|
Name |
Accession |
Description |
Interval |
E-value |
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-423 |
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: 607.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDrTRCEVTGNGG 80
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 81 ALRsGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128 80 GLK-EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 GHVEVDGSVSSQFLTALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQsPGNYLV 239
Cdd:COG0128 158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGELNAIDMDMNHIPDAAMTIA 319
Cdd:COG0128 237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128 317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
|
410 420
....*....|....*....|....*
gi 695731700 399 TPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:COG0128 397 GPVTIDDAECVAKSFPDFFELLESL 421
|
|
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
1-424 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 606.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTRceVTGNGG 80
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 81 ALrSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860 82 QF-PVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 159 GGHVEVDGSVSSQFLTALLMTAPL-APQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGNY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGE--LNAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK---LQFAEIGTYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*
gi 695731700 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVA 435
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-423 |
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: 551.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRtrCEVTGNGGALRSGEElELF 91
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGT--VEIVGGGGLGLPPEA-VLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 92 LGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQ 171
Cdd:cd01556 78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 172 FLTALLMTAPLAPQDTVITIkGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPgNYLVEGDASSASYFLA 251
Cdd:cd01556 158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 252 AGAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAIVTWGD-DFISCTH-GELNAIDMDMNHIPDAAMTIATAALFAKGTT 329
Cdd:cd01556 236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 330 TLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTP-PAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01556 314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
|
410
....*....|....*.
gi 695731700 408 CTAKTFPDYFEQLARI 423
Cdd:cd01556 394 CVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-423 |
2.99e-165 |
|
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: 470.22 E-value: 2.99e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 14 GTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrcEVTGNGGALRSGEeleLFLG 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGKEPQAE---LDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 94 NAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQFL 173
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 174 TALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGnYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 254 AIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHG-ELNAIDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 333 NIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 695731700 412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-420 |
6.46e-164 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 467.16 E-value: 6.46e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 7 QPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGV-HYTLSDDRTRCEVTGNGGALRSG 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 86 EELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGfTGGHVEVD 165
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 166 GSVSSQFLTALLMTAPLAPQDTVITIkgELVSKPYIDITLHLMKTFGVEVENQ-SYQRFVVRGAQQYQSpGNYLVEGDAS 244
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIE--NLASEPYIDDTENMLKKFGAKIEGSgTELSITVKGGEKLPG-QEYRVEGDRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 245 SASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDF-ISCTHGELNAIDMDMNHIPDAAMTIATAAL 323
Cdd:pfam00275 237 SAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 324 FAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK-LQFAEIGTYNDHRMAMCFSLVAL-SDTPV 401
Cdd:pfam00275 317 FAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGET 396
|
410
....*....|....*....
gi 695731700 402 TILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 397 IIDDIECTDRSFPDFEEKL 415
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-423 |
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: 607.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDrTRCEVTGNGG 80
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 81 ALRsGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128 80 GLK-EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 GHVEVDGSVSSQFLTALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQsPGNYLV 239
Cdd:COG0128 158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGELNAIDMDMNHIPDAAMTIA 319
Cdd:COG0128 237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128 317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
|
410 420
....*....|....*....|....*
gi 695731700 399 TPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:COG0128 397 GPVTIDDAECVAKSFPDFFELLESL 421
|
|
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
1-424 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 606.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTRceVTGNGG 80
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 81 ALrSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860 82 QF-PVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 159 GGHVEVDGSVSSQFLTALLMTAPL-APQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGNY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGE--LNAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK---LQFAEIGTYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*
gi 695731700 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVA 435
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-424 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 590.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYtlsdDRTRCEVTGNGG 80
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI----EDDEVVVEGVGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 81 ALRSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYlEQENYPPLRLRGGFTGG 160
Cdd:PRK02427 78 GGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRGGKKGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 161 HVEVDGSVSSQFLTALLMTAPL-APQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQ---SYQRFVVRGAQQYQsPGN 236
Cdd:PRK02427 157 PIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVegwGYRRIVIKGGQRLR-GQD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 237 YLVEGDASSASYFLAAGAIKGG-TVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDF--------ISCTHGELNAIDMD 307
Cdd:PRK02427 236 ITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEReggepvgdIRVRSSELKGIDID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 308 MNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLqfAEIGTYNDHRM 387
Cdd:PRK02427 316 IPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHRI 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 695731700 388 AMCFSLVAL-SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK02427 394 AMAFAIAGLaAEGPVTIDDPECVAKSFPDFFEDLASLG 431
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
1-425 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 570.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTRCEVTGNGG 80
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 81 ALRSG----EELELFLGNAGTAMRPLAAALCLGSNN--IVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRL- 153
Cdd:PLN02338 81 KFPVSgdskEDVELFLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVn 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 154 -RGGFTGGHVEVDGSVSSQFLTALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQ-SYQRFVVRGAQQY 231
Cdd:PLN02338 161 aAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSdSWDRFFIKGGQKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 232 QSPGNYLVEGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCT--------HGELNA 303
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTgpprdafgGKHLKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 304 IDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYN 383
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYD 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 695731700 384 DHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARIST 425
Cdd:PLN02338 401 DHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAK 442
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-423 |
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: 551.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRtrCEVTGNGGALRSGEElELF 91
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGT--VEIVGGGGLGLPPEA-VLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 92 LGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQ 171
Cdd:cd01556 78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 172 FLTALLMTAPLAPQDTVITIkGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPgNYLVEGDASSASYFLA 251
Cdd:cd01556 158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 252 AGAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAIVTWGD-DFISCTH-GELNAIDMDMNHIPDAAMTIATAALFAKGTT 329
Cdd:cd01556 236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 330 TLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTP-PAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01556 314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
|
410
....*....|....*.
gi 695731700 408 CTAKTFPDYFEQLARI 423
Cdd:cd01556 394 CVAKSFPNFFEDLESL 409
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-423 |
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: 544.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDdrTRCEVTGNGGALRSGEELELF 91
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 92 LGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQ 171
Cdd:cd01554 79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 172 FLTALLMTAPLAPQDTVITIKgelVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPgNYLVEGDASSASYFLA 251
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 252 AGAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAIVTWGDDFISCTHGELNAIDMDMNHIP---DAAMTIATAALFAKGT 328
Cdd:cd01554 235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554 313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
|
410
....*....|....*.
gi 695731700 408 CTAKTFPDYFEQLARI 423
Cdd:cd01554 393 AINTSYPSFFDDLESL 408
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-423 |
2.99e-165 |
|
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: 470.22 E-value: 2.99e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 14 GTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrcEVTGNGGALRSGEeleLFLG 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGKEPQAE---LDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 94 NAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQFL 173
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 174 TALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGnYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 254 AIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHG-ELNAIDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 333 NIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 695731700 412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-420 |
6.46e-164 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 467.16 E-value: 6.46e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 7 QPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGV-HYTLSDDRTRCEVTGNGGALRSG 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 86 EELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGfTGGHVEVD 165
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 166 GSVSSQFLTALLMTAPLAPQDTVITIkgELVSKPYIDITLHLMKTFGVEVENQ-SYQRFVVRGAQQYQSpGNYLVEGDAS 244
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIE--NLASEPYIDDTENMLKKFGAKIEGSgTELSITVKGGEKLPG-QEYRVEGDRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 245 SASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDF-ISCTHGELNAIDMDMNHIPDAAMTIATAAL 323
Cdd:pfam00275 237 SAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 324 FAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK-LQFAEIGTYNDHRMAMCFSLVAL-SDTPV 401
Cdd:pfam00275 317 FAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGET 396
|
410
....*....|....*....
