|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
4-378 |
2.85e-136 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 393.28 E-value: 2.85e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 4 RIFLSSPDVTQAEEDALVRAFRSNWIApLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLT 83
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLT-LGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 84 FAATANAITYTGAEPVFVDAD-ESGNMNPALLEQALTTlrreghEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAA 162
Cdd:COG0399 80 FVATANAILYVGATPVFVDIDpDTYNIDPEALEAAITP------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 163 ESLGATRDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQARQPVVHYEHTDIGYNYRLSNILAAL 242
Cdd:COG0399 154 QALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKYEHVELGYNYRMDELQAAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 243 GRAQLNRLEEMIERRRALRIRYRELFAAVPGVEMFGEPSGvdggpTRDNFWLSSILVDpgtAGFTAEDLRVHLAGQDIEA 322
Cdd:COG0399 234 GLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPG-----AEHVYHLYVIRLD---EGEDRDELIAALKARGIGT 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092787536 323 RPLW-KPMHLQPVFA--GRRAFTDGTGERLFTTGLSLPSGSVLDESSIGRVVESITSFL 378
Cdd:COG0399 306 RVHYpIPLHLQPAYRdlGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| NHT_00031 |
TIGR04181 |
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ... |
5-359 |
1.34e-125 |
|
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar.
Pssm-ID: 275034 Cd Length: 359 Bit Score: 366.10 E-value: 1.34e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 5 IFLSSPDVTQAEEDALVRAFRSNWIAPLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLTF 84
Cdd:TIGR04181 1 IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 85 AATANAITYTGAEPVFVDAD-ESGNMNPALLEQALTTL----------RREGHEIKAVVPVDLLGKTADHATIGRIAADH 153
Cdd:TIGR04181 81 VATANAISYLGAEPVFVDVDpDTLGLDPDALEEFLEEEaerkdgvlinKETGRRIKACVPVHVFGHPADMDEIMEICDEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 154 GAVVLSDAAESLGATRDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQARQP-VVHYEHTDIGYN 232
Cdd:TIGR04181 161 NLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPhPWEFEHDEVGYN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 233 YRLSNILAALGRAQLNRLEEMIERRRALRIRYRELFAAVPGVEMFGEPSGvdggpTRDNFWLSSILVDPGTAgftAEDLR 312
Cdd:TIGR04181 241 YRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGVEFLPEPAG-----ARSNYWLNALLLDSKLD---RDELL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1092787536 313 VHLAGQDIEARPLWKPMHLQPVFAGRRAFTDGTGERLFTTGLSLPSG 359
Cdd:TIGR04181 313 EALNENGIQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
16-374 |
4.13e-124 |
|
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: 361.86 E-value: 4.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 16 EEDALVRAFRSNWIaPLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLTFAATANAITYTG 95
Cdd:cd00616 1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 96 AEPVFVDADE-SGNMNPALLEQALTtlrregHEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAAESLGATRDGKQS 174
Cdd:cd00616 80 ATPVFVDIDPdTYNIDPELIEAAIT------PRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 175 AAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQARQPVVH-YEHTDIGYNYRLSNILAALGRAQLNRLEEM 253
Cdd:cd00616 154 GTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFkYEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 254 IERRRALRIRYRELFAAVPGVEMFGEPSGVDGgptrdNFWLSSILVDPGTaGFTAEDLRVHLAGQDIEARPLWKPMHLQP 333
Cdd:cd00616 234 IARRREIAERYKELLADLPGIRLPDVPPGVKH-----SYHLYVIRLDPEA-GESRDELIEALKEAGIETRVHYPPLHHQP 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1092787536 334 VFAGRRAFTDGT---GERLFTTGLSLPSGSVLDESSIGRVVESI 374
Cdd:cd00616 308 PYKKLLGYPPGDlpnAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
10-375 |
2.34e-98 |
|
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: 296.50 E-value: 2.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 10 PDVTQAEEDALVRAFRSNWIApLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLTFAATAN 89
