|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
8-401 |
2.82e-153 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 437.58 E-value: 2.82e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 8 TIPFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTY 87
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 88 TASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVEskkkifnpKNDLqslfnr 167
Cdd:COG0399 81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAK--------KHGL------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 168 vIVMTDGAHAFGAIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVWrnnqglDDEWLYKQFMLYSLHGQSKDAlakvqk 247
Cdd:COG0399 147 -KVIEDAAQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVT------NDEELAERARSLRNHGRDRDA------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 248 gawEYDIVYPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSGHLYLVRIPgiSE 327
Cdd:COG0399 214 ---KYEHVELGYNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLD--EG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100952959 328 NQRNEIVVKMAEAGVACNVHY-KPLPMFTAYKNLGFDIHDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFKKI 401
Cdd:COG0399 289 EDRDELIAALKARGIGTRVHYpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
20-399 |
1.52e-135 |
|
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: 392.29 E-value: 1.52e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 20 EIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYTASASIIEHVGA 99
Cdd:cd00616 1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 100 KIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVESKkkifnpkndlqslfnRVIVMTDGAHAFG 179
Cdd:cd00616 81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRH---------------GLPVIEDAAQALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 180 AIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVWrnnqglDDEWLYKQFMLYSLHGQSKDalakvqkgAWEYDIVYPAY 259
Cdd:cd00616 146 ATYKGRKVGTFGDAGAFSFHPTKNLTTGEGGAVVT------NDEELAERARLLRNHGRDRD--------RFKYEHEILGY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 260 KCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSGHLYLVRIPGISENQRNEIVVKMAE 339
Cdd:cd00616 212 NYRLSEIQAAIGLAQLEKLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKE 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100952959 340 AGVACNVHYKPLPMFTAYK-NLGFDIHDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFK 399
Cdd:cd00616 292 AGIETRVHYPPLHHQPPYKkLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
14-399 |
1.33e-110 |
|
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: 328.86 E-value: 1.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 14 PDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYTASASI 93
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 94 IEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVESKKkifnpkndlqslfnrVIVMTD 173
Cdd:pfam01041 81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHG---------------LPVIED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 174 GAHAFGAIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYKQFMLYSLHGQSKDALAKvqkgaWEYD 253
Cdd:pfam01041 146 AAHALGATYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVV------TNDPELAEKARVLRNHGMVRKADKR-----YWHE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 254 IvyPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSG-HLYLVRIPGISENqRNE 332
Cdd:pfam01041 215 V--LGYNYRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAwHLFPILVPEEAIN-RDE 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1100952959 333 IVVKMAEAGVACNVHY-KPLPMFTAYKNLGFDI-HDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFK 399
Cdd:pfam01041 292 LVEALKEAGIGTRVHYpIPLHLQPYYRDLFGYApGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
9-401 |
1.11e-108 |
|
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: 324.67 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 9 IPFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYT 88
Cdd:TIGR03588 1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 89 ASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAIT----EKTKVIIPVDIAGKMCDYDTIYEiveskkkifnpkndLQSL 164
Cdd:TIGR03588 81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAA--------------LAKK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 165 FNRVIVmTDGAHAFGAIRNGMK--CGQVADFTCFSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYKQFMLYSLHGQSKD-- 240
Cdd:TIGR03588 147 HGLKII-EDASHALGAEYGGKPvgNCRYADATVFSFHPVKIITTAEGGAVT------TNDEELAERMRLLRSHGITKDpl 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 241 ALAKVQKGAWEYDIVYPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSGHLYLV 320
Cdd:TIGR03588 220 LFEKQDEGPWYYEQQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 321 RIPGISENQRNEIVVKMAEAGVACNVHYKPLPMFTAYKNlGFDIHDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFKK 400
Cdd:TIGR03588 300 LLDQEFGCTRKEVFEALRAAGIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRK 378
|
.
