|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
1-427 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 597.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 1 MESLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTRcdITGNGG 80
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGAlELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860 82 QFPVKQA-DLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 159 GGDIEVDGSVSSQFLTALLMTAPL-APEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPGRY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIACTRGE--LHAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 315 AMTIATTALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAK---LHHADIGTYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 446367334 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARMSTPA 427
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVAQAD 438
|
|
| 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: 592.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 1 MESLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSaDRTRCDITGNGG 80
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEEL-DGGTLRVTGVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGAlELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128 80 GLKEPDA-VLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 160 GDIEVDGSVSSQFLTALLMTAPLAPEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHsPGRYLV 239
Cdd:COG0128 158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 240 EGDASSASYFLAAGAIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIACTRGELHAIDMDMNHIPDAAMTIA 319
Cdd:COG0128 237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 320 TTALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGTYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128 317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
|
410 420
....*....|....*....|....*
gi 446367334 399 TPVTILDPKCTAKTFPDYFEQLARM 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: 546.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 12 VDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSAdrTRCDITGNGGALRAPGALELF 91
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 92 LGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGFTGGDIEVDGSVSSQ 171
Cdd:cd01554 79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 172 FLTALLMTAPLAPEDTTIRVKgelVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPgRYLVEGDASSASYFLA 251
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 252 AGAIKGGTVKVTGIGRKSmqGDIRFADