|
Name |
Accession |
Description |
Interval |
E-value |
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
18-364 |
1.84e-146 |
|
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: 418.10 E-value: 1.84e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 18 FIPYLEIIWQNKQFTNnGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVATAHSLVLNG 95
Cdd:cd00616 1 ELEAVEEVLDSGWLTL-GPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGpgDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 96 LKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHGDL 175
Cdd:cd00616 80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 176 SVLSFHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFGYIDETN---INIIGSNGKMSEVNAAFGLLQLEHMDTFLRGRMN 252
Cdd:cd00616 160 GAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFkyeHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 253 ADMFYRQKLKDITGISIVIPSGQKISNFSYFPILVESDFPLSRDELFNYLKNQNIFARRYFYPVIPDFQAYLNVG-EVCD 331
Cdd:cd00616 240 IAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLGyPPGD 319
|
330 340 350
....*....|....*....|....*....|...
gi 379332635 332 VKNAREIASKVLCLPMHAELSSDILEYIVSTIR 364
Cdd:cd00616 320 LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
4-366 |
1.42e-138 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 398.29 E-value: 1.42e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 4 PIFVTQPNLPplEEFIPYLEIIWQNKQFTNnGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTP 81
Cdd:COG0399 1 MIPLSRPSIG--EEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGpgDEVITPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 82 YSFVATAHSLVLNGLKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFG 161
Cdd:COG0399 78 FTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 162 VEDDDGSVLRHGDLSVLSFHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFGYIDETN--INIIGSNGKMSEVNAAFGLLQ 239
Cdd:COG0399 158 ATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKyeHVELGYNYRMDELQAAIGLAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 240 LEHMDTFLRGR-MNADmFYRQKLKDITGISIVIPSGQKISNFSYFPILVESdfPLSRDELFNYLKNQNIFARRYFYPVIP 318
Cdd:COG0399 238 LKRLDEFIARRrAIAA-RYREALADLPGLTLPKVPPGAEHVYHLYVIRLDE--GEDRDELIAALKARGIGTRVHYPIPLH 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 379332635 319 DFQAYLNVG-EVCDVKNAREIASKVLCLPMHAELSSDILEYIVSTIREI 366
Cdd:COG0399 315 LQPAYRDLGyRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
16-364 |
1.17e-111 |
|
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: 330.01 E-value: 1.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 16 EEFIPYLEIIWQNKQFTNnGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVATAHSLVL 93
Cdd:pfam01041 5 EEELAAVREVLKSGWLTT-GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGpgDEVITPSFTFVATANAALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 94 NGLKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHG 173
Cdd:pfam01041 84 LGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 174 DLSVLSFHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFG----YIDETNINIIGSNGKMSEVNAAFGLLQLEHMDTFLRG 249
Cdd:pfam01041 164 DAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGmvrkADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIAR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 250 RMNADMFYRQKLKDITGISIV-IPSGQKISNFSYFPILVESDFpLSRDELFNYLKNQNIFARRYFYPVIPDFQAYLNVGE 328
Cdd:pfam01041 244 RREIAALYQTLLADLPGFTPLtTPPEADVHAWHLFPILVPEEA-INRDELVEALKEAGIGTRVHYPIPLHLQPYYRDLFG 322
|
330 340 350
....*....|....*....|....*....|....*...
