|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
1-426 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 601.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRceIIGNGG 80
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 81 PLHAESArELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGG--FT 158
Cdd:PRK11860 82 QFPVKQA-DLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 159 GGNVDVDGSVSSQFLTALLMTAPL-APEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 238 LVEGDASSASYFLAAAAIRGGT-VKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGE--LNAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEK---LKFAEIATYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 446367389 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARISQP 426
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVAQA 437
|
|
| 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: 600.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSaDRTRCEIIGNGG 80
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEEL-DGGTLRVTGVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 81 PLHAESArELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEqENYPPLRLQGG-FTG 159
Cdd:COG0128 80 GLKEPDA-VLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 160 GNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQsPGTYLV 239
Cdd:COG0128 158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 240 EGDASSASYFLAAAAIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIA 319
Cdd:COG0128 237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLKFAEIATYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128 317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
|
410 420
....*....|....*....|....*
gi 446367389 399 TPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:COG0128 397 GPVTIDDAECVAKSFPDFFELLESL 421
|
|
| 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: 596.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 12 VDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSAdrTRCEIIGNGGPLHAESARELF 91
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 92 LGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQ 171
Cdd:cd01554 79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 172 FLTALLMTAPLAPEDTVIRIKgdlVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPgTYLVEGDASSASYFLA 251
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 252 AAAIRGGTVKVTGIGRNSmqGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIP---DAAMTIATAALFAKGT 328
Cdd:cd01554 235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLKFAEIATYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554 313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
|
410
....*....|....*.
gi 446367389 408 CTAKTFPDYFEQLARI 423
Cdd:cd01554 393 AINTSYPSFFDDLESL 408
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-420 |
3.55e-162 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 462.92 E-value: 3.55e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 7 QPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVS-YTLSADRTRCEIIGNGGPLHAE 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEiIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 86 SARELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGfTGGNVDVD 165
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 166 GSVSSQFLTALLMTAPLAPEDTVIrIKGdLVSKPYIDITLNLMKTFGVEIENQHY-QQFVVKGGQsyQSPGT-YLVEGDA 243
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTT-IEN-LASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGE--KLPGQeYRVEGDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 244 SSASYFLAAAAIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDY-ISCTRGELNAIDMDMNHIPDAAMTIATAA 322
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 323 LFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEK-LKFAEIATYNDHRMAMCFSLVAL-SDTP 400
Cdd:pfam00275 316 AFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGE 395
|
410 420
....*....|....*....|
gi 446367389 401 VTILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 396 TIIDDIECTDRSFPDFEEKL 415
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-423 |
3.00e-160 |
|
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: 457.51 E-value: 3.00e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 14 GTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTrcEIIGNGGplhAESARELFLG 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGG---KEPQAELDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 94 NAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFL 173
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 174 TALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGtYLVEGDASSASYFLAAA 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 254 AIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRG-ELNAIDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 333 NIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLKFAEIATYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 446367389 412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
1-426 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 601.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRceIIGNGG 80
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 81 PLHAESArELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGG--FT 158
Cdd:PRK11860 82 QFPVKQA-DLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 159 GGNVDVDGSVSSQFLTALLMTAPL-APEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 238 LVEGDASSASYFLAAAAIRGGT-VKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGE--LNAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEK---LKFAEIATYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 446367389 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARISQP 426
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVAQA 437
|
|
| 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: 600.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSaDRTRCEIIGNGG 80
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEEL-DGGTLRVTGVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 81 PLHAESArELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEqENYPPLRLQGG-FTG 159
Cdd:COG0128 80 GLKEPDA-VLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 160 GNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQsPGTYLV 239
Cdd:COG0128 158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 240 EGDASSASYFLAAAAIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIA 319
Cdd:COG0128 237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLKFAEIATYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128 317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
|
410 420
....*....|....*....|....*
gi 446367389 399 TPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:COG0128 397 GPVTIDDAECVAKSFPDFFELLESL 421
|
|
| 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: 596.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 12 VDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSAdrTRCEIIGNGGPLHAESARELF 91
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 92 LGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQ 171
Cdd:cd01554 79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 172 FLTALLMTAPLAPEDTVIRIKgdlVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPgTYLVEGDASSASYFLA 251
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 252 AAAIRGGTVKVTGIGRNSmqGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIP---DAAMTIATAALFAKGT 328
Cdd:cd01554 235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLKFAEIATYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554 313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
|
410
....*....|....*.