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLT-TGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 90 AITYTGAEPVFVDAD-ESGNMNPALLEQALTTLRregheiKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAAESLGAT 168
Cdd:pfam01041 80 AALRLGAKPVFVDIDpDTYNIDPEAIEAAITPRT------KAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 169 RDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQ--ARQPVVHYEHTDIGYNYRLSNILAALGRAQ 246
Cdd:pfam01041 154 YQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHgmVRKADKRYWHEVLGYNYRMTEIQAAIGLAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 247 LNRLEEMIERRRALRIRYRELFAAVPGVemfgEPSGVDGGPTRDNFWLSSILVDpgTAGFTAEDLRVHLAGQDIEARPL- 325
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLADLPGF----TPLTTPPEADVHAWHLFPILVP--EEAINRDELVEALKEAGIGTRVHy 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1092787536 326 WKPMHLQPVFAGRRAFTDGT---GERLFTTGLSLPSGSVLDESSIGRVVESIT 375
Cdd:pfam01041 308 PIPLHLQPYYRDLFGYAPGDlpnAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
1-380 |
9.38e-54 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 182.15 E-value: 9.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 1 MTDRIFLSSPDVTQAEEDALVRAFRSNWIAPlGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTS 80
Cdd:PRK11658 1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITT-GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 81 SLTFAATANAITYTGAEPVFVDADESGNM-NPALLEQALTTlrreghEIKAVVPVDLLGKTADHATIGRIAADHGAVVLS 159
Cdd:PRK11658 80 SLTWVSTLNMIVLLGATPVMVDVDRDTLMvTPEAIEAAITP------RTKAIIPVHYAGAPADLDAIRAIGERYGIPVIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 160 DAAESLGATRDGKQSAAYGvAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLA------------TQARQPvvHYEHT 227
Cdd:PRK11658 154 DAAHAVGTYYKGRHIGARG-TAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKfhglgvdafdrqTQGRAP--QAEVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 228 DIGYNYRLSNILAALGRAQLNRLEEMIERRRALRIRYRELFAAVPgVEMFGEPSgvdgGPTRDNFWLSSILVDPGTAGFT 307
Cdd:PRK11658 231 TPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLP-FQPLSLPA----WPHQHAWHLFIIRVDEERCGIS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 308 AEDLRVHLAGQDIEARPLWKPMHLQPVFagRRAF-------TDGTGERLfttgLSLPSGSVLDESSIGRVVESITSFLES 380
Cdd:PRK11658 306 RDALMEALKERGIGTGLHFRAAHTQKYY--RERFptlslpnTEWNSERI----CSLPLFPDMTDADVDRVITALQQIAGQ 379
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
4-378 |
2.85e-136 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 393.28 E-value: 2.85e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 4 RIFLSSPDVTQAEEDALVRAFRSNWIApLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLT 83
Cdd:COG0399 1 MIPLSRPSIGEEEIAAVVEVLRSGWLT-LGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 84 FAATANAITYTGAEPVFVDAD-ESGNMNPALLEQALTTlrreghEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAA 162
Cdd:COG0399 80 FVATANAILYVGATPVFVDIDpDTYNIDPEALEAAITP------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 163 ESLGATRDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQARQPVVHYEHTDIGYNYRLSNILAAL 242
Cdd:COG0399 154 QALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKYEHVELGYNYRMDELQAAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 243 GRAQLNRLEEMIERRRALRIRYRELFAAVPGVEMFGEPSGvdggpTRDNFWLSSILVDpgtAGFTAEDLRVHLAGQDIEA 322
Cdd:COG0399 234 GLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPG-----AEHVYHLYVIRLD---EGEDRDELIAALKARGIGT 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092787536 323 RPLW-KPMHLQPVFA--GRRAFTDGTGERLFTTGLSLPSGSVLDESSIGRVVESITSFL 378
Cdd:COG0399 306 RVHYpIPLHLQPAYRdlGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| NHT_00031 |
TIGR04181 |
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ... |
5-359 |
1.34e-125 |
|
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar.
