|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
2-428 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 610.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 2 QESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTRceIQGQGG 81
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 82 PFNTLvELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGG--FS 159
Cdd:PRK11860 82 QFPVK-QADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 160 GGNVTVDGSVSSQFLTALLMAAPL-APANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPGHY 238
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 239 LVEGDASSASYFLAAAAIKGGT-VKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISCTRGE--LNAIDMDMNHIPDA 315
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 316 AMTIATAALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQ---LQFADIGTYNDHRMAMCF 392
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 506220940 393 SLVAL--SDTPVTILDPKCTAKTFPDYFAQLARISHSA 428
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVAQAD 438
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
3-424 |
0e+00 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 595.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 3 ESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDrTRCEIQGQGGP 82
Cdd:COG0128 2 SSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 83 FNTlVELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEqENYPPLHLKGG-FSGG 161
Cdd:COG0128 81 LKE-PDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 162 NVTVDGSVSSQFLTALLMAAPLAPANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQsPGHYLVE 241
Cdd:COG0128 159 EYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 242 GDASSASYFLAAAAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISCTRGELNAIDMDMNHIPDAAMTIAT 321
Cdd:COG0128 238 GDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 322 AALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLQFADIGTYNDHRMAMCFSLVAL-SDT 400
Cdd:COG0128 318 LAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAEG 397
|
410 420
....*....|....*....|....
gi 506220940 401 PVTILDPKCTAKTFPDYFAQLARI 424
Cdd:COG0128 398 PVTIDDAECVAKSFPDFFELLESL 421
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
13-424 |
0e+00 |
|
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.
Pssm-ID: 238797 Cd Length: 409 Bit Score: 547.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 13 VDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSlsEDRTRCEIQGQGGPFNTlVELELF 92
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIE--EEGGTVEIVGGGGLGLP-PEAVLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 93 LGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGFSGGNVTVDGSVSSQ 172
Cdd:cd01556 78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 173 FLTALLMAAPLAPANTAIdIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPgHYLVEGDASSASYFLA 252
Cdd:cd01556 158 FKSALLLAAPLAEGPTTI-IIGELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 253 AAAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAQIVWGD-DFISCTR-GELNAIDMDMNHIPDAAMTIATAALFAQGTT 330
Cdd:cd01556 236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 331 TLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTP-PAQLQFADIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 408
Cdd:cd01556 314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
|
410
....*....|....*.
gi 506220940 409 CTAKTFPDYFAQLARI 424
Cdd:cd01556 394 CVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
15-424 |
1.41e-163 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273574 Cd Length: 409 Bit Score: 466.37 E-value: 1.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 15 GTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTrcEIQGQGGPFNtlvELELFLG 94
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGKEP---QAELDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 95 NAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGFSGGNVTVDGSVSSQFL 174
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 175 TALLMAAPLAPANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPGhYLVEGDASSASYFLAAA 254
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 255 AIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISCTRG-ELNAIDMDMNHIPDAAMTIATAALFAQGTTTLR 333
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 334 NIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLQFADIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 412
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 506220940 413 TFPDYFAQLARI 424
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
8-418 |
1.31e-159 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 456.37 E-value: 1.31e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 8 QPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGV-NYSLSEDRTRCEIQGQGGPFNTL 86
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 87 VELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGfSGGNVTVD 166
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 167 GSVSSQFLTALLMAAP-LAPANTAIDikgELVSKPYIDITLHLMKTFGVEVENQNY-QRFVIQGGQQyqSPGH-YLVEGD 243
Cdd:pfam00275 160 GDVSSQFVTSLLMLAAlLAEGTTTIE---NLASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGEK--LPGQeYRVEGD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 244 ASSASYFLAAAAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDF-ISCTRGELNAIDMDMNHIPDAAMTIATA 322
Cdd:pfam00275 235 RSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 323 ALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQ-LQFADIGTYNDHRMAMCFSLVAL-SDT 400
Cdd:pfam00275 315 AAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEG 394
|
410
....*....|....*...