gi 379332635 329 V--CDVKNAREIASKVLCLPMHAELSSDILEYIVSTIR 364
Cdd:pfam01041 323 YapGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
28-366 |
5.38e-81 |
|
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: 252.25 E-value: 5.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 28 NKQFTNNGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVATAHSLVLNGLKPVFVDIDS 105
Cdd:TIGR03588 21 KSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGpgDRVWTTPITFVATANCALYCGAKVDFVDIDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 106 KTLNIDPRRIEEAITPE----TQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSV--LRHGDLSVLS 179
Cdd:TIGR03588 101 DTGNIDEDALEKKLAAAkgklPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVgnCRYADATVFS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 180 FHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFGYIDETNINI-------------IGSNGKMSEVNAAFGLLQLEHMDTF 246
Cdd:TIGR03588 181 FHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEkqdegpwyyeqqeLGFNYRMTDIQAALGLSQLKKLDRF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 247 LRGRMNADMFYRQKLKDITGISIVIPSGQKISNFSYFPILVESDFPLSRDELFNYLKNQNIFARRYFYPV--IPDFQAYL 324
Cdd:TIGR03588 261 VAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALRAAGIGVQVHYIPVhlQPYYRQGF 340
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 379332635 325 NVGevcDVKNAREIASKVLCLPMHAELSSDILEYIVSTIREI 366
Cdd:TIGR03588 341 GDG---DLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
11-366 |
1.10e-57 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 191.59 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 11 NLPPL--EEFIpYLEIIWQNKQFTNNGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVA 86
Cdd:PRK11706 5 NKPPVvgTELD-YIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQpgDEVIMPSYTFVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 87 TAHSLVLNGLKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDD 166
Cdd:PRK11706 84 TANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 167 ---GSVlrhGDLSVLSFHATKVFSTFEGGAIVCNSKEM-------KEK-IDRLKNF-GYIDETNINIIGSNGKMSEVNAA 234
Cdd:PRK11706 164 ralGTI---GHIGCFSFHETKNYTAGEGGALLINDPALieraeiiREKgTNRSQFFrGQVDKYTWVDIGSSYLPSELQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 235 FGLLQLEHMDTFLRGRMNADMFYRQKLKDIT---GISIVIPSGQKISNFSYFPILVESDfpLSRDELFNYLKNQNIFArr 311
Cdd:PRK11706 241 YLWAQLEAADRINQRRLALWQRYYDALAPLAeagRIELPSIPDDCKHNAHMFYIKLRDL--EDRSALINFLKEAGIMA-- 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 379332635 312 YF-YpvIP--DFQAYLNVGEVC-DVKNAREIASKVLCLPMHAELSSDILEYIVSTIREI 366
Cdd:PRK11706 317 VFhY--IPlhSSPAGERFGRFHgEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEF 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
18-364 |
1.84e-146 |
|
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: 418.10 E-value: 1.84e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 18 FIPYLEIIWQNKQFTNnGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVATAHSLVLNG 95
Cdd:cd00616 1 ELEAVEEVLDSGWLTL-GPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGpgDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 96 LKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHGDL 175
Cdd:cd00616 80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 176 SVLSFHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFGYIDETN---INIIGSNGKMSEVNAAFGLLQLEHMDTFLRGRMN 252
Cdd:cd00616 160 GAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFkyeHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 253 ADMFYRQKLKDITGISIVIPSGQKISNFSYFPILVESDFPLSRDELFNYLKNQNIFARRYFYPVIPDFQAYLNVG-EVCD 331
Cdd:cd00616 240 IAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLGyPPGD 319
|
330 340 350
....*....|....*....|....*....|...
gi 379332635 332 VKNAREIASKVLCLPMHAELSSDILEYIVSTIR 364
Cdd:cd00616 320 LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
4-366 |
1.42e-138 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 398.29 E-value: 1.42e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 4 PIFVTQPNLPplEEFIPYLEIIWQNKQFTNnGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTP 81
Cdd:COG0399 1 MIPLSRPSIG--EEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGpgDEVITPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 82 YSFVATAHSLVLNGLKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFG 161
Cdd:COG0399 78 FTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 162 VEDDDGSVLRHGDLSVLSFHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFGYIDETN--INIIGSNGKMSEVNAAFGLLQ 239
Cdd:COG0399 158 ATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKyeHVELGYNYRMDELQAAIGLAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 240 LEHMDTFLRGR-MNADmFYRQKLKDITGISIVIPSGQKISNFSYFPILVESdfPLSRDELFNYLKNQNIFARRYFYPVIP 318
Cdd:COG0399 238 LKRLDEFIARRrAIAA-RYREALADLPGLTLPKVPPGAEHVYHLYVIRLDE--GEDRDELIAALKARGIGTRVHYPIPLH 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 379332635 319 DFQAYLNVG-EVCDVKNAREIASKVLCLPMHAELSSDILEYIVSTIREI 366
Cdd:COG0399 315 LQPAYRDLGyRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
16-364 |
1.17e-111 |
|
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: 330.01 E-value: 1.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 16 EEFIPYLEIIWQNKQFTNnGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVATAHSLVL 93
Cdd:pfam01041 5 EEELAAVREVLKSGWLTT-GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGpgDEVITPSFTFVATANAALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 94 NGLKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHG 173
Cdd:pfam01041 84 LGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 174 DLSVLSFHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFG----YIDETNINIIGSNGKMSEVNAAFGLLQLEHMDTFLRG 249
Cdd:pfam01041 164 DAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGmvrkADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIAR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 250 RMNADMFYRQKLKDITGISIV-IPSGQKISNFSYFPILVESDFpLSRDELFNYLKNQNIFARRYFYPVIPDFQAYLNVGE 328
Cdd:pfam01041 244 RREIAALYQTLLADLPGFTPLtTPPEADVHAWHLFPILVPEEA-INRDELVEALKEAGIGTRVHYPIPLHLQPYYRDLFG 322
|
330 340 350
....*....|....*....|....*....|....*...