Pssm-ID: 275034 Cd Length: 359 Bit Score: 366.10 E-value: 1.34e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 5 IFLSSPDVTQAEEDALVRAFRSNWIAPLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLTF 84
Cdd:TIGR04181 1 IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 85 AATANAITYTGAEPVFVDAD-ESGNMNPALLEQALTTL----------RREGHEIKAVVPVDLLGKTADHATIGRIAADH 153
Cdd:TIGR04181 81 VATANAISYLGAEPVFVDVDpDTLGLDPDALEEFLEEEaerkdgvlinKETGRRIKACVPVHVFGHPADMDEIMEICDEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 154 GAVVLSDAAESLGATRDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQARQP-VVHYEHTDIGYN 232
Cdd:TIGR04181 161 NLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPhPWEFEHDEVGYN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 233 YRLSNILAALGRAQLNRLEEMIERRRALRIRYRELFAAVPGVEMFGEPSGvdggpTRDNFWLSSILVDPGTAgftAEDLR 312
Cdd:TIGR04181 241 YRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGVEFLPEPAG-----ARSNYWLNALLLDSKLD---RDELL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1092787536 313 VHLAGQDIEARPLWKPMHLQPVFAGRRAFTDGTGERLFTTGLSLPSG 359
Cdd:TIGR04181 313 EALNENGIQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
16-374 |
4.13e-124 |
|
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: 361.86 E-value: 4.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 16 EEDALVRAFRSNWIaPLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLTFAATANAITYTG 95
Cdd:cd00616 1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 96 AEPVFVDADE-SGNMNPALLEQALTtlrregHEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAAESLGATRDGKQS 174
Cdd:cd00616 80 ATPVFVDIDPdTYNIDPELIEAAIT------PRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 175 AAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQARQPVVH-YEHTDIGYNYRLSNILAALGRAQLNRLEEM 253
Cdd:cd00616 154 GTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFkYEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 254 IERRRALRIRYRELFAAVPGVEMFGEPSGVDGgptrdNFWLSSILVDPGTaGFTAEDLRVHLAGQDIEARPLWKPMHLQP 333
Cdd:cd00616 234 IARRREIAERYKELLADLPGIRLPDVPPGVKH-----SYHLYVIRLDPEA-GESRDELIEALKEAGIETRVHYPPLHHQP 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1092787536 334 VFAGRRAFTDGT---GERLFTTGLSLPSGSVLDESSIGRVVESI 374
Cdd:cd00616 308 PYKKLLGYPPGDlpnAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
10-375 |
2.34e-98 |
|
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: 296.50 E-value: 2.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 10 PDVTQAEEDALVRAFRSNWIApLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLTFAATAN 89
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLT-TGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 90 AITYTGAEPVFVDAD-ESGNMNPALLEQALTTLRregheiKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAAESLGAT 168
Cdd:pfam01041 80 AALRLGAKPVFVDIDpDTYNIDPEAIEAAITPRT------KAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 169 RDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQ--ARQPVVHYEHTDIGYNYRLSNILAALGRAQ 246
Cdd:pfam01041 154 YQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHgmVRKADKRYWHEVLGYNYRMTEIQAAIGLAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 247 LNRLEEMIERRRALRIRYRELFAAVPGVemfgEPSGVDGGPTRDNFWLSSILVDpgTAGFTAEDLRVHLAGQDIEARPL- 325
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLADLPGF----TPLTTPPEADVHAWHLFPILVP--EEAINRDELVEALKEAGIGTRVHy 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1092787536 326 WKPMHLQPVFAGRRAFTDGT---GERLFTTGLSLPSGSVLDESSIGRVVESIT 375
Cdd:pfam01041 308 PIPLHLQPYYRDLFGYAPGDlpnAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
8-378 |
3.55e-82 |
|
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: 255.72 E-value: 3.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 8 SSPDVTQAEEDALVRAFRSNWIAPlGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLTFAAT 87
Cdd:TIGR03588 4 GRQSIDQDDIDAVVEVLKSDFLTQ-GPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 88 ANAITYTGAEPVFVDAD-ESGNMNPALLEQALTTLRREghEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAAESLG 166
Cdd:TIGR03588 83 ANCALYCGAKVDFVDIDpDTGNIDEDALEKKLAAAKGK--LPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 167 ATRDGKQ--SAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLATQA--RQPVV---------HYEHTDIGYNY 233
