHNILLLVDEAYAGFV------FGSPDAVATRA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 196 FHATK----VVNSF--------EGGGIVTDDDTRAERLRALHNFGLGhDGVGAGINAKMSEaAAAMGLTSLEAFADAVAS 263
Cdd:pfam00155 194 LLAEGpnllVVGSFskafglagWRVGYILGNAAVISQLRKLARPFYS-STHLQAAAAAALS-DPLLVASELEEMRQRIKE 271
|
..
gi 5902172 264 NR 265
Cdd:pfam00155 272 RR 273
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
59-197 |
1.18e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 43.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 59 QRIADLAGVR---NCVATCNATAGLQLL------LREAEvtgEVIMPSM----TFVATAHAVRWLGLRPVFCDIDPDtGC 125
Cdd:COG0520 66 EKVARFIGAAspdEIIFTRGTTEAINLVayglgrLKPGD---EILITEMehhsNIVPWQELAERTGAEVRVIPLDED-GE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 126 LDPKLVEAAVTPRT------------GAILGVHlwgrpsrvdELAAIAAEHGLKLFYDAAHA----------LGCtsrqr 183
Cdd:COG0520 142 LDLEALEALLTPRTklvavthvsnvtGTVNPVK---------EIAALAHAHGALVLVDGAQSvphlpvdvqaLGC----- 207
|
170
....*....|....
gi 5902172 184 rlgsfgDAEVFSFH 197
Cdd:COG0520 208 ------DFYAFSGH 215
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
52-222 |
2.77e-04 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 42.71 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 52 PLVREFEQRIADLAGVRNCVATCNATAGLQLLLRE-AEVTGEVIMPSmtfvaTAHAVRW----------LGLRPVfcdiD 120
Cdd:cd06502 32 PTTAKLEARAAELFGKEAALFVPSGTAANQLALAAhTQPGGSVICHE-----TAHIYTDeagapeflsgVKLLPV----P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 121 PDTGCLDPKLVEAAVT-------PRTGAI-------LGVhlwGRPsrVDELAAIAA---EHGLKL------FYDAAHALG 177
Cdd:cd06502 103 GENGKLTPEDLEAAIRprddihfPPPSLVslentteGGT---VYP--LDELKAISAlakENGLPLhldgarLANAAAALG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5902172 178 CTSRQRRLGsfgdAEVFSFHATKVVNSFEGGGIVTDDD--TRAERLR 222
Cdd:cd06502 178 VALKTYKSG----VDSVSFCLSKGGGAPVGAVVVGNRDfiARARRRR 220
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
92-284 |
5.41e-04 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 41.87 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 92 EVIMPSMTFVATAHAVRWLGLRPVFCDIDPDTGCL-DPKLVEAAVTPRTGAIL--------GVHLwgRPSRVDELAAIAA 162
Cdd:PRK07550 116 EVILPLPWYFNHKMWLDMLGIRPVYLPCDEGPGLLpDPAAAEALITPRTRAIAlvtpnnptGVVY--PPELLHELYDLAR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 163 EHGLKLFYD-----------AAHALGCTSRqrrlgsFGDAEV--FSFHATKVVNSFEGGGIVTDDDTRAERLRALHNFgl 229
Cdd:PRK07550 194 RHGIALILDetyrdfdsgggAPHDLFADPD------WDDTLVhlYSFSKSYALTGHRVGAVVASPARIAEIEKFMDTV-- 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5902172 230 ghdgvgAGINAKMSEAAAAMGLTSLeafADAVASNRA----NYELYRQELSGLPGVRLI 284
Cdd:PRK07550 266 ------AICAPRIGQIAVAWGLPNL---ADWRAGNRAeiarRRDAFRAVFARLPGWELL 315
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
49-143 |
1.89e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 40.18 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902172 49 NGG-PLVRefeQRIADLAGVR--------NCVATCNATAGLQLLLREAEVTG-EVIMPSMTFVATAHAVRWLGLRPVFCD 118
Cdd:PRK06836 72 NAGyPEVR---EAIAESLNRRfgtpltadHIVMTCGAAGALNVALKAILNPGdEVIVFAPYFVEYRFYVDNHGGKLVVVP 148
|
90 100
....*....|....*....|....*
gi 5902172 119 IDPDTGCLDPKLVEAAVTPRTGAIL 143
Cdd:PRK06836 149 TDTDTFQPDLDALEAAITPKTKAVI 173
|
|
| |