gi 379332635 329 V--CDVKNAREIASKVLCLPMHAELSSDILEYIVSTIR 364
Cdd:pfam01041 323 YapGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
28-366 |
5.38e-81 |
|
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: 252.25 E-value: 5.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 28 NKQFTNNGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVATAHSLVLNGLKPVFVDIDS 105
Cdd:TIGR03588 21 KSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGpgDRVWTTPITFVATANCALYCGAKVDFVDIDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 106 KTLNIDPRRIEEAITPE----TQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSV--LRHGDLSVLS 179
Cdd:TIGR03588 101 DTGNIDEDALEKKLAAAkgklPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVgnCRYADATVFS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 180 FHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFGYIDETNINI-------------IGSNGKMSEVNAAFGLLQLEHMDTF 246
Cdd:TIGR03588 181 FHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEkqdegpwyyeqqeLGFNYRMTDIQAALGLSQLKKLDRF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 247 LRGRMNADMFYRQKLKDITGISIVIPSGQKISNFSYFPILVESDFPLSRDELFNYLKNQNIFARRYFYPV--IPDFQAYL 324
Cdd:TIGR03588 261 VAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALRAAGIGVQVHYIPVhlQPYYRQGF 340
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 379332635 325 NVGevcDVKNAREIASKVLCLPMHAELSSDILEYIVSTIREI 366
Cdd:TIGR03588 341 GDG---DLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
11-366 |
1.10e-57 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 191.59 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 11 NLPPL--EEFIpYLEIIWQNKQFTNNGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVA 86
Cdd:PRK11706 5 NKPPVvgTELD-YIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQpgDEVIMPSYTFVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 87 TAHSLVLNGLKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDD 166
Cdd:PRK11706 84 TANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 167 ---GSVlrhGDLSVLSFHATKVFSTFEGGAIVCNSKEM-------KEK-IDRLKNF-GYIDETNINIIGSNGKMSEVNAA 234
Cdd:PRK11706 164 ralGTI---GHIGCFSFHETKNYTAGEGGALLINDPALieraeiiREKgTNRSQFFrGQVDKYTWVDIGSSYLPSELQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 235 FGLLQLEHMDTFLRGRMNADMFYRQKLKDIT---GISIVIPSGQKISNFSYFPILVESDfpLSRDELFNYLKNQNIFArr 311
Cdd:PRK11706 241 YLWAQLEAADRINQRRLALWQRYYDALAPLAeagRIELPSIPDDCKHNAHMFYIKLRDL--EDRSALINFLKEAGIMA-- 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 379332635 312 YF-YpvIP--DFQAYLNVGEVC-DVKNAREIASKVLCLPMHAELSSDILEYIVSTIREI 366
Cdd:PRK11706 317 VFhY--IPlhSSPAGERFGRFHgEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEF 373
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
35-365 |
1.85e-51 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 177.00 E-value: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 35 GPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQA-----LGVKG-----EVITTPYSFVATAHSLVLNGLKPVFVDID 104
Cdd:PRK15407 62 GRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSAltspkLGDRAlkpgdEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 105 SKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHGDLSVLSF---- 180
Cdd:PRK15407 142 LPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFypah 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 181 HATkvfsTFEGGAIVCNSKEMKEKIDRLKN---------------------------FGYIDETNINIIGSNGKMSEVNA 233
Cdd:PRK15407 222 HIT----MGEGGAVFTNDPLLKKIIESFRDwgrdcwcapgcdntcgkrfgwqlgelpFGYDHKYTYSHLGYNLKITDMQA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 234 AFGLLQLEHMDTFLRGRMNADMFYRQKLKDITGiSIVIPSGQKISNFSYF--PILVESDFPLSRDELFNYLKNQNIFARR 311