Cdd:TIGR03588 161 AEYGGKPvgNCRYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGitKDPLLfekqdegpwYYEQQELGFNY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 234 RLSNILAALGRAQLNRLEEMIERRRALRIRYRELFAAVPGVEMFGEPSGvdggpTRDNFWLSSILVDPgTAGFTAEDLRV 313
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLG-----SKSAWHLYPILLDQ-EFGCTRKEVFE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092787536 314 HLAGQDIEARPLWKPMHLQPVFagRRAFTDG---TGERLFTTGLSLPSGSVLDESSIGRVVESITSFL 378
Cdd:TIGR03588 315 ALRAAGIGVQVHYIPVHLQPYY--RQGFGDGdlpSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
1-380 |
9.38e-54 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 182.15 E-value: 9.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 1 MTDRIFLSSPDVTQAEEDALVRAFRSNWIAPlGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTS 80
Cdd:PRK11658 1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITT-GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 81 SLTFAATANAITYTGAEPVFVDADESGNM-NPALLEQALTTlrreghEIKAVVPVDLLGKTADHATIGRIAADHGAVVLS 159
Cdd:PRK11658 80 SLTWVSTLNMIVLLGATPVMVDVDRDTLMvTPEAIEAAITP------RTKAIIPVHYAGAPADLDAIRAIGERYGIPVIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 160 DAAESLGATRDGKQSAAYGvAAAVSFNGNKIMTTSGGGALLTDDEEMAARTRYLA------------TQARQPvvHYEHT 227
Cdd:PRK11658 154 DAAHAVGTYYKGRHIGARG-TAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKfhglgvdafdrqTQGRAP--QAEVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 228 DIGYNYRLSNILAALGRAQLNRLEEMIERRRALRIRYRELFAAVPgVEMFGEPSgvdgGPTRDNFWLSSILVDPGTAGFT 307
Cdd:PRK11658 231 TPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLP-FQPLSLPA----WPHQHAWHLFIIRVDEERCGIS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 308 AEDLRVHLAGQDIEARPLWKPMHLQPVFagRRAF-------TDGTGERLfttgLSLPSGSVLDESSIGRVVESITSFLES 380
Cdd:PRK11658 306 RDALMEALKERGIGTGLHFRAAHTQKYY--RERFptlslpnTEWNSERI----CSLPLFPDMTDADVDRVITALQQIAGQ 379
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
4-379 |
3.33e-32 |
|
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: 124.55 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 4 RIFLSSPDVTQAEEDALVRAFRSNWIAPLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLT 83
Cdd:TIGR02379 1 MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 84 FAATANAITYTGAEPVFVDADESG-NMNPALLEQALTtlrregHEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAA 162
Cdd:TIGR02379 81 FVSTANAFVLRGAKIVFVDIRPDTmNIDETLIEAAIT------DRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 163 ESLGATRDGKQSAAYGVAAAVSFNGNKIMTTSG-GGALLTDDEEMAARTRYLATQA-------RQPVVHYEHTDIGYNYR 234
Cdd:TIGR02379 155 QGVMSTYKGRALGSIGHIGTFSFHETKNYTSGGeGGALLINDQAFIERAEIIREKGtnrsqffRGEVDKYTWRDIGSSYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 235 LSNILAALGRAQLNRLEEMIERRRALRIRYRELFAAVPGVEMFGEPSGVDGgpTRDN---FWLSSILVDPGTAgftaedL 311
Cdd:TIGR02379 235 PSELQAAYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGIIELPSIPDG--CQHNahmFYIKLRDIDDRSE------L 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092787536 312 RVHLAGQDIEARPLWKPMHLQPvfAGRRaFTDGTGERLFTTGLS-----LPSGSVLDESSIGRVVESITSFLE 379
Cdd:TIGR02379 307 INFLKEQEIMAVFHYIPLHSSP--AGRH-FGRFHGEDIYTTKESerlvrLPLFYGLSPEDQRRVIATLCDYLS 376
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
4-255 |
4.61e-31 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 121.48 E-value: 4.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 4 RIFLSSPDVTQAEEDALVRAFRSNWIAPLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVGPGDLVPTSSLT 83
Cdd:PRK11706 1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 84 FAATANAITYTGAEPVFVDAD-ESGNMNPALLEQALTtlrregHEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAA 162
Cdd:PRK11706 81 FVSTANAFVLRGAKIVFVDIRpDTMNIDETLIEAAIT------PKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 163 ESLGATRDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMAA-----------RTRYLatqaRQPVVHYEHTDIGY 231
Cdd:PRK11706 155 QGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIEraeiirekgtnRSQFF----RGQVDKYTWVDIGS 230
|
250 260
....*....|....*....|....