gi 506220940 401 PVTILDPKCTAKTFPDYF 418
Cdd:pfam00275 395 ETIIDDIECTDRSFPDFE 412
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
2-428 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 610.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 2 QESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTRceIQGQGG 81
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 82 PFNTLvELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGG--FS 159
Cdd:PRK11860 82 QFPVK-QADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 160 GGNVTVDGSVSSQFLTALLMAAPL-APANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPGHY 238
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 239 LVEGDASSASYFLAAAAIKGGT-VKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISCTRGE--LNAIDMDMNHIPDA 315
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 316 AMTIATAALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQ---LQFADIGTYNDHRMAMCF 392
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 506220940 393 SLVAL--SDTPVTILDPKCTAKTFPDYFAQLARISHSA 428
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVAQAD 438
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
3-424 |
0e+00 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 595.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 3 ESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDrTRCEIQGQGGP 82
Cdd:COG0128 2 SSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 83 FNTlVELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEqENYPPLHLKGG-FSGG 161
Cdd:COG0128 81 LKE-PDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 162 NVTVDGSVSSQFLTALLMAAPLAPANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQsPGHYLVE 241
Cdd:COG0128 159 EYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 242 GDASSASYFLAAAAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISCTRGELNAIDMDMNHIPDAAMTIAT 321
Cdd:COG0128 238 GDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 322 AALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLQFADIGTYNDHRMAMCFSLVAL-SDT 400
Cdd:COG0128 318 LAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAEG 397
|
410 420
....*....|....*....|....
gi 506220940 401 PVTILDPKCTAKTFPDYFAQLARI 424
Cdd:COG0128 398 PVTIDDAECVAKSFPDFFELLESL 421
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-426 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 588.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 1 MQESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYslseDRTRCEIQGQG 80
Cdd:PRK02427 1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI----EDDEVVVEGVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 81 GPFNTLVELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYlEQENYPPLHLKGGFSG 160
Cdd:PRK02427 77 GGGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRGGKKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 161 GNVTVDGSVSSQFLTALLMAAPL-APANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQ---NYQRFVIQGGQQYQsPG 236
Cdd:PRK02427 156 GPIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVegwGYRRIVIKGGQRLR-GQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 237 HYLVEGDASSASYFLAAAAIKGG-TVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDF--------ISCTRGELNAIDM 307
Cdd:PRK02427 235 DITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEReggepvgdIRVRSSELKGIDI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 308 DMNHIPDAAMTIATAALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLqfADIGTYNDHR 387
Cdd:PRK02427 315 DIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 506220940 388 MAMCFSLVAL-SDTPVTILDPKCTAKTFPDYFAQLARISH 426
Cdd:PRK02427 393 IAMAFAIAGLaAEGPVTIDDPECVAKSFPDFFEDLASLGA 432
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
3-425 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 569.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 3 ESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTRCEIQGQGGP 82
Cdd:PLN02338 2 EEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 83 FNT----LVELELFLGNAGTAMRPLAAALCLGTNNV--VLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHL-- 154
Cdd:PLN02338 82 FPVsgdsKEDVELFLGNAGTAMRPLTAAVTAAGGNAsyVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVna 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 155 KGGFSGGNVTVDGSVSSQFLTALLMAAPLAPANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQN-YQRFVIQGGQQYQ 233
Cdd:PLN02338 162 AGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDsWDRFFIKGGQKYK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 234 SPGHYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISCTR--------GELNAI 305
Cdd:PLN02338 242 SPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGpprdafggKHLKAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 306 DMDMNHIPDAAMTIATAALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLQFADIGTYND 385
Cdd:PLN02338 322 DVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYDD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 506220940 386 HRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFAQLARIS 425
Cdd:PLN02338 402 HRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIA 441
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
13-424 |
0e+00 |
|
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.