Cdd:PRK15407 298 AIGLAQLEKLPGFIEARKANFAYLKEGLASLED-FLILPEATPNSDPSWFgfPITVKEDAGFTRVELVKYLEENKIGTRL 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 379332635 312 YFYPVIPDFQAYLNVGE--VCDVKNAREIASKVLCLPMHAELSSDILEYIVSTIRE 365
Cdd:PRK15407 377 LFAGNLTRQPYFKGVKYrvVGELTNTDRIMNDTFWIGVYPGLTEEMLDYVIEKIEE 432
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
35-307 |
4.26e-47 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 164.04 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 35 GPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVATAHSLVLNGLKPVFVDIDSKTLNIDP 112
Cdd:PRK11658 32 GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGpgDEVITPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 113 RRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHGDlSVLSFHATKVFSTFEGG 192
Cdd:PRK11658 112 EAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHIGARGT-AIFSFHAIKNITCAEGG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 193 AIVCNSKEMKEKIDRLKNFGY-IDETNINIIGSNGK-----------MSEVNAAFGLLQLEHMDTFLRGRMNADMFYRQK 260
Cdd:PRK11658 191 LVVTDDDELADRLRSLKFHGLgVDAFDRQTQGRAPQaevltpgykynLADINAAIALVQLAKLEALNARRREIAARYLQA 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 379332635 261 LKDITGISIVIPSGQKISNFSYFPILVESDF-PLSRDELFNYLKNQNI 307
Cdd:PRK11658 271 LADLPFQPLSLPAWPHQHAWHLFIIRVDEERcGISRDALMEALKERGI 318
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
11-366 |
1.71e-46 |
|
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131432 Cd Length: 376 Bit Score: 162.68 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 11 NLPP-LEEFIPYLEIIWQNKQFTNNGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVK--GEVITTPYSFVAT 87
Cdd:TIGR02379 5 NKPPvTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQpgDEVIMPSYTFVST 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 88 AHSLVLNGLKPVFVDIDSKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDG 167
Cdd:TIGR02379 85 ANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMSTYKGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 168 SVLRHGDLSVLSFHATK-VFSTFEGGAIVCNSKEMKEK--------IDRLKNF-GYIDETNINIIGSNGKMSEVNAAFGL 237
Cdd:TIGR02379 165 ALGSIGHIGTFSFHETKnYTSGGEGGALLINDQAFIERaeiirekgTNRSQFFrGEVDKYTWRDIGSSYLPSELQAAYLW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 238 LQLEHMDTFLRGRMNADMFYRQKLKDITGISIV----IPSGQKiSNFSYFPILVESDfpLSRDELFNYLKNQNIFARRYF 313
Cdd:TIGR02379 245 AQLEQADRINQQRLALWQNYYDALAPLEEKGIIelpsIPDGCQ-HNAHMFYIKLRDI--DDRSELINFLKEQEIMAVFHY 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 379332635 314 YPvIPDFQAYLNVGEVC--DVKNAREiASKVLCLPMHAELSSDILEYIVSTIREI 366
Cdd:TIGR02379 322 IP-LHSSPAGRHFGRFHgeDIYTTKE-SERLVRLPLFYGLSPEDQRRVIATLCDY 374
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
9-320 |
5.38e-16 |
|
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: 78.15 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 9 QPNLPPLEEFIPYLEIIWQNKQFTNNGPM--HQKLEKKLCEFLGVEY--------ISLFNNGTIALITAVQALGVKG-EV 77
Cdd:cd00609 7 EPDFPPPPEVLEALAAAALRAGLLGYYPDpgLPELREAIAEWLGRRGgvdvppeeIVVTNGAQEALSLLLRALLNPGdEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 78 ITTPYSFVATAHSLVLNGLKPVFVDIDSK-TLNIDPRRIEEAITPETQAIMpVHCYGNPCDT-------QAIADIAQKYN 149
Cdd:cd00609 87 LVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLLY-LNNPNNPTGAvlseeelEELAELAKKHG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 150 LKVIYDAAHA-FGVEDDDGSVLRHGD-----LSVLSFhaTKVFST--FEGGAIVCNSKEMKEKIDRLKNFGYIdetNINI 221
Cdd:cd00609 166 ILIISDEAYAeLVYDGEPPPALALLDayervIVLRSF--SKTFGLpgLRIGYLIAPPEELLERLKKLLPYTTS---GPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 222 IGsngkmsevnAAFGLLQLEHMDTFLRG-----RMNADMFYrQKLKDITGISIVIPSGqkisnfSYFpILVESDFPLSRD 296
Cdd:cd00609 241 LS---------QAAAAAALDDGEEHLEElreryRRRRDALL-EALKELGPLVVVKPSG------GFF-LWLDLPEGDDEE 303
|
330 340
....*....|....*....|....*.