gi 1092787536 232 NYRLSNILAALGRAQLNRLEEMIE 255
Cdd:PRK11706 231 SYLPSELQAAYLWAQLEAADRINQ 254
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
15-382 |
8.72e-26 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 107.66 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 15 AEEDALVRAFRSNWIApLGPEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNL--------GVGPGDLVPTSSLTFAA 86
Cdd:PRK15407 45 KELQNLVDASLDFWLT-TGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALtspklgdrALKPGDEVITVAAGFPT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 87 TANAITYTGAEPVFVDAD-ESGNMNPALLEQALTtlrregHEIKAVVPVDLLGKTADHATIGRIAADHGAVVLSDAAESL 165
Cdd:PRK15407 124 TVNPIIQNGLVPVFVDVElPTYNIDASLLEAAVS------PKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDAL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 166 GATRDGKQSAAYGVAAAVSFNGNKIMTTSGGGALLTDDEEMA---------ARTRYLAT------------QARQPVVHY 224
Cdd:PRK15407 198 GSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKkiiesfrdwGRDCWCAPgcdntcgkrfgwQLGELPFGY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 225 EH----TDIGYNYRLSNILAALGRAQLNRLEEMIERRRALRIRYRELFAAVPGVEMFGEPSgvdggPTRDNFWLS-SILV 299
Cdd:PRK15407 278 DHkytySHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLEDFLILPEAT-----PNSDPSWFGfPITV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 300 DPGtAGFTAEDLRVHLAGQDIEARPLW-----KpmhlQPVFAGRR-------AFTDGTGERLFTTGLsLPSgsvLDESSI 367
Cdd:PRK15407 353 KED-AGFTRVELVKYLEENKIGTRLLFagnltR----QPYFKGVKyrvvgelTNTDRIMNDTFWIGV-YPG---LTEEML 423
|
410
....*....|....*
gi 1092787536 368 GRVVESITSFLESRA 382
Cdd:PRK15407 424 DYVIEKIEEFFGLNF 438
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
36-202 |
5.68e-10 |
|
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: 57.78 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 36 VDALESELAEYT--GRSHAVVLSSGTAALHLGLLNLgVGPGDLVPTSSLTF-AATANAITYTGAEPVFVDADEsgnmNPA 112
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHgSRYWVAAELAGAKPVPVPVDD----AGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 113 LLEQALTTLRRE-GHEIKAVV---PVDLLGKTADHATIGRIAADHGAVVLSDAAESLGATRDGKQSAAYGVAAAVSFNGN 188
Cdd:cd01494 77 GGLDVAILEELKaKPNVALIVitpNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 1092787536 189 KIMTTSGGGALLTD 202
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
6-162 |
3.64e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 54.62 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 6 FLSSPDVTQAEEDALvrAFRSNWIAPLGPEVDALESELAEYTGRSH--------AVVLSSGTAALHLGLLNLGVGPGDLV 77
Cdd:pfam00155 13 GDTLPAVAKAEKDAL--AGGTRNLYGPTDGHPELREALAKFLGRSPvlkldreaAVVFGSGAGANIEALIFLLANPGDAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 78 PTSSLTFAATANAITYTGAEPVFVDADESGNMNPAL--LEQALTTlrreghEIKAVV---PVDLLGKTADHA---TIGRI 149
Cdd:pfam00155 91 LVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFdaLEAALKE------KPKVVLhtsPHNPTGTVATLEeleKLLDL 164
|
170
....*....|...