Pssm-ID: 238797 Cd Length: 409 Bit Score: 547.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 13 VDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSlsEDRTRCEIQGQGGPFNTlVELELF 92
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIE--EEGGTVEIVGGGGLGLP-PEAVLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 93 LGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGFSGGNVTVDGSVSSQ 172
Cdd:cd01556 78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 173 FLTALLMAAPLAPANTAIdIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPgHYLVEGDASSASYFLA 252
Cdd:cd01556 158 FKSALLLAAPLAEGPTTI-IIGELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 253 AAAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAQIVWGD-DFISCTR-GELNAIDMDMNHIPDAAMTIATAALFAQGTT 330
Cdd:cd01556 236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 331 TLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTP-PAQLQFADIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 408
Cdd:cd01556 314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
|
410
....*....|....*.
gi 506220940 409 CTAKTFPDYFAQLARI 424
Cdd:cd01556 394 CVAKSFPNFFEDLESL 409
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
13-424 |
0e+00 |
|
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine enolpyruvyl transferase. Both enzymes catalyze the reaction of enolpyruvyl transfer.
Pssm-ID: 238795 Cd Length: 408 Bit Score: 526.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 13 VDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEdrTRCEIQGQGGPFNTLVELELF 92
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 93 LGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGFSGGNVTVDGSVSSQ 172
Cdd:cd01554 79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 173 FLTALLMAAPLAPANTAIDIKgelVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPgHYLVEGDASSASYFLA 252
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 253 AAAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAQIVWGDDFISCTRGELNAIDMDMNHIP---DAAMTIATAALFAQGT 329
Cdd:cd01554 235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 330 TTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLQFADIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 408
Cdd:cd01554 313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
|
410
....*....|....*.
gi 506220940 409 CTAKTFPDYFAQLARI 424
Cdd:cd01554 393 AINTSYPSFFDDLESL 408
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
15-424 |
1.41e-163 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273574 Cd Length: 409 Bit Score: 466.37 E-value: 1.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 15 GTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTrcEIQGQGGPFNtlvELELFLG 94
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGKEP---QAELDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 95 NAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGFSGGNVTVDGSVSSQFL 174
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 175 TALLMAAPLAPANTAIDIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPGhYLVEGDASSASYFLAAA 254
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 255 AIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISCTRG-ELNAIDMDMNHIPDAAMTIATAALFAQGTTTLR 333
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 334 NIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLQFADIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 412
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 506220940 413 TFPDYFAQLARI 424
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
8-418 |
1.31e-159 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 456.37 E-value: 1.31e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 8 QPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGV-NYSLSEDRTRCEIQGQGGPFNTL 86
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 87 VELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGfSGGNVTVD 166
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 167 GSVSSQFLTALLMAAP-LAPANTAIDikgELVSKPYIDITLHLMKTFGVEVENQNY-QRFVIQGGQQyqSPGH-YLVEGD 243
Cdd:pfam00275 160 GDVSSQFVTSLLMLAAlLAEGTTTIE---NLASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGEK--LPGQeYRVEGD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 244 ASSASYFLAAAAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDF-ISCTRGELNAIDMDMNHIPDAAMTIATA 322
Cdd:pfam00275 235 RSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 323 ALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQ-LQFADIGTYNDHRMAMCFSLVAL-SDT 400
Cdd:pfam00275 315 AAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEG 394
|
410
....*....|....*...
gi 506220940 401 PVTILDPKCTAKTFPDYF 418
Cdd:pfam00275 395 ETIIDDIECTDRSFPDFE 412
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
3-427 |
2.48e-154 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 452.24 E-value: 2.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 3 ESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNysLSEDRTRCEIQGQGGP 82
Cdd:PRK11861 241 EHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVK--LSRDGGTCVVGGTRGA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 83 FnTLVELELFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGADIIYLEQENYPPLHLKGGFSGGN 162
Cdd:PRK11861 319 F-TAKTADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISVD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 163 --VTVDGSVSSQFLTALLMAAPLAPAN---TAIDIKGELVSKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQSPGH 237
Cdd:PRK11861 398 apIRVRGDVSSQFLTALLMTLPLVKAKdgaSVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPGT 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 238 YLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAQIVWGDDFISC-----TRGELNAIDMDMNHI 312
Cdd:PRK11861 478 IMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVrgighDHGRLAPIDMDFNLI 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 313 PDAAMTIATAALFAQGTTTLRNIYNWRVKETDRLAAMATELRKVGATVEEGHDFITVTPPAQLQ-FADIGTYNDHRMAMC 391
Cdd:PRK11861 558 PDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTpNASIDTYDDHRMAMC 637
|
410 420 430
....*....|....*....|....*....|....*.
gi 506220940 392 FSLVALSDTPVTILDPKCTAKTFPDYFAQLARISHS 427
Cdd:PRK11861 638 FSLVSLGGVPVRINDPKCVGKTFPDYFDRFLALANA 673
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
241-424 |
5.42e-55 |
|
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.