gi 1100952959 401 I 401
Cdd:TIGR03588 379 V 379
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
9-402 |
2.57e-78 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 246.86 E-value: 2.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 9 IPFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYT 88
Cdd:PRK11658 5 LPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 89 ASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVESKKkifnpkndlqslfnrV 168
Cdd:PRK11658 85 STLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYG---------------I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 169 IVMTDGAHAFGAIRNGMKCGQVAdfTC-FSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYKQFMLYSLHGQSKDALAKVQK 247
Cdd:PRK11658 150 PVIEDAAHAVGTYYKGRHIGARG--TAiFSFHAIKNITCAEGGLVV------TDDDELADRLRSLKFHGLGVDAFDRQTQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 248 G-AWEYDIVYPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRAL--LPLGIISLQHYGENfsSSGHLYLVRIP- 323
Cdd:PRK11658 222 GrAPQAEVLTPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALadLPFQPLSLPAWPHQ--HAWHLFIIRVDe 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 324 ---GISenqRNEIVVKMAEAGVACNVHYKPLPMFTAYKNLGFDIHdYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFKK 400
Cdd:PRK11658 300 ercGIS---RDALMEALKERGIGTGLHFRAAHTQKYYRERFPTLS-LPNTEWNSERICSLPLFPDMTDADVDRVITALQQ 375
|
..
gi 1100952959 401 IM 402
Cdd:PRK11658 376 IA 377
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
8-401 |
2.82e-153 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 437.58 E-value: 2.82e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 8 TIPFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTY 87
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 88 TASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVEskkkifnpKNDLqslfnr 167
Cdd:COG0399 81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAK--------KHGL------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 168 vIVMTDGAHAFGAIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVWrnnqglDDEWLYKQFMLYSLHGQSKDAlakvqk 247
Cdd:COG0399 147 -KVIEDAAQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVT------NDEELAERARSLRNHGRDRDA------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 248 gawEYDIVYPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSGHLYLVRIPgiSE 327
Cdd:COG0399 214 ---KYEHVELGYNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLD--EG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100952959 328 NQRNEIVVKMAEAGVACNVHY-KPLPMFTAYKNLGFDIHDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFKKI 401
Cdd:COG0399 289 EDRDELIAALKARGIGTRVHYpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
20-399 |
1.52e-135 |
|
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: 392.29 E-value: 1.52e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 20 EIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYTASASIIEHVGA 99
Cdd:cd00616 1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 100 KIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVESKkkifnpkndlqslfnRVIVMTDGAHAFG 179
Cdd:cd00616 81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRH---------------GLPVIEDAAQALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 180 AIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVWrnnqglDDEWLYKQFMLYSLHGQSKDalakvqkgAWEYDIVYPAY 259
Cdd:cd00616 146 ATYKGRKVGTFGDAGAFSFHPTKNLTTGEGGAVVT------NDEELAERARLLRNHGRDRD--------RFKYEHEILGY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 260 KCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSGHLYLVRIPGISENQRNEIVVKMAE 339
Cdd:cd00616 212 NYRLSEIQAAIGLAQLEKLDEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKE 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100952959 340 AGVACNVHYKPLPMFTAYK-NLGFDIHDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFK 399
Cdd:cd00616 292 AGIETRVHYPPLHHQPPYKkLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
14-399 |
1.33e-110 |
|
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: 328.86 E-value: 1.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 14 PDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYTASASI 93
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 94 IEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVESKKkifnpkndlqslfnrVIVMTD 173
Cdd:pfam01041 81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHG---------------LPVIED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 174 GAHAFGAIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYKQFMLYSLHGQSKDALAKvqkgaWEYD 253
Cdd:pfam01041 146 AAHALGATYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVV------TNDPELAEKARVLRNHGMVRKADKR-----YWHE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 254 IvyPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSG-HLYLVRIPGISENqRNE 332
Cdd:pfam01041 215 V--LGYNYRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAwHLFPILVPEEAIN-RDE 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1100952959 333 IVVKMAEAGVACNVHY-KPLPMFTAYKNLGFDI-HDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFK 399
Cdd:pfam01041 292 LVEALKEAGIGTRVHYpIPLHLQPYYRDLFGYApGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
9-401 |
1.11e-108 |
|
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: 324.67 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 9 IPFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYT 88
Cdd:TIGR03588 1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 89 ASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAIT----EKTKVIIPVDIAGKMCDYDTIYEiveskkkifnpkndLQSL 164
Cdd:TIGR03588 81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAA--------------LAKK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 165 FNRVIVmTDGAHAFGAIRNGMK--CGQVADFTCFSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYKQFMLYSLHGQSKD-- 240
Cdd:TIGR03588 147 HGLKII-EDASHALGAEYGGKPvgNCRYADATVFSFHPVKIITTAEGGAVT------TNDEELAERMRLLRSHGITKDpl 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 241 ALAKVQKGAWEYDIVYPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPLGIISLQHYGENFSSSGHLYLV 320
Cdd:TIGR03588 220 LFEKQDEGPWYYEQQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 321 RIPGISENQRNEIVVKMAEAGVACNVHYKPLPMFTAYKNlGFDIHDYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFKK 400
Cdd:TIGR03588 300 LLDQEFGCTRKEVFEALRAAGIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRK 378
|
.