gi 1092787536 150 AADHGAVVLSDAA 162
Cdd:pfam00155 165 AKEHNILLLVDEA 177
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
34-219 |
7.31e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 53.37 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 34 PEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGVgPGDLVP---TSSLTFAATANAITYTGAEPVFVDADESGNMN 110
Cdd:pfam01212 32 PTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQ-RGDEVIcgePAHIHFDETGGHAELGGVQPRPLDGDEAGNMD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 111 PALLEQAlttLRREGHEIKAVVPVDLLGKTADHA-----------TIGRIAADHGAVVLSDAAESLGATRDGKQSAA--Y 177
Cdd:pfam01212 111 LEDLEAA---IREVGADIFPPTGLISLENTHNSAggqvvslenlrEIAALAREHGIPVHLDGARFANAAVALGVIVKeiT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092787536 178 GVAAAVSFNGNKIMTTSGGGALLTDDEEMAARTR---YLATQARQ 219
Cdd:pfam01212 188 SYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRqrkYLGGGLRQ 232
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
34-160 |
1.63e-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: 52.59 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 34 PEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLgVGPGDLVPTSSLTFAATANAITYT----GAEPVFVDADEsgnm 109
Cdd:cd00614 40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYGGTYRLFERLlpklGIEVTFVDPDD---- 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1092787536 110 nPALLEQALTTlrreghEIKAV---VPVDLLGKTADHATIGRIAADHGAVVLSD 160
Cdd:cd00614 115 -PEALEAAIKP------ETKLVyveSPTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
10-162 |
3.44e-07 |
|
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: 51.57 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 10 PDVTQAEEDALVRAFRSNWIAPLGPEV--DALESELAEYTGRSHA--------VVLSSGTAALHLGLLNLgVGPGDLVPT 79
Cdd:cd00609 10 FPPPPEVLEALAAAALRAGLLGYYPDPglPELREAIAEWLGRRGGvdvppeeiVVTNGAQEALSLLLRAL-LNPGDEVLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 80 SSLTFAATANAITYTGAEPVFVDADESGNMNP--ALLEQALTtlrregHEIKAVV------PvdlLGKTADHAT---IGR 148
Cdd:cd00609 89 PDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLdlELLEAAKT------PKTKLLYlnnpnnP---TGAVLSEEEleeLAE 159
|
170
....*....|....
gi 1092787536 149 IAADHGAVVLSDAA 162
Cdd:cd00609 160 LAKKHGILIISDEA 173
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
29-184 |
9.14e-06 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 47.39 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 29 IAPLGPEVDALESELAE-----YTGRSHAVVLS-SGTAALHLGLLNLgVGPGD--LVPTS---SLTFAATANAItytGAE 97
Cdd:COG0075 24 IGHRDPEFVELMDEVREllkkvFGTENDVVILTgSGTGAMEAALANL-VSPGDkvLVLVNgafGERWAEIAERY---GAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 98 PVFVDADESGNMNPALLEQALttlrREGHEIKAVVPV----------DLlgktadhATIGRIAADHGAVVLSDAAESLGA 167
Cdd:COG0075 100 VVVLEVPWGEAVDPEEVEEAL----AADPDIKAVAVVhnetstgvlnPL-------EEIGALAKEHGALLIVDAVSSLGG 168
|
170 180
....*....|....*....|
gi 1092787536 168 TR---DgkqsaAYGVAAAVS 184
Cdd:COG0075 169 VPldmD-----EWGIDVVVS 183
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
48-199 |
9.66e-05 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 43.97 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 48 GRSHAVVLSSG-TAALHLGLLNLG-VGPGDLVPTSSLTFAAtaNAITY------TGAEPVFVDADESGNMNPALLEQALT 119
Cdd:COG0520 75 ASPDEIIFTRGtTEAINLVAYGLGrLKPGDEILITEMEHHS--NIVPWqelaerTGAEVRVIPLDEDGELDLEALEALLT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 120 tlrrEGHEIKAVVPV-DLLGKTADHATIGRIAADHGAVVLSDAAeslgatrdgkQSAAYG---VAA----AVSFNGNKIM 191
Cdd:COG0520 153 ----PRTKLVAVTHVsNVTGTVNPVKEIAALAHAHGALVLVDGA----------QSVPHLpvdVQAlgcdFYAFSGHKLY 218
|
....*...