Pssm-ID: 238794 Cd Length: 211 Bit Score: 181.32 E-value: 5.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 241 EGDASSASYFLAAAAIKGGTVKVTGIGRNSV-----QGDIRFADVLEKM-GAQIVWG---DDFISCTRGELNAIDMDMNH 311
Cdd:cd01553 7 KGGGQILRSFLVLAAISGGPITVTGIRPDRAkpgllRQHLTFLKALEKIcGATVEGGelgSDRISFRPGTVRGGDVRFAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 312 -----IPDAAMTIATAALFAQGTTTLRNIYNWRV----KETDRLAAMATELRKVGATVEEGHD------------FITVT 370
Cdd:cd01553 87 gsagsCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEVS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506220940 371 PPAQLQFADIgtyndhRMAMCFSLVAlsdTPVTILDPKCTAKTFPDYFAQLARI 424
Cdd:cd01553 167 PVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
1-423 |
1.62e-40 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 153.61 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 1 MQESLTLQPIARVDGTINLPGSKSVSNRALLLAALAKGTTTLTNLLDSDDVRHMLNALKALGVNYSlSEDRTRCEIQGQG 80
Cdd:PRK14806 300 NDVSYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIE-GPHNGRVTIHGVG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 81 --------GPfntlveleLFLGNAGTAMRPLAAALCLGTNNVVLTGEPRMKERPIGHLVDALRQGGAdIIYLEQENYPPL 152
Cdd:PRK14806 379 lhglkappGP--------LYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGA-VIETGEEGRPPL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 153 HLKGGFSGGNVTVDGSV-SSQFLTALLMAAPLAPANTAidikgelVSKPYI--DITLHLMKTFGVEVEnQNYQRFVIQGG 229
Cdd:PRK14806 450 SIRGGQRLKGIHYDLPMaSAQVKSCLLLAGLYAEGETS-------VTEPAPtrDHTERMLRGFGYPVK-VEGNTISVEGG 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 230 QQYQSpGHYLVEGDASSASYFLAAAAIKGGT-VKVTGIGRNSVQgdIRFADVLEKMGAQI-------VWGDDF--ISCTR 299
Cdd:PRK14806 522 GKLTA-TDIEVPADISSAAFFLVAASIAEGSeLTLEHVGINPTR--TGVIDILKLMGADItlenereVGGEPVadIRVRG 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 300 GELNAIDMDMNHIPDA-----AMTIATAalFAQGTTTLRNIYNWRVKETDRLAAMATELRKVG--ATVEEGHDFITVTPP 372
Cdd:PRK14806 599 ARLKGIDIPEDQVPLAidefpVLFVAAA--CAEGRTVLTGAEELRVKESDRIQVMADGLKTLGidCEPTPDGIIIEGGIF 676
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 506220940 373 AQlqfADIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAKTFPDyFAQLAR 423
Cdd:PRK14806 677 GG---GEVESHGDHRIAMSFSVASLrASGPITIHDCANVATSFPN-FLELAN 724
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
37-380 |
2.03e-11 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440529 Cd Length: 416 Bit Score: 65.39 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 37 KGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTrCEIQGqGGPFNTLVELELflgnaGTAMRplAAALCLGtnnvVL 116
Cdd:COG0766 36 DGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGT-LTIDA-SNINSTEAPYEL-----VRKMR--ASILVLG----PL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 117 TGepRMKE-------------RPIG-HLvDALRQGGADIIYlEQENYpplHLK-GGFSGGNVTVDG-SVssqflTA---L 177
Cdd:COG0766 103 LA--RFGEarvslpggcaigaRPIDlHL-KGLEALGAEIEI-EHGYI---EARaGRLKGARIYLDFpSV-----GAtenI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 178 LMAAPLApantaidiKGELV-----SKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYqSPGHYLVEGD---ASSasy 249
Cdd:COG0766 171 MMAAVLA--------EGTTVienaaREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKL-HGAEHTVIPDrieAGT--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 250 FLAAAAIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAQIVWGDDFISCTR-GELNAIDM----------DMNHIpdaAM 317
Cdd:COG0766 239 FLVAAAITGGDVTVKNV----IPEHLEaVLAKLREAGVEIEEGDDGIRVRGpGRLKAVDIktapypgfptDLQAQ---FM 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506220940 318 TIATaalFAQGTTTLR-NIYNWRVKETDrlaamatELRKVGATVE-EGHDfITVTPPAQLQFADI 380
Cdd:COG0766 312 ALLT---QAEGTSVITeTVFENRFMHVD-------ELNRMGADIKlDGHT-AIVRGVTKLSGAPV 365
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
37-380 |
1.33e-09 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.