gi 446367389 408 CTAKTFPDYFEQLARI 423
Cdd:cd01554 393 AINTSYPSFFDDLESL 408
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-425 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 585.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYtlsaDRTRCEIIGNGG 80
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI----EDDEVVVEGVGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 81 PLHAESARELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYlEQENYPPLRLQGGFTGG 160
Cdd:PRK02427 78 GGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRGGKKGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 161 NVDVDGSVSSQFLTALLMTAPL-APEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQ---HYQQFVVKGGQSYQsPGT 236
Cdd:PRK02427 157 PIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVegwGYRRIVIKGGQRLR-GQD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 237 YLVEGDASSASYFLAAAAIRGG-TVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDY--------ISCTRGELNAIDMD 307
Cdd:PRK02427 236 ITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEReggepvgdIRVRSSELKGIDID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 308 MNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLkfAEIATYNDHRM 387
Cdd:PRK02427 316 IPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHRI 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 446367389 388 AMCFSLVAL-SDTPVTILDPKCTAKTFPDYFEQLARISQ 425
Cdd:PRK02427 394 AMAFAIAGLaAEGPVTIDDPECVAKSFPDFFEDLASLGA 432
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
1-425 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 561.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGG 80
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 81 PL----HAESARELFLGNAGTAMRPLAAALCL--GSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQ 154
Cdd:PLN02338 81 KFpvsgDSKEDVELFLGNAGTAMRPLTAAVTAagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 155 --GGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQH-YQQFVVKGGQSY 231
Cdd:PLN02338 161 aaGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDsWDRFFIKGGQKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 232 QSPGTYLVEGDASSASYFLAAAAIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTR--------GELNA 303
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGpprdafggKHLKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 304 IDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLKFAEIATYN 383
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYD 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446367389 384 DHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISQ 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: 544.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 12 VDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRtrCEIIGNGGPLHAESArELF 91
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGT--VEIVGGGGLGLPPEA-VLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 92 LGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQ 171
Cdd:cd01556 78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 172 FLTALLMTAPLAPEDTVIRIkGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPgTYLVEGDASSASYFLA 251
Cdd:cd01556 158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 252 AAAIRGGTVKVTGIGRNSmqGDIRFADVLEKMGATICWGD-DYISCTR-GELNAIDMDMNHIPDAAMTIATAALFAKGTT 329
Cdd:cd01556 236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 330 TLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPE-KLKFAEIATYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01556 314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPlKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
|
410
....*....|....*.
gi 446367389 408 CTAKTFPDYFEQLARI 423
Cdd:cd01556 394 CVAKSFPNFFEDLESL 409
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-420 |
3.55e-162 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 462.92 E-value: 3.55e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 7 QPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVS-YTLSADRTRCEIIGNGGPLHAE 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEiIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 86 SARELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGfTGGNVDVD 165
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 166 GSVSSQFLTALLMTAPLAPEDTVIrIKGdLVSKPYIDITLNLMKTFGVEIENQHY-QQFVVKGGQsyQSPGT-YLVEGDA 243
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTT-IEN-LASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGE--KLPGQeYRVEGDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 244 SSASYFLAAAAIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDY-ISCTRGELNAIDMDMNHIPDAAMTIATAA 322
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 323 LFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEK-LKFAEIATYNDHRMAMCFSLVAL-SDTP 400
Cdd:pfam00275 316 AFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGE 395
|
410 420
....*....|....*....|
gi 446367389 401 VTILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 396 TIIDDIECTDRSFPDFEEKL 415
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-423 |
3.00e-160 |
|
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: 457.51 E-value: 3.00e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 14 GTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTrcEIIGNGGplhAESARELFLG 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGG---KEPQAELDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 94 NAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFL 173
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 174 TALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGtYLVEGDASSASYFLAAA 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 254 AIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRG-ELNAIDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 333 NIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLKFAEIATYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 446367389 412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-420 |
3.45e-154 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 451.85 E-value: 3.45e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSytLSADRTRCEIIGNGG 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVK--LSRDGGTCVVGGTRG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 81 PLHAESArELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITYLEQENYPPLRLQGGFTGG 160
Cdd:PRK11861 318 AFTAKTA-DLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 161 N--VDVDGSVSSQFLTALLMTAPLAPED---TVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPG 235
Cdd:PRK11861 397 DapIRVRGDVSSQFLTALLMTLPLVKAKdgaSVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPG 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 236 TYLVEGDASSASYFLAAAAIRGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISC-----TRGELNAIDMDMNH 310
Cdd:PRK11861 477 TIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVrgighDHGRLAPIDMDFNL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 311 IPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEKLK-FAEIATYNDHRMAM 389
Cdd:PRK11861 557 IPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTpNASIDTYDDHRMAM 636
|
410 420 430
....*....|....*....|....*....|.