gi 1100952959 401 I 401
Cdd:TIGR03588 379 V 379
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
9-402 |
2.57e-78 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 246.86 E-value: 2.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 9 IPFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYT 88
Cdd:PRK11658 5 LPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 89 ASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVESKKkifnpkndlqslfnrV 168
Cdd:PRK11658 85 STLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYG---------------I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 169 IVMTDGAHAFGAIRNGMKCGQVAdfTC-FSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYKQFMLYSLHGQSKDALAKVQK 247
Cdd:PRK11658 150 PVIEDAAHAVGTYYKGRHIGARG--TAiFSFHAIKNITCAEGGLVV------TDDDELADRLRSLKFHGLGVDAFDRQTQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 248 G-AWEYDIVYPAYKCNMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRAL--LPLGIISLQHYGENfsSSGHLYLVRIP- 323
Cdd:PRK11658 222 GrAPQAEVLTPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALadLPFQPLSLPAWPHQ--HAWHLFIIRVDe 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 324 ---GISenqRNEIVVKMAEAGVACNVHYKPLPMFTAYKNLGFDIHdYPNAYKQYANEVTLPLHTLLSDEDVKYVVENFKK 400
Cdd:PRK11658 300 ercGIS---RDALMEALKERGIGTGLHFRAAHTQKYYRERFPTLS-LPNTEWNSERICSLPLFPDMTDADVDRVITALQQ 375
|
..
gi 1100952959 401 IM 402
Cdd:PRK11658 376 IA 377
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
9-401 |
7.89e-55 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 185.81 E-value: 7.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 9 IPFSPPDISETEIQEVVKALKSGWIT-TGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILGIGPGDEVITSAYTY 87
Cdd:PRK11706 2 IPFNKPPVVGTELDYIQQAMSSGKLCgDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 88 TASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIPVDIAGKMCDYDTIYEIVEskkkifnpKNDLqslfnr 167
Cdd:PRK11706 82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAK--------KHNL------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 168 vIVMTDGAHAFGAIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYK-------------QFmlysL 234
Cdd:PRK11706 148 -FVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALL------INDPALIEraeiirekgtnrsQF----F 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 235 HGQskdalakVQKGAWEyDI--VYPaykcnMTDIMASIGLIQLDRYEGLLQRRKEIIETYDRALLPL---GIISLQHYGE 309
Cdd:PRK11706 217 RGQ-------VDKYTWV-DIgsSYL-----PSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPLaeaGRIELPSIPD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 310 NFSSSGHLYLVRIPgiSENQRNEIVVKMAEAGVACNVHYKPLPMFTAYKNLGFDIHDYPNAYKQYANEVTLPLHTLLSDE 389
Cdd:PRK11706 284 DCKHNAHMFYIKLR--DLEDRSALINFLKEAGIMAVFHYIPLHSSPAGERFGRFHGEDRYTTKESERLLRLPLFYNLTDV 361
|
410
....*....|..