gi 695731700 402 TILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 397 IIDDIECTDRSFPDFEEKL 415
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-420 |
4.62e-159 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 464.18 E-value: 4.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVhyTLSDDRTRCEVTGNGG 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGV--KLSRDGGTCVVGGTRG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 81 ALrSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTG- 159
Cdd:PRK11861 318 AF-TAKTADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISv 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 -GHVEVDGSVSSQFLTALLMTAPLAPQD---TVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPG 235
Cdd:PRK11861 397 dAPIRVRGDVSSQFLTALLMTLPLVKAKdgaSVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPG 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 236 NYLVEGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISC-----THGELNAIDMDMNH 310
Cdd:PRK11861 477 TIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVrgighDHGRLAPIDMDFNL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 311 IPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQ-FAEIGTYNDHRMAM 389
Cdd:PRK11861 557 IPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTpNASIDTYDDHRMAM 636
|
410 420 430
....*....|....*....|....*....|.
gi 695731700 390 CFSLVALSDTPVTILDPKCTAKTFPDYFEQL 420
Cdd:PRK11861 637 CFSLVSLGGVPVRINDPKCVGKTFPDYFDRF 667
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
240-423 |
1.80e-57 |
|
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: 187.87 E-value: 1.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSV-----QGDIRFADVLEKM-GAIVTWG---DDFISCTHGELNAIDMDMNH 310
Cdd:cd01553 7 KGGGQILRSFLVLAAISGGPITVTGIRPDRAkpgllRQHLTFLKALEKIcGATVEGGelgSDRISFRPGTVRGGDVRFAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 311 -----IPDAAMTIATAALFAKGTTTLRNIYNWRV----KETDRLFAMATELRKVGAEVEEGED------------YIRVT 369
Cdd:cd01553 87 gsagsCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEVS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695731700 370 PPAKLQFAEIgtyndhRMAMCFSLVAlsdTPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:cd01553 167 PVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
3-422 |
1.82e-39 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 150.53 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 3 SLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVhytLSDDRTRCEVTGNGGAL 82
Cdd:PRK14806 303 SYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGV---VIEGPHNGRVTIHGVGL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 83 R--SGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEyLEQENYPPLRLRGGFTGG 160
Cdd:PRK14806 380 HglKAPPGPLYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIE-TGEEGRPPLSIRGGQRLK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 161 HVEVDGSV-SSQFLTALLMTAPLAPQDTVITikgELvsKPYIDITLHLMKTFGVEVENQSyQRFVVRGAQQYQSpGNYLV 239
Cdd:PRK14806 459 GIHYDLPMaSAQVKSCLLLAGLYAEGETSVT---EP--APTRDHTERMLRGFGYPVKVEG-NTISVEGGGKLTA-TDIEV 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGT-VKVTGIGRNSVQgdIRFADVLEKMGAIVTW-----------GDdfISCTHGELNAIDMD 307
Cdd:PRK14806 532 PADISSAAFFLVAASIAEGSeLTLEHVGINPTR--TGVIDILKLMGADITLenerevggepvAD--IRVRGARLKGIDIP 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 308 MNHIPDA-----AMTIATAalFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTppAKLQFA-EIGT 381
Cdd:PRK14806 608 EDQVPLAidefpVLFVAAA--CAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIE--GGIFGGgEVES 683