gi 379332635 297 ELFNYLKNQNIFAR--RYFYPVIPDF 320
Cdd:cd00609 304 FLERLLLEAGVVVRpgSAFGEGGEGF 329
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
30-318 |
9.77e-16 |
|
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: 77.22 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 30 QFTNNGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVKGEVIttpYSfVATAHSLVLNGL------KPVFVDI 103
Cdd:cd06454 40 LISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAGKGDLI---IS-DSLNHASIIDGIrlsgakKRIFKHN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 104 DSKTLNidpRRIEEAITPETQAI--------MPvhcyGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGS------- 168
Cdd:cd06454 116 DMEDLE---KLLREARRPYGKKLivtegvysMD----GDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRgveefgg 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 169 VLRHGDLSVLSFhaTKVFSTFeGGAIVCNskemKEKIDRLKNF--GYIDETNiniigsngkMSEVNAAFGLLQLEHM--D 244
Cdd:cd06454 189 LTDDVDIIMGTL--GKAFGAV-GGYIAGS----KELIDYLRSYarGFIFSTS---------LPPAVAAAALAALEVLqgG 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379332635 245 TFLRGR--MNADMFyRQKLKDItGISIvipsgqkISNFSYFPILVESDFPLSRDELFNYLKNQNIFARRYFYPVIP 318
Cdd:cd06454 253 PERRERlqENVRYL-RRGLKEL-GFPV-------GGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
38-195 |
5.02e-12 |
|
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: 63.56 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 38 HQKLEKKLCEFL--GVEYISLFNNGTIALITAVQALGVKG-EVITTPYSFVA-TAHSLVLNGLKPVFVDIDSKTLNIDPR 113
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGdEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 114 --RIEEAITPETQAIMPVHCYGNPCDTQA---IADIAQKYNLKVIYDAAHAFG------VEDDDGsvlrHGDLSVLSFHa 182
Cdd:cd01494 82 aiLEELKAKPNVALIVITPNTTSGGVLVPlkeIRKIAKEYGILLLVDAASAGGaspapgVLIPEG----GADVVTFSLH- 156
|
170
....*....|...
gi 379332635 183 tKVFSTFEGGAIV 195
Cdd:cd01494 157 -KNLGGEGGGVVI 168
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
34-210 |
6.13e-10 |
|
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: 59.91 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 34 NGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVKGEVITTP-------YSFVAtaHSLVLNGLKPVFVDIDsk 106
Cdd:cd00614 38 GNPTVDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASddlyggtYRLFE--RLLPKLGIEVTFVDPD-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 107 tlniDPRRIEEAITPETQAIMpVHCYGNP----CDTQAIADIAQKYNLKVIYDAAHAFGVEDDDgsvLRHG-DLSVLSfh 181
Cdd:cd00614 114 ----DPEALEAAIKPETKLVY-VESPTNPtlkvVDIEAIAELAHEHGALLVVDNTFATPYLQRP---LELGaDIVVHS-- 183
|
170 180 190
....*....|....*....|....*....|..