gi 1100952959 390 DVKYVVENFKKI 401
Cdd:PRK11706 362 EQRTVIDTILEF 373
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
5-287 |
5.02e-29 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 117.29 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 5 AGRT-IPFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAA-----MELTLRILG---IG 75
Cdd:PRK15407 30 PGKSpIPPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSAnllafSALTSPKLGdraLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 76 PGDEVITSAYTY-TASASIIEHvGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVIIpvdIA---GKMCDYDTIYEIVEsk 151
Cdd:PRK15407 110 PGDEVITVAAGFpTTVNPIIQN-GLVPVFVDVELPTYNIDASLLEAAVSPKTKAIM---IAhtlGNPFDLAAVKAFCD-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 152 kkifnpKNDLQslfnrviVMTDGAHAFGAIRNGMKCGQVADFTCFSFHAVKNLTTAEGGAVVwrnnqgLDDEWLYKQFML 231
Cdd:PRK15407 184 ------KHNLW-------LIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVF------TNDPLLKKIIES 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100952959 232 YSLHGQS------KD---------ALAKVQKGaweYD--IVYP--AYKCNMTDIMASIGLIQLDRYEGLLQRRKE 287
Cdd:PRK15407 245 FRDWGRDcwcapgCDntcgkrfgwQLGELPFG---YDhkYTYShlGYNLKITDMQAAIGLAQLEKLPGFIEARKA 316
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
11-149 |
5.75e-11 |
|
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: 63.61 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 11 FSPPDisetEIQE-VVKALKSGWI--TTGPRTKAFEKKIAQYV----GIN----RAVCLNSATAAMELTLRILgIGPGDE 79
Cdd:COG0436 42 FPTPD----HIREaAIEALDDGVTgyTPSAGIPELREAIAAYYkrryGVDldpdEILVTNGAKEALALALLAL-LNPGDE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100952959 80 VITSAYTYTASASIIEHVGAKIVLVDT-APDSFEMDYSKLAEAITEKTKVII------PvdiAGKMCDYDTIYEIVE 149
Cdd:COG0436 117 VLVPDPGYPSYRAAVRLAGGKPVPVPLdEENGFLPDPEALEAAITPRTKAIVlnspnnP---TGAVYSREELEALAE 190
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
40-177 |
7.53e-11 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 63.09 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 40 KAFEKKIAQYVGI--------NRAVCLNSATAAMELTLRILGIGPGDEVITSAYTYTASASIIEHVGAKIVLVD-TAPDS 110
Cdd:pfam00155 42 PELREALAKFLGRspvlkldrEAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlYDSND 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 111 FEMDYSKLAEAITEKTKVII---PVDIAGKMCDYDTIYEIVESKKKifnpkndlqslfNRVIVMTDGAHA 177
Cdd:pfam00155 122 FHLDFDALEAALKEKPKVVLhtsPHNPTGTVATLEELEKLLDLAKE------------HNILLLVDEAYA 179
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
10-130 |
9.65e-10 |
|
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: 59.66 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 10 PFSPPDISETEIQEVVKALKSGWITTGPRTKAFEKKIAQYVGI--------NRAVCLNSATAAMELTLRILgIGPGDEVI 81
Cdd:cd00609 9 DFPPPPEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRAL-LNPGDEVL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1100952959 82 TSAYTYTASASIIEHVGAKIVLVDTAPD-SFEMDYSKLAEAITEKTKVII 130
Cdd:cd00609 88 VPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLLY 137
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
59-155 |
4.53e-09 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 57.81 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 59 NSATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVII---PVDIA 135
Cdd:PRK07683 96 IGASEAIDIAFRTI-LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPSNPT 174
|
90 100
....*....|....*....|..
gi 1100952959 136 GKMCDYDTIYEIVE--SKKKIF 155
Cdd:PRK07683 175 GVTLSKEELQDIADvlKDKNIF 196
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
61-130 |
1.72e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 55.97 E-value: 1.72e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 61 ATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVII 130
Cdd:PRK06836 105 AAGALNVALKAI-LNPGDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVI 173
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
37-148 |
1.58e-07 |
|
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: 52.97 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 37 PRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHV----GAKIVLVDTApdsfe 112
Cdd:cd00614 40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYGGTYRLFERLlpklGIEVTFVDPD----- 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 1100952959 113 mDYSKLAEAITEKTKVII---PVDIAGKMCDYDTIYEIV 148
Cdd:cd00614 114 -DPEALEAAIKPETKLVYvesPTNPTLKVVDIEAIAELA 151
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
39-199 |
3.61e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 51.68 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 39 TKAFE---KKIAQYVGINRA---VCLNSATAAMELTLRILG-IGPGDEVITSAYTYtaSASII------EHVGAKIVLVD 105
Cdd:COG0520 58 TDAYEaarEKVARFIGAASPdeiIFTRGTTEAINLVAYGLGrLKPGDEILITEMEH--HSNIVpwqelaERTGAEVRVIP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 106 TAPDsFEMDYSKLAEAITEKTKVI----------IPVDIAgkmcdydtiyEIVESKKKifnpkndlqslfNRVIVMTDGA 175
Cdd:COG0520 136 LDED-GELDLEALEALLTPRTKLVavthvsnvtgTVNPVK----------EIAALAHA------------HGALVLVDGA 192
|
170 180
....*....|....*....|....*..