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 695731700 382 YNDHRMAMCFSLVAL-SDTPVTILDPKCTAKTFPDyFEQLAR 422
Cdd:PRK14806 684 HGDHRIAMSFSVASLrASGPITIHDCANVATSFPN-FLELAN 724
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
36-379 |
3.25e-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: 64.62 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 36 NGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrceVTGNGGALRSGE---ELelflgnaGTAMRplAAALCLGSnn 112
Cdd:COG0766 36 DGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGT---LTIDASNINSTEapyEL-------VRKMR--ASILVLGP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 113 ivLTGepRMKE-------------RPIG-HLvDALRQGGAQIEYlEQENYpplRLR-GGFTGGHVEVDG-SVssqflTA- 175
Cdd:COG0766 102 --LLA--RFGEarvslpggcaigaRPIDlHL-KGLEALGAEIEI-EHGYI---EARaGRLKGARIYLDFpSV-----GAt 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 176 --LLMTAPLAPQDTVItikgELVSK-PYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYqSPGNYLVEGD---ASSasyF 249
Cdd:COG0766 168 enIMMAAVLAEGTTVI----ENAARePEIVDLANFLNAMGAKIEGAGTDTITIEGVEKL-HGAEHTVIPDrieAGT---F 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 250 LAAGAIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAIVTWGDDFISCT-HGELNAIDM----------DMNHIpdaAMT 317
Cdd:COG0766 240 LVAAAITGGDVTVKNV----IPEHLEaVLAKLREAGVEIEEGDDGIRVRgPGRLKAVDIktapypgfptDLQAQ---FMA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695731700 318 IATaalFAKGTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGeDYIRVTPPAKLQFAEI 379
Cdd:COG0766 313 LLT---QAEGTSVITeTVFENR-------FMHVDELNRMGADIKlDG-HTAIVRGVTKLSGAPV 365
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
36-379 |
8.78e-08 |
|
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: 54.02 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 36 NGTTVLTNLLDSDDVRHMLNALKALGVHYtlsddrtrcEVTGNGGAL---RSGEELELFLGNAGTaMRplAAALCLGsnn 112
Cdd:cd01555 25 DEPVTLRNVPDLLDVETMIELLRSLGAKV---------EFEGENTLVidaSNINSTEAPYELVRK-MR--ASILVLG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 113 iVLTGepRMKE-------------RPIG-HLVdALRQGGAQIEylEQENYPPLRLRGGFTGGHVEVD-GSVssqflTA-- 175
Cdd:cd01555 90 -PLLA--RFGEarvslpggcaigaRPVDlHLK-GLEALGAKIE--IEDGYVEAKAAGRLKGARIYLDfPSV-----GAte 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 176 -LLMTAPLAPQDTVItikgELVSK-PYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQsPGNYLVEGDASSASYFLAAG 253
Cdd:cd01555 159 nIMMAAVLAEGTTVI----ENAARePEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLH-GAEHTVIPDRIEAGTFLVAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 254 AIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAIVTWGDDFISCTH--GELNAIDMDMNHIP----DAAMTIATAALFAK 326
Cdd:cd01555 234 AITGGDITVENV----IPEHLEaVLAKLREMGAKIEIGEDGIRVDGdgGRLKAVDIETAPYPgfptDLQAQFMALLTQAE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 695731700 327 GTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGEDYIrVTPPAKLQFAEI 379
Cdd:cd01555 310 GTSVITeTIFENR-------FMHVDELNRMGADIKvEGNTAI-IRGVTKLSGAPV 356
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
36-360 |
1.29e-05 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 46.95 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 36 NGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrceVTGNGGALRSGE---ELelflgnAGTaMRplAAALCLGsnn 112
Cdd:PRK09369 36 EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGT---VTIDASNINNTEapyEL------VKK-MR--ASILVLG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 113 ivltgeP---RMKE-------------RPIG-HLvDALRQGGAQIEylEQENYPPLRLRGGFTGGHVEVDG-SVssqflT 174