Pssm-ID: 238796 Cd Length: 400 Bit Score: 59.41 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 37 KGTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTrCEIQGqggpfNTLVELELFLGNAGTaMRplAAALCLGtnnvVL 116
Cdd:cd01555 25 DEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENT-LVIDA-----SNINSTEAPYELVRK-MR--ASILVLG----PL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 117 TGepRMKE-------------RPIG-HLVdALRQGGADIIylEQENYPPLHLKGGFSGGNVTVD-GSVssqflTA---LL 178
Cdd:cd01555 92 LA--RFGEarvslpggcaigaRPVDlHLK-GLEALGAKIE--IEDGYVEAKAAGRLKGARIYLDfPSV-----GAtenIM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 179 MAAPLAP-----ANTAIDikgelvskPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYQsPGHYLVEGDASSASYFLAA 253
Cdd:cd01555 162 MAAVLAEgttviENAARE--------PEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLH-GAEHTVIPDRIEAGTFLVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 254 AAIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAQIVWGDDFISCTR--GELNAIDM----------DMNHIPDAAMTIa 320
Cdd:cd01555 233 AAITGGDITVENV----IPEHLEaVLAKLREMGAKIEIGEDGIRVDGdgGRLKAVDIetapypgfptDLQAQFMALLTQ- 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220940 321 taalfAQGTTTLR-NIYNWRVKETDrlaamatELRKVGA--TVEEGHdfITVTPPAQLQFADI 380
Cdd:cd01555 308 -----AEGTSVITeTIFENRFMHVD-------ELNRMGAdiKVEGNT--AIIRGVTKLSGAPV 356
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
38-380 |
1.57e-06 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 50.03 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 38 GTTTLTNLLDSDDVRHMLNALKALGVNYSLSEDRTrCEIQGQGgpfntLVELELFLGNAGTaMRplAAALCLGtnnvvlt 117
Cdd:PRK09369 37 EPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGT-VTIDASN-----INNTEAPYELVKK-MR--ASILVLG------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 118 geP---RMKE-------------RPIG-HLvDALRQGGADIIylEQENYPPLHLKGGFSGGNVTVDG-SVssqflTA--- 176
Cdd:PRK09369 101 --PllaRFGEakvslpggcaigaRPVDlHL-KGLEALGAEIE--IEHGYVEAKADGRLKGAHIVLDFpSV-----GAten 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 177 LLMAAPLApantaidiKGELV-----SKPYIDITLHLMKTFGVEVENQNYQRFVIQGGQQYqSPGHYLVEGDASSASYFL 251
Cdd:PRK09369 171 ILMAAVLA--------EGTTVienaaREPEIVDLANFLNKMGAKISGAGTDTITIEGVERL-HGAEHTVIPDRIEAGTFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 252 AAAAIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAQIVWGDDFISCTR-GELNAIDM----------DMNhipdaAMTI 319
Cdd:PRK09369 242 VAAAITGGDVTIRGA----RPEHLEaVLAKLREAGAEIEEGEDGIRVDMpGRLKAVDIktapypgfptDMQ-----AQFM 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506220940 320 ATAALfAQGTTTLR-NIYNWRVKETDrlaamatELRKVGATVE-EGHDfITVTPPAQLQFADI 380
Cdd:PRK09369 313 ALLTQ-AEGTSVITeTIFENRFMHVP-------ELIRMGADIEvDGHT-AVVRGVEKLSGAPV 366
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
278-382 |
4.26e-05 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440529 Cd Length: 416 Bit Score: 45.36 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 278 ADVLEKMGAQIVW-GDDFISCT-RGELNAIDMDMnhIPD--AAMTIATAALFAQGTTTLRNIynwrvkETDRLAAMATEL 353
Cdd:COG0766 196 ANFLNAMGAKIEGaGTDTITIEgVEKLHGAEHTV--IPDriEAGTFLVAAAITGGDVTVKNV------IPEHLEAVLAKL 267
|
90 100
....*....|....*....|....*....