gi 1100952959 176 HAFGAIR---NGMKCgqvaDFTCFSFH 199
Cdd:COG0520 193 QSVPHLPvdvQALGC----DFYAFSGH 215
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
76-130 |
4.52e-07 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 51.66 E-value: 4.52e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1100952959 76 PGDEVITSAYTYTASASIIEHVGAKIVLVDTAPD-SFEMDYSKLAEAITEKTKVII 130
Cdd:PRK05764 114 PGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEEnGFKLTVEQLEAAITPKTKALI 169
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
61-138 |
1.19e-06 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 50.36 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 61 ATAAmeLTLRILG-IGPGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVII---PVDIAG 136
Cdd:PRK08912 96 ATEA--LAAALLAlVEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLlnnPLNPAG 173
|
..
gi 1100952959 137 KM 138
Cdd:PRK08912 174 KV 175
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
74-130 |
2.94e-06 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 49.14 E-value: 2.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1100952959 74 IGPGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVII 130
Cdd:PRK09082 112 VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLII 168
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
40-130 |
4.60e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 48.56 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 40 KAFEKKIAQYVGINRAVCLNSATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHVGAKIVLVDT-APDSFEMDYSKL 118
Cdd:PRK06348 77 KYYSKNYDLSFKRNEIMATVGACHGMYLALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILETyEEDGFQINVKKL 155
|
90
....*....|..
gi 1100952959 119 AEAITEKTKVII 130
Cdd:PRK06348 156 EALITSKTKAII 167
|
|
| PRK08248 |
PRK08248 |
homocysteine synthase; |
37-140 |
1.43e-05 |
|
homocysteine synthase;
Pssm-ID: 236201 [Multi-domain] Cd Length: 431 Bit Score: 47.15 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 37 PRTKAFEKKIAQYVGINRAVCLNSATAAmeLTLRILGI-GPGDEVITSAYTYTASASIIEH----VGAKIVLVD-TAPDS 110
Cdd:PRK08248 64 PTTDVFEKRIAALEGGIGALAVSSGQAA--ITYSILNIaSAGDEIVSSSSLYGGTYNLFAHtlpkLGITVKFVDpSDPEN 141
|
90 100 110
....*....|....*....|....*....|
gi 1100952959 111 FEmdysklaEAITEKTKVIIPVDIAGKMCD 140
Cdd:PRK08248 142 FE-------AAITDKTKALFAETIGNPKGD 164
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
40-181 |
1.56e-05 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 46.79 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 40 KAFEKKIAQYVGINRAVCLNSATAAMELTLRILGiGPGDEVITSAYTYtasASIIE---HVGAKIVLV---DtaPDSFEm 113
Cdd:cd06454 49 EELEEELAEFHGKEAALVFSSGYAANDGVLSTLA-GKGDLIISDSLNH---ASIIDgirLSGAKKRIFkhnD--MEDLE- 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100952959 114 dySKLAEAITEKTKVIIPVD----IAGKMCDydtIYEIVESKKKiFNpkndlqslfnrVIVMTDGAHAFGAI 181
Cdd:cd06454 122 --KLLREARRPYGKKLIVTEgvysMDGDIAP---LPELVDLAKK-YG-----------AILFVDEAHSVGVY 176
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
61-186 |
1.66e-05 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 46.65 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 61 ATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHVGAKIVLVDT-APDSFEMDYSKLAEAITEKTKVII---PVDIAG 136
Cdd:PRK07682 90 ASQALDVAMRAI-INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATtLENEFKVQPAQIEAAITAKTKAILlcsPNNPTG 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1100952959 137 KMCDYDTIYEIVEskkkiFNPKNDLQSLFNRVI--VMTDGAH-AFGAIRnGMK 186
Cdd:PRK07682 169 AVLNKSELEEIAV-----IVEKHDLIVLSDEIYaeLTYDEAYtSFASIK-GMR 215
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
42-138 |
4.43e-05 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 45.24 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 42 FEKKIAQYVGINRAVCLNSA-TAAMELTlrILG-IGPGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDSFEMDYSKLA 119
Cdd:PLN00175 104 FKKDTGLVVDPEKEVTVTSGcTEAIAAT--ILGlINPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELK 181
|
90 100
....*....|....*....|..