gi 1092787536 192 TTSGGGAL 199
Cdd:COG0520 219 GPTGIGVL 226
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
9-167 |
1.29e-04 |
|
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: 43.70 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 9 SPDVTQAEEDAL----VRAFRSNWIAPLGPEVDALESELAEYTGRSHAVVLSSGTAAlHLGLLNLGVGPGDLVPTSSLTF 84
Cdd:cd06454 17 HPEVIEAAKEALdkygVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAA-NDGVLSTLAGKGDLIISDSLNH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 85 AATANAITYTGAEP-VFVDADesgnmnPALLEQALTTLRRegHEIKAVVPVD----LLGKTADHATIGRIAADHGAVVLS 159
Cdd:cd06454 96 ASIIDGIRLSGAKKrIFKHND------MEDLEKLLREARR--PYGKKLIVTEgvysMDGDIAPLPELVDLAKKYGAILFV 167
|
....*...
gi 1092787536 160 DAAESLGA 167
Cdd:cd06454 168 DEAHSVGV 175
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
53-166 |
2.57e-04 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 42.62 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 53 VVLSSGTAALHLGLLNLG--VGPGDLVPTSSL----TFAATANAITYTGAEPVFVDADESGNMNPALLEQALTtlrrEGH 126
Cdd:pfam00266 65 IFTSGTTEAINLVALSLGrsLKPGDEIVITEMehhaNLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT----PKT 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1092787536 127 EIKAVVPV-DLLGKTADHATIGRIAADHGAVVLSDAAESLG 166
Cdd:pfam00266 141 KLVAITHVsNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
34-218 |
3.84e-04 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 42.07 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 34 PEVDALESELAEYTGRSHAVVLSSGTAAlhlgllNLGV-----GPGDLVPTSSLTFAATANAITYTGAEpvFVDADESgn 108
Cdd:PRK05958 84 PAHEALEEELAEWFGAERALLFSSGYAA------NLAVltalaGKGDLIVSDKLNHASLIDGARLSRAR--VRRYPHN-- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 109 mNPALLEQALTTLRREgheiKAVVPVDLL----GKTADHATIGRIAADHGAVVLSDAAESLGATrdGKQSAayGVAAAVS 184
Cdd:PRK05958 154 -DVDALEALLAKWRAG----RALIVTESVfsmdGDLAPLAELVALARRHGAWLLVDEAHGTGVL--GPQGR--GLAAEAG 224
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092787536 185 FNG--NKIMTTSGG------GALLTDDEEMAartRYLATQAR 218
Cdd:PRK05958 225 LAGepDVILVGTLGkalgssGAAVLGSETLI---DYLINRAR 263
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
53-166 |
5.60e-04 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 41.68 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 53 VVLSSG-TAALHLGLLNLG--VGPGDLVPTSSLTFAAtaNAITY------TGAEPVFVDADESGNMNPALLEQALTtlrr 123
Cdd:cd06453 64 IIFTRNtTEAINLVAYGLGraNKPGDEIVTSVMEHHS--NIVPWqqlaerTGAKLKVVPVDDDGQLDLEALEKLLT---- 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1092787536 124 EGHEIKAVVPV-DLLGKTADHATIGRIAADHGAVVLSDAAESLG 166
Cdd:cd06453 138 ERTKLVAVTHVsNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAG 181
|
|
| PRK05613 |
PRK05613 |
O-acetylhomoserine/O-acetylserine sulfhydrylase; |
34-102 |
8.25e-04 |
|
O-acetylhomoserine/O-acetylserine sulfhydrylase;
Pssm-ID: 168128 [Multi-domain] Cd Length: 437 Bit Score: 41.40 E-value: 8.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092787536 34 PEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLGvGPGDLVPTSSLTFAATANAITYT----GAEPVFVD 102
Cdd:PRK05613 69 PTVEALENRIASLEGGVHAVAFASGQAAETAAILNLA-GAGDHIVTSPRLYGGTETLFLVTlnrlGIEVTFVE 140
|
|
| cysta_beta_ly_E |
TIGR01329 |
cystathionine beta-lyase, eukaryotic; This model represents cystathionine beta-lyase ... |
34-160 |
9.96e-04 |
|
cystathionine beta-lyase, eukaryotic; This model represents cystathionine beta-lyase (alternate name: beta-cystathionase), one of several pyridoxal-dependent enzymes of cysteine, methionine, and homocysteine metabolism. This enzyme is involved in the biosynthesis of Met from Cys.