gi 446367389 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 |
6.14e-63 |
|
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: 202.12 E-value: 6.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 240 EGDASSASYFLAAAAIRGGTVKVTGIGRNSM-----QGDIRFADVLEKM-GATICWG---DDYISCTRGELNAIDMDMNH 310
Cdd:cd01553 7 KGGGQILRSFLVLAAISGGPITVTGIRPDRAkpgllRQHLTFLKALEKIcGATVEGGelgSDRISFRPGTVRGGDVRFAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 311 -----IPDAAMTIATAALFAKGTTTLRNIYNWRV----KETDRLFAMATELRKVGAEVEEGHD------------FIRIT 369
Cdd:cd01553 87 gsagsCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEVS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446367389 370 PPEKLKFAEIatyndhRMAMCFSLVAlsdTPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:cd01553 167 PVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
3-422 |
8.01e-40 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 151.69 E-value: 8.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 3 SLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYT-LSADRTRCEIIGNGGp 81
Cdd:PRK14806 303 SYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEgPHNGRVTIHGVGLHG- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 82 LHAESArELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKITyLEQENYPPLRLQGGFTGGN 161
Cdd:PRK14806 382 LKAPPG-PLYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIE-TGEEGRPPLSIRGGQRLKG 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 162 VDVDGSV-SSQFLTALLMTAPLAP-EDTVIRikgdlvSKPYIDITLNLMKTFGVEIEnQHYQQFVVKGGQSYQspGTYL- 238
Cdd:PRK14806 460 IHYDLPMaSAQVKSCLLLAGLYAEgETSVTE------PAPTRDHTERMLRGFGYPVK-VEGNTISVEGGGKLT--ATDIe 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 239 VEGDASSASYFLAAAAIRGGT-VKVTGIGRNSMQgdIRFADVLEKMGATICW-----------GDdyISCTRGELNAIDM 306
Cdd:PRK14806 531 VPADISSAAFFLVAASIAEGSeLTLEHVGINPTR--TGVIDILKLMGADITLenerevggepvAD--IRVRGARLKGIDI 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 307 DMNHIPDA-----AMTIATAalFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPEkLKFAEIAT 381
Cdd:PRK14806 607 PEDQVPLAidefpVLFVAAA--CAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGGI-FGGGEVES 683
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446367389 382 YNDHRMAMCFSLVAL-SDTPVTILDPKCTAKTFPDyFEQLAR 422
Cdd:PRK14806 684 HGDHRIAMSFSVASLrASGPITIHDCANVATSFPN-FLELAN 724
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
37-379 |
1.07e-12 |
|
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: 69.24 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 37 GKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTrCEIIGnGGPLHAESARELflgnaGTAMRplAAALCLGSndivLT 116
Cdd:COG0766 37 GPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGT-LTIDA-SNINSTEAPYEL-----VRKMR--ASILVLGP----LL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 117 GepRMKE-------------RPIG-HLvDALRQGGAKITYlEQENYpplRLQ-GGFTGGNVDVDG-SVssqflTA---LL 177
Cdd:COG0766 104 A--RFGEarvslpggcaigaRPIDlHL-KGLEALGAEIEI-EHGYI---EARaGRLKGARIYLDFpSV-----GAtenIM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 178 MTAPLAPEDTVIR-------IkGDLvskpyIDItLNLMktfGVEIENQHYQQFVVKGGQSYqSPGTYLVEGD---ASSas 247