Cdd:PRK09369 101 ------PllaRFGEakvslpggcaigaRPVDlHL-KGLEALGAEIE--IEHGYVEAKADGRLKGAHIVLDFpSV-----G 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 175 A---LLMTAPLAPQDTVItikgELVSK-PYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYqSPGNYLVEGDASSASYFL 250
Cdd:PRK09369 167 AtenILMAAVLAEGTTVI----ENAARePEIVDLANFLNKMGAKISGAGTDTITIEGVERL-HGAEHTVIPDRIEAGTFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 251 AAGAIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAIVTWGDDFISCT-HGELNAIDM----------DMNhipdaAMTI 318
Cdd:PRK09369 242 VAAAITGGDVTIRGA----RPEHLEaVLAKLREAGAEIEEGEDGIRVDmPGRLKAVDIktapypgfptDMQ-----AQFM 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 695731700 319 ATAALfAKGTTTlrniynwrVKET---DRLFaMATELRKVGAEVE 360
Cdd:PRK09369 313 ALLTQ-AEGTSV--------ITETifeNRFM-HVPELIRMGADIE 347
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
246-379 |
3.47e-05 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 45.62 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 246 ASYFLAAGAIKGGTVKVTGIGRNSVQGdirFADVLEKMGAIVTWGDDFIS-CTHGELNAIDMDMNHIP----DAAMTIAT 320
Cdd:PRK12830 235 AGTYMILAAACGGGVTINNVIPEHLES---FIAKLEEMGVRVEVNEDSIFvEKQGNLKAVDIKTLPYPgfatDLQQPLTP 311
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 321 AALFAKGTTTLR-NIYNWRVKETDrlfamatELRKVGAEVEEGEDYIRVTPPAKLQFAEI 379
Cdd:PRK12830 312 LLLKANGRSVVTdTIYEKRFKHVD-------ELKRMGANIKVEGRSAIITGPSKLTGAKV 364
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
277-375 |
2.67e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 43.10 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 277 ADVLEKMGAIVT-WGDDFI---------SCTHgelnAIdmdmnhIPD---AAmTIATAALFAKGTTTLRNIynwrvkETD 343
Cdd:PRK09369 197 ANFLNKMGAKISgAGTDTItiegverlhGAEH----TV------IPDrieAG-TFLVAAAITGGDVTIRGA------RPE 259
|
90 100 110
....*....|....*....|....*....|..
gi 695731700 344 RLFAMATELRKVGAEVEEGEDYIRVTPPAKLQ 375
Cdd:PRK09369 260 HLEAVLAKLREAGAEIEEGEDGIRVDMPGRLK 291
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
278-382 |
1.16e-03 |
|
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: 41.12 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 278 DVLEKMGAIVTWGDDFISCTHGEL--NAIDMDMnhiPD--AAMTIATAALFAKGTTTLRNIYnwrvKE---TDrlfaMAT 350
Cdd:COG0766 129 KGLEALGAEIEIEHGYIEARAGRLkgARIYLDF---PSvgATENIMMAAVLAEGTTVIENAA----REpeiVD----LAN 197
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 695731700 351 ELRKVGAEVE-EGEDYIRVTPPAKLQFA---------EIGTY 382
Cdd:COG0766 198 FLNAMGAKIEgAGTDTITIEGVEKLHGAehtvipdriEAGTF 239
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
160-378 |
2.69e-03 |
|
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: 39.76 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 GHVEVDGSVSSqfLTALLMTAPLAPQDTVIT----IKGelvskpyIDITLHLMKTFGVEVENQSYQRFVV--RGAQQYQS 233
Cdd:cd01555 3 GEVRISGAKNA--ALPILAAALLTDEPVTLRnvpdLLD-------VETMIELLRSLGAKVEFEGENTLVIdaSNINSTEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 234 PGNYlvegdASS--ASyFLAAGAI--KGGTVKVTG-----IGRNSVQGDIRfadVLEKMGAIVTWGDDFISCTH-GEL-- 301
Cdd:cd01555 74 PYEL-----VRKmrAS-ILVLGPLlaRFGEARVSLpggcaIGARPVDLHLK---GLEALGAKIEIEDGYVEAKAaGRLkg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 302 NAIDMDMnhiPD--AAMTIATAALFAKGTTTLRNIYnwrvKE---TDrlfaMATELRKVGAEVE-EGEDYIRVTPPAKLQ 375
Cdd:cd01555 145 ARIYLDF---PSvgATENIMMAAVLAEGTTVIENAA----REpeiVD----LANFLNKMGAKIEgAGTDTIRIEGVERLH 213
|
...
gi 695731700 376 FAE 378
Cdd:cd01555 214 GAE 216
|
|
|