Pssm-ID: 273557 [Multi-domain] Cd Length: 378 Bit Score: 40.97 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 34 PEVDALESELAEYTGRSHAVVLSSGTAALH--LGLLNlgvgPGDLVPTSSLTFAATANAITY----TGAEPVFVDADESG 107
Cdd:TIGR01329 47 PTRTALESLLAKLDKADRAFAFSSGMAALDviTRLLN----NGDEIIAGDDLYGGTDRLLTQvvprSGVVVVHVDTTDLD 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1092787536 108 NMNPALLEQALTTLRREgheikavvPVDLLGKTADHATIGRIAADHGAVVLSD 160
Cdd:TIGR01329 123 KVKAALGPKTKLVLLES--------PTNPLQKIVDIRKISEMAHAQNALVVVD 167
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
52-184 |
1.55e-03 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 40.35 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 52 AVVLSSGTAALHLGLLNLgVGPGDLVptssLTFAA------TANAITYTGAEPVFVDADESGNMNPALLEQALttlrrEG 125
Cdd:cd06451 53 FLLSGSGTGAMEAALSNL-LEPGDKV----LVGVNgvfgdrWADMAERYGADVDVVEKPWGEAVSPEEIAEAL-----EQ 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092787536 126 HEIKAVVPVDllGKTA-----DHATIGRIAADHGAVVLSDAAESLGATRdgKQSAAYGVAAAVS 184
Cdd:cd06451 123 HDIKAVTLTH--NETStgvlnPLEGIGALAKKHDALLIVDAVSSLGGEP--FRMDEWGVDVAYT 182
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
34-160 |
1.63e-03 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 40.03 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 34 PEVDALESELAEYTGRSHAVVLSSGTAALHLGLLNLgVGPGDLVPTSSLTFAATANAITYT----GAEPVFVDAdesgnM 109
Cdd:COG0626 58 PTRRALEEALAALEGGEAALAFASGMAAISAVLLAL-LKAGDHVVASDDLYGGTRRLLDKVlarfGIEVTFVDP-----T 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1092787536 110 NPALLEQALTtlrregHEIKAV---VPVDLLGKTADHATIGRIAADHGAVVLSD 160
Cdd:COG0626 132 DLAAVEAAIR------PNTKLVfleTPSNPTLEVVDIAAIAAIAHAAGALLVVD 179
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
34-158 |
4.07e-03 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 38.96 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 34 PEVDALESELAEYTGRSHA-VVLSSGTAALHLGLLNLGVGPGDLVPTSSLTFAATANAITYTGAEPVFVDADESGNMNPA 112
Cdd:COG0079 48 PDATALREALAEYYGVPPEqVLVGNGSDELIQLLARAFLGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPLDEDFSLDLD 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1092787536 113 LLEQALTtlrregHEIKAVV------PVdllGKTADHATIGRIAA---DHGAVVL 158
Cdd:COG0079 128 ALLAAIT------ERTDLVFlcnpnnPT---GTLLPREELEALLEalpADGLVVV 173
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
73-160 |
9.05e-03 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 37.80 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092787536 73 PGD--LVPTSSltFAATANAITYTGAEPVFVDADESGN--MNPALLEQALT--TlrregheiKAVV---PVDLLGKTADH 143
Cdd:PRK05764 114 PGDevIIPAPY--WVSYPEMVKLAGGVPVFVPTGEENGfkLTVEQLEAAITpkT--------KALIlnsPSNPTGAVYSP 183
|
90 100
....*....|....*....|
gi 1092787536 144 AT---IGRIAADHGAVVLSD 160
Cdd:PRK05764 184 EEleaIADVAVEHDIWVLSD 203
|
|
| |