gi 379332635 182 ATKVF---STFEGGAIVCNSKEMKEKIDRLKN 210
Cdd:cd00614 184 ATKYIgghSDVIAGVVVGSGEALIQRLRFLRL 215
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
34-214 |
7.31e-10 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 59.68 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 34 NGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVKGEVIttpysFV-ATAHSLVLNGLK----PVFV----DID 104
Cdd:COG0156 80 TTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLI-----FSdELNHASIIDGARlsgaKVVRfrhnDMD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 105 SktLNidpRRIEEAITPETQAI-------MpvhcYGNPCDTQAIADIAQKYNLKVIYDAAHAFGV--EDDDGSVLRHG-- 173
Cdd:COG0156 155 D--LE---RLLKKARAARRKLIvtdgvfsM----DGDIAPLPEIVELAEKYGALLYVDDAHGTGVlgETGRGLVEHFGle 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 379332635 174 ---DLSVLSFhaTKVFSTFeGGAIVCnSKEMkekIDRLKNF--GYI 214
Cdd:COG0156 226 drvDIIMGTL--SKALGSS-GGFVAG-SKEL---IDYLRNRarPFI 264
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
38-320 |
1.73e-09 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 58.47 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 38 HQKLEKKLCEFLGVEYIS--------LFNNGTIALI-TAVQALGVKGEVITTP-YSFVATAHSLVLNGLKPVFVDI-DSK 106
Cdd:pfam00155 41 HPELREALAKFLGRSPVLkldreaavVFGSGAGANIeALIFLLANPGDAILVPaPTYASYIRIARLAGGEVVRYPLyDSN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 107 TLNIDPRRIEEAITPETQAImpVHCY-GNPCDT-------QAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHGDLS-V 177
Cdd:pfam00155 121 DFHLDFDALEAALKEKPKVV--LHTSpHNPTGTvatleelEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRALLAeG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 178 LSFHATKVFST------FEGGAIVCNSkEMKEKIDRLKNFGYIDETniniigsngkMSEVNAA------FGLLQLEHMDT 245
Cdd:pfam00155 199 PNLLVVGSFSKafglagWRVGYILGNA-AVISQLRKLARPFYSSTH----------LQAAAAAalsdplLVASELEEMRQ 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379332635 246 FLRGRmnADMFyRQKLKDItGISIVIPSGqkisnfSYFPILVESdfPLSRDELFNYLKNQ-NIFARRYFYPVIPDF 320
Cdd:pfam00155 268 RIKER--RDYL-RDGLQAA-GLSVLPSQA------GFFLLTGLD--PETAKELAQVLLEEvGVYVTPGSSPGVPGW 331
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
63-159 |
7.69e-08 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 53.59 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 63 ALITAVQALGVKG-EVITTPYSFVATAHSLVLNGLKPVFVDIDSKT-LNIDPRRIEEAITPETQAIM------PVHCYGN 134
Cdd:PRK07682 93 ALDVAMRAIINPGdEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcspnnPTGAVLN 172
|
90 100
....*....|....*....|....*
gi 379332635 135 PCDTQAIADIAQKYNLKVIYDAAHA 159
Cdd:PRK07682 173 KSELEEIAVIVEKHDLIVLSDEIYA 197
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
63-155 |
4.69e-07 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 51.28 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 63 ALITAVQALGVKG-EV-ITTPYsFVATAHSLVLNGLKPVFVDIDSKT-LNIDPRRIEEAITPETQAIM---PvhcyGNPC 136
Cdd:PRK05764 103 ALYNAFMALLDPGdEViIPAPY-WVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKALIlnsP----SNPT 177
|
90 100
....*....|....*....|....*.
gi 379332635 137 -------DTQAIADIAQKYNLKVIYD 155
Cdd:PRK05764 178 gavyspeELEAIADVAVEHDIWVLSD 203
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
39-157 |
6.02e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 47.21 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 39 QKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVKG-EVITTPYSFVAT----AHSlVLNGLKPVFVDIDsKTLNIDPR 113
Cdd:pfam01212 35 NRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGdEVICGEPAHIHFdetgGHA-ELGGVQPRPLDGD-EAGNMDLE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 379332635 114 RIEEAITPETQAIMP---VHCYGNPCDTQ-----------AIADIAQKYNLKVIYDAA 157
Cdd:pfam01212 113 DLEAAIREVGADIFPptgLISLENTHNSAggqvvslenlrEIAALAREHGIPVHLDGA 170
|
|
| SelA |
pfam03841 |
L-seryl-tRNA selenium transferase; |
41-209 |
7.32e-06 |
|
L-seryl-tRNA selenium transferase;
Pssm-ID: 309101 Cd Length: 367 Bit Score: 47.33 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 41 LEKKLCEFLGVEYISLFNNGTIALITAVQALGVKGEVITTPYSFVATAHSLVL------NGLKPVFVDIDSKTLNIDprr 114
Cdd:pfam03841 52 IEELLCELTGAEDALVVNNNAAAVLLVLNTLAAGKEVIISRGELVEIGGSFRIpdvmkqAGVKLVEVGTTNRTHLKD--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 115 IEEAITPETQAIMPVHC-------YGNPCDTQAIADIAQKYNLKVIYD---------AAHAFGVEDDDGSVLRHGdLSVL 178
Cdd:pfam03841 129 YEQAINENTALLMKVHTsnyriqgFTKEVELAELVELGHEKGLPVYEDlgsgslvdlSQYGLPKEPTVQELIAQG-VDLV 207
|
170 180 190
....*....|....*....|....*....|.