Cdd:COG0766 172 MAAVLAEGTTVIEnaarepeI-VDL-----ANF-LNAM---GAKIEGAGTDTITIEGVEKL-HGAEHTVIPDrieAGT-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 248 yFLAAAAIRGGTVKVTGIGRNSMQGdirFADVLEKMGATICWGDDYISCTR-GELNAIDM----------DMNHIpdaAM 316
Cdd:COG0766 239 -FLVAAAITGGDVTVKNVIPEHLEA---VLAKLREAGVEIEEGDDGIRVRGpGRLKAVDIktapypgfptDLQAQ---FM 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446367389 317 TIATaalFAKGTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGHDfIRITPPEKLKFAEI 379
Cdd:COG0766 312 ALLT---QAEGTSVITeTVFENR-------FMHVDELNRMGADIKlDGHT-AIVRGVTKLSGAPV 365
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
37-405 |
1.25e-11 |
|
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: 65.96 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 37 GKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTrCEIIgnggPLHAESaRELFLGNAGTaMRplAAALCLGsndiVLT 116
Cdd:cd01555 26 EPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENT-LVID----ASNINS-TEAPYELVRK-MR--ASILVLG----PLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 117 GepRMKE-------------RPIG-HLVdALRQGGAKITylEQENYPPLRLQGGFTGGNVDVD-GSVssqflTA---LLM 178
Cdd:cd01555 93 A--RFGEarvslpggcaigaRPVDlHLK-GLEALGAKIE--IEDGYVEAKAAGRLKGARIYLDfPSV-----GAtenIMM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 179 TAPLAPEDTVIRikgDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQsPGTYLVEGDASSASYFLAAAAIRGG 258
Cdd:cd01555 163 AAVLAEGTTVIE---NAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLH-GAEHTVIPDRIEAGTFLVAAAITGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 259 TVKVTGIGRNSMqgdIRFADVLEKMGATICWGDDYISCTR--GELNAIDM----------DMNHIPDAAMTIataalfAK 326
Cdd:cd01555 239 DITVENVIPEHL---EAVLAKLREMGAKIEIGEDGIRVDGdgGRLKAVDIetapypgfptDLQAQFMALLTQ------AE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 327 GTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGHDFIrITPPEKLKFAEI-ATynDHRMAMCFSLVALSDTPVTI 403
Cdd:cd01555 310 GTSVITeTIFENR-------FMHVDELNRMGADIKvEGNTAI-IRGVTKLSGAPVmAT--DLRAGAALVLAGLAAEGETI 379
|
..
gi 446367389 404 LD 405
Cdd:cd01555 380 IS 381
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
37-379 |
1.07e-07 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 53.50 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 37 GKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRceIIGNGGPLHAESARELflgnAGTaMRplAAALCLGsndivlt 116
Cdd:PRK09369 37 EPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTV--TIDASNINNTEAPYEL----VKK-MR--ASILVLG------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 117 geP---RMKE-------------RPIG-HLvDALRQGGAKITylEQENYPPLRLQGGFTGGNVDVDG-SVssqflTA--- 175
Cdd:PRK09369 101 --PllaRFGEakvslpggcaigaRPVDlHL-KGLEALGAEIE--IEHGYVEAKADGRLKGAHIVLDFpSV-----GAten 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 176 LLMTAPLAPEDTVIRikgDLVSKPYI-DIT--LNLMktfGVEIENQHYQQFVVKGGQSYqSPGTYLVEGDASSASYFLAA 252