gi 506220940 354 RKVGATVEEGHDFITVTPPAQLQFADIGT 382
Cdd:COG0766 268 REAGVEIEEGDDGIRVRGPGRLKAVDIKT 296
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
237-378 |
1.15e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 44.08 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 237 HYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSVQGdirFADVLEKMGAQIVWGDDFISCTR-GELNAIDMDMNHIP-- 313
Cdd:PRK12830 225 RHTVIPDRIEAGTYMILAAACGGGVTINNVIPEHLES---FIAKLEEMGVRVEVNEDSIFVEKqGNLKAVDIKTLPYPgf 301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506220940 314 --DAAMTIATAALFAQGTTTLR-NIYNWRVKETDrlaamatELRKVGATVEEGHDFITVTPPAQLQFA 378
Cdd:PRK12830 302 atDLQQPLTPLLLKANGRSVVTdTIYEKRFKHVD-------ELKRMGANIKVEGRSAIITGPSKLTGA 362
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
161-370 |
3.02e-04 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.
Pssm-ID: 238796 Cd Length: 400 Bit Score: 42.85 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 161 GNVTVDGSVSSqfLTALLMAAPLAPANTAI----DIKGelvskpyIDITLHLMKTFGVEVENQNYQRFVIQ--GGQQYQS 234
Cdd:cd01555 3 GEVRISGAKNA--ALPILAAALLTDEPVTLrnvpDLLD-------VETMIELLRSLGAKVEFEGENTLVIDasNINSTEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 235 PGHYlvegdASS--ASYFLAAAAI-KGGTVKVTG-----IGRNSVQGDIRfadVLEKMGAQIVWGDDFISCTR-GEL--N 303
Cdd:cd01555 74 PYEL-----VRKmrASILVLGPLLaRFGEARVSLpggcaIGARPVDLHLK---GLEALGAKIEIEDGYVEAKAaGRLkgA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 304 AIDMDMnhiPD--AAMTIATAALFAQGTTTLRNIYnwRVKETDRLAAMateLRKVGATVE-EGHDFITVT 370
Cdd:cd01555 146 RIYLDF---PSvgATENIMMAAVLAEGTTVIENAA--REPEIVDLANF---LNKMGAKIEgAGTDTIRIE 207
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
279-383 |
4.89e-04 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440529 Cd Length: 416 Bit Score: 42.28 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 279 DVLEKMGAQIVWGDDFISCTRGEL--NAIDMDMnhiPD--AAMTIATAALFAQGTTTLRNIYnwrvKE---TDrLAAMat 351
Cdd:COG0766 129 KGLEALGAEIEIEHGYIEARAGRLkgARIYLDF---PSvgATENIMMAAVLAEGTTVIENAA----REpeiVD-LANF-- 198
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 506220940 352 eLRKVGATVE-EGHDFITVTPPAQLQFAD---------IGTY 383
Cdd:COG0766 199 -LNAMGAKIEgAGTDTITIEGVEKLHGAEhtvipdrieAGTF 239
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
278-382 |
1.86e-03 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 40.40 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506220940 278 ADVLEKMGAQI-VWGDDFISCTrG--ELNAIDmdmnH--IPD---AAmTIATAALFAQGTTTLRNIynwrvkETDRLAAM 349
Cdd:PRK09369 197 ANFLNKMGAKIsGAGTDTITIE-GveRLHGAE----HtvIPDrieAG-TFLVAAAITGGDVTIRGA------RPEHLEAV 264
|
90 100 110
....*....|....*....|....*....|...
gi 506220940 350 ATELRKVGATVEEGHDFITVTPPAQLQFADIGT 382
Cdd:PRK09369 265 LAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKT 297
|
|
| |