gi 379332635 179 SFHATKVFSTFEGGAIVCNskemKEKIDRLK 209
Cdd:pfam03841 208 SFSGDKLLGGPQAGIIVGK----KELIERIK 234
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
38-158 |
9.32e-06 |
|
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: 46.86 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 38 HQKLEKKLCEFLGVEYISLFNNGTIALI-TAVQALGVKGEVITTPY-SFVATAHSLVLNGLKPVFV--DIDSKT---LNI 110
Cdd:cd00615 61 IKEAQELAARAFGAKHTFFLVNGTSSSNkAVILAVCGPGDKILIDRnCHKSVINGLVLSGAVPVYLkpERNPYYgiaGGI 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 379332635 111 DPRRIEEAIT--PETQAIMPVHC--YGNPCDTQAIADIAQKYNLKVIYDAAH 158
Cdd:cd00615 141 PPETFKKALIehPDAKAAVITNPtyYGICYNLRKIVEEAHHRGLPVLVDEAH 192
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
20-165 |
2.70e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 45.83 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 20 PYLEIIWQNKQFTNNGPMHQ------------KLEKKLCEFLGVEY-----ISLFNNGTIALITAVQALGVKG-EVI-TT 80
Cdd:PRK05957 41 PPPEAIEALNNFLANPENHKyqavqgipplleAITQKLQQDNGIELnneqaIVVTAGSNMAFMNAILAITDPGdEIIlNT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 81 PYSFvatAH--SLVLNGLKPVFVDIDsKTLNIDPRRIEEAITPETQAIMPVHCyGNPC-------DTQAIADIAQKYNLK 151
Cdd:PRK05957 121 PYYF---NHemAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIVTISP-NNPTgvvypeaLLRAVNQICAEHGIY 195
|
170
....*....|....
gi 379332635 152 VIYDAAHAFGVEDD 165
Cdd:PRK05957 196 HISDEAYEYFTYDG 209
|
|
| SelA |
COG1921 |
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis]; |
38-157 |
3.38e-05 |
|
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441524 Cd Length: 399 Bit Score: 45.50 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 38 HQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVKGEVIttpysfVATAHsLV-------------LNGLKPVFVDID 104
Cdd:COG1921 67 YDHVEELLCELTGAEAALVVNNNAAAVLLALAALAAGKEVI------VSRGE-LVeiggsfripdvmaLSGAKLVEVGTT 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 105 SKTlniDPRRIEEAITPETQAIMPVHC-----YGNPC--DTQAIADIAQKYNLKVIYDAA 157
Cdd:COG1921 140 NRT---HLRDYEAAITENTAALLKVHTsnyriVGFTEevSLAELAELAHEHGLPVIVDLG 196
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
63-155 |
5.85e-05 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 44.56 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 63 ALITAVQALGVKG-EVI-TTPYSFvatAH--SLVLNGLKPVFVDIDSK-TLNIDPRRIEEAITPETQAIMPVhCYGNPCD 137
Cdd:PRK07550 102 AFWAAMVTLAGAGdEVIlPLPWYF---NHkmWLDMLGIRPVYLPCDEGpGLLPDPAAAEALITPRTRAIALV-TPNNPTG 177
|
90 100
....*....|....*....|....*
gi 379332635 138 T-------QAIADIAQKYNLKVIYD 155
Cdd:PRK07550 178 VvyppellHELYDLARRHGIALILD 202
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
43-166 |
1.37e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 43.59 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 43 KKLCEFLGV---EYISLFNNGTIALITAVQALGV--KG-EVITTPYSFvataHSLVL--------NGLKPVFVDIDsKTL 108
Cdd:COG0520 66 EKVARFIGAaspDEIIFTRGTTEAINLVAYGLGRlkPGdEILITEMEH----HSNIVpwqelaerTGAEVRVIPLD-EDG 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 109 NIDPRRIEEAITPETQ------------AIMPVHcygnpcdtqAIADIAQKYNLKVIYDAAHAFGVEDDD 166
Cdd:COG0520 141 ELDLEALEALLTPRTKlvavthvsnvtgTVNPVK---------EIAALAHAHGALVLVDGAQSVPHLPVD 201
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
39-208 |