Cdd:PRK09369 171 ILMAAVLAEGTTVIE---NAAREPEIvDLAnfLNKM---GAKISGAGTDTITIEGVERL-HGAEHTVIPDRIEAGTFLVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 253 AAIRGGTVKVTGIGRNSMQGdirFADVLEKMGATICWGDDYISCTR-GELNAIDM----------DMNhipdaAMTIATA 321
Cdd:PRK09369 244 AAITGGDVTIRGARPEHLEA---VLAKLREAGAEIEEGEDGIRVDMpGRLKAVDIktapypgfptDMQ-----AQFMALL 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446367389 322 ALfAKGTTTlrniynwrVKET---DRLFaMATELRKVGAEVE-EGHDFIrITPPEKLKFAEI 379
Cdd:PRK09369 316 TQ-AEGTSV--------ITETifeNRFM-HVPELIRMGADIEvDGHTAV-VRGVEKLSGAPV 366
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
160-378 |
8.45e-07 |
|
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: 50.94 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 160 GNVDVDGSVSSqfLTALLMTAPLAPEDTVIRIKGDLVSkpyIDITLNLMKTFGVEIENQHYQQFVV--KGGQSYQSPGTY 237
Cdd:cd01555 3 GEVRISGAKNA--ALPILAAALLTDEPVTLRNVPDLLD---VETMIELLRSLGAKVEFEGENTLVIdaSNINSTEAPYEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 238 lvegdASS--ASYFLAAAAI-RGGTVKVTG-----IGRnsmqgdiRFAD----VLEKMGATICWGDDYISCTR-GEL--N 302
Cdd:cd01555 78 -----VRKmrASILVLGPLLaRFGEARVSLpggcaIGA-------RPVDlhlkGLEALGAKIEIEDGYVEAKAaGRLkgA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 303 AIDMDMnhiPD--AAMTIATAALFAKGTTTLRNIYnwrvKE---TDrlfaMATELRKVGAEVE-EGHDFIRITPPEKLKF 376
Cdd:cd01555 146 RIYLDF---PSvgATENIMMAAVLAEGTTVIENAA----REpeiVD----LANFLNKMGAKIEgAGTDTIRIEGVERLHG 214
|
..
gi 446367389 377 AE 378
Cdd:cd01555 215 AE 216
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
277-381 |
1.70e-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: 46.90 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 277 ADVLEKMGATICW-GDDYISCT-RGELNAIDMDMnhIPD--AAMTIATAALFAKGTTTLRNIynwrvkETDRLFAMATEL 352
Cdd:COG0766 196 ANFLNAMGAKIEGaGTDTITIEgVEKLHGAEHTV--IPDriEAGTFLVAAAITGGDVTVKNV------IPEHLEAVLAKL 267
|
90 100
....*....|....*....|....*....
gi 446367389 353 RKVGAEVEEGHDFIRITPPEKLKFAEIAT 381
Cdd:COG0766 268 REAGVEIEEGDDGIRVRGPGRLKAVDIKT 296
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
247-379 |
3.40e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 42.53 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 247 SYFLAAAAIrGGTVKVTGIGRNSMQGdirFADVLEKMGATICWGDDYISCTR-GELNAIDMDMNHIP----DAAMTIATA 321
Cdd:PRK12830 237 TYMILAAAC-GGGVTINNVIPEHLES---FIAKLEEMGVRVEVNEDSIFVEKqGNLKAVDIKTLPYPgfatDLQQPLTPL 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446367389 322 ALFAKGTTTLR-NIYNWRVKETDrlfamatELRKVGAEVEEGHDFIRITPPEKLKFAEI 379
Cdd:PRK12830 313 LLKANGRSVVTdTIYEKRFKHVD-------ELKRMGANIKVEGRSAIITGPSKLTGAKV 364
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
277-381 |
2.27e-03 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 40.01 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367389 277 ADVLEKMGATI-CWGDDYIScTRG--ELNAIDmdmnH--IPD---AAmTIATAALFAKGTTTLRNIynwrvkETDRLFAM 348
Cdd:PRK09369 197 ANFLNKMGAKIsGAGTDTIT-IEGveRLHGAE----HtvIPDrieAG-TFLVAAAITGGDVTIRGA------RPEHLEAV 264
|
90 100 110
....*....|....*....|....*....|...
gi 446367389 349 ATELRKVGAEVEEGHDFIRITPPEKLKFAEIAT 381
Cdd:PRK09369 265 LAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKT 297
|
|
| |