gi 1100952959 120 EAITEKTKVII---PVDIAGKM 138
Cdd:PLN00175 182 AAFTSKTRAILintPHNPTGKM 203
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
76-130 |
8.23e-05 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 44.39 E-value: 8.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1100952959 76 PGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITEKTKVII 130
Cdd:PRK12414 113 PGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
26-149 |
8.31e-05 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 44.54 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 26 KALKSGWITTGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHVGAKIVLVD 105
Cdd:PRK07324 54 KKLTYGWIEGSPEFKEAVASLYQNVKPENILQTNGATGANFLVLYAL-VEPGDHVISVYPTYQQLYDIPESLGAEVDYWQ 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1100952959 106 TAPDS-FEMDYSKLAEAITEKTKVII---PVDIAGKMCDYDTIYEIVE 149
Cdd:PRK07324 133 LKEENgWLPDLDELRRLVRPNTKLICinnANNPTGALMDRAYLEEIVE 180
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
35-147 |
1.75e-04 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 43.55 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 35 TGPRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHV----GAKIVLVDTA-PD 109
Cdd:PRK05994 61 TNPTNAVLEERVAALEGGTAALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINQFGHAfksfGWQVRWADADdPA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1100952959 110 SFEmdysklaEAITEKTKVIIPVDIA---GKMCDYDTIYEI 147
Cdd:PRK05994 140 SFE-------RAITPRTKAIFIESIAnpgGTVTDIAAIAEV 173
|
|
| PRK07503 |
PRK07503 |
methionine gamma-lyase; Provisional |
37-129 |
4.80e-04 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 181005 [Multi-domain] Cd Length: 403 Bit Score: 42.10 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 37 PRTKAFEKKIAQYVGINRAVCLNSATAAMELTLRILgIGPGDEVITSAYTYTASASIIEH----VGAKIVLVDTApdsfe 112
Cdd:PRK07503 65 PTLALLEQRMASLEGGEAAVALASGMGAITATLWTL-LRPGDEVIVDQTLYGCTFAFLHHglgeFGVTVRHVDLT----- 138
|
90
....*....|....*..
gi 1100952959 113 mDYSKLAEAITEKTKVI 129
Cdd:PRK07503 139 -DPAALKAAISDKTRMV 154
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
60-130 |
8.61e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 41.08 E-value: 8.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100952959 60 SATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHVGAKIVLV--DTAPDSFEMDYSKLAEAITEKTKVII 130
Cdd:PRK06108 92 SGVQALMLAAQAL-VGPGDEVVAVTPLWPNLVAAPKILGARVVCVplDFGGGGWTLDLDRLLAAITPRTRALF 163
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
39-129 |
1.33e-03 |
|
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: 40.53 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100952959 39 TKAFE---KKIAQYVGINRA---VCLNSATAAMELTLRILG--IGPGDEVITsaytytasaSIIEH-------------V 97
Cdd:cd06453 42 TDAYEaarEKVARFINAPSPdeiIFTRNTTEAINLVAYGLGraNKPGDEIVT---------SVMEHhsnivpwqqlaerT 112
|
90 100 110
....*....|....*....|....*....|..
gi 1100952959 98 GAKIVLVDTAPDSfEMDYSKLAEAITEKTKVI 129
Cdd:cd06453 113 GAKLKVVPVDDDG-QLDLEALEKLLTERTKLV 143
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
61-130 |
2.76e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 39.71 E-value: 2.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100952959 61 ATAAMELTLRILgIGPGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDSFEMDYSKLAEAITE---KTKVII 130
Cdd:PRK07309 100 ATEALSASLTAI-LEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILEqgdKLKAVI 171
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
61-130 |
3.52e-03 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 39.25 E-value: 3.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100952959 61 ATAAmeLTLRILG-IGPGDEVITSAYTYTASASIIEHVGAKIVLVDTAPDS--FEMDYSKLAEAITEKTKVII 130
Cdd:PRK07777 94 ATEA--IAAAVLGlVEPGDEVLLIEPYYDSYAAVIAMAGAHRVPVPLVPDGrgFALDLDALRAAVTPRTRALI 164
|
|
| |