1.39e-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: 43.48 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 39 QKLEKKLCEFLGVEYISLFNNGTIALITAVQALgvkgeviTTPYSFV---ATAHSL--------VLNGLKPVFVDIDSKT 107
Cdd:cd06502 35 AKLEARAAELFGKEAALFVPSGTAANQLALAAH-------TQPGGSVichETAHIYtdeagapeFLSGVKLLPVPGENGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 108 LniDPRRIEEAITPETQAIMP---------VH--CYGNPCD-TQAIADIAQKYNLKV------IYDAAHAFGVedDDGSV 169
Cdd:cd06502 108 L--TPEDLEAAIRPRDDIHFPppslvslenTTegGTVYPLDeLKAISALAKENGLPLhldgarLANAAAALGV--ALKTY 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 379332635 170 LRHGDlsVLSFHATKVFSTFeGGAIVCNSKEMKEKIDRL 208
Cdd:cd06502 184 KSGVD--SVSFCLSKGGGAP-VGAVVVGNRDFIARARRR 219
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
76-165 |
9.73e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 40.86 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 76 EVIT-TPYsFVATAHSLVLNGLKPVFVD-IDSKTLNIDPRRIEEAITPETQAIMpVHCYGNPCDT-------QAIADIAQ 146
Cdd:PRK06348 115 EVIIhEPY-FTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAII-LNSPNNPTGAvfsketlEEIAKIAI 192
|
90 100
....*....|....*....|
gi 379332635 147 KYNLKVIYDAAH-AFGVEDD 165
Cdd:PRK06348 193 EYDLFIISDEVYdGFSFYED 212
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
115-155 |
2.08e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 39.83 E-value: 2.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 379332635 115 IEEAITPETQAIMpvhcYGNPC----------DTQAIADIAQKYNLKVIYD 155
Cdd:PRK07568 155 IEKLITPKTKAIL----ISNPGnptgvvytkeELEMLAEIAKKHDLFLISD 201
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
88-155 |
2.24e-03 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 39.70 E-value: 2.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379332635 88 AHSLVLNGLKPVFVDIDsktlniDPRRIEEAITPETQAIMpVHCYGNP----CDTQAIADIAQKYNLKVIYD 155
Cdd:PRK05994 120 GHAFKSFGWQVRWADAD------DPASFERAITPRTKAIF-IESIANPggtvTDIAAIAEVAHRAGLPLIVD 184
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
38-214 |
3.05e-03 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 39.12 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 38 HQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVKGEVIttpysfvatahsLVLNGL-KPVFVDIDSKTLNI------ 110
Cdd:PLN03227 45 HLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKRGDLL------------VVDRGVnEALLVGVSLSRANVrwfrhn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 111 ---DPRRIEEAITPETQAI---MPVH--------CYGN-----PCDtqAIADIAQKYNLKVIYDAAHAFGVEDDDG-SVL 170
Cdd:PLN03227 113 dmkDLRRVLEQVRAQDVALkrkPTDQrrflvvegLYKNtgtlaPLK--ELVALKEEFHYRLILDESFSFGTLGKSGrGSL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 379332635 171 RHGDLSvLSFHATKVFSTFEG-----GAIVCNSKEMKEKiDRLKNFGYI 214
Cdd:PLN03227 191 EHAGLK-PMVHAEIVTFSLENafgsvGGMTVGSEEVVDH-QRLSGSGYC 237
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
49-155 |
8.54e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 38.00 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379332635 49 LGVEYISLFNNGTIALITAVQALGVKGE--VITTPY--SFVATAHSLvlnGLKPVFVDIDSK----TLNIDprRIEEAIT 120
Cdd:PRK06108 82 TPPERIAVTSSGVQALMLAAQALVGPGDevVAVTPLwpNLVAAPKIL---GARVVCVPLDFGgggwTLDLD--RLLAAIT 156
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 379332635 121 PETQAIMpVHCYGNPC-------DTQAIADIAQKYNLKVIYD 155
Cdd:PRK06108 157 PRTRALF-INSPNNPTgwtasrdDLRAILAHCRRHGLWIVAD 197
|
|
| |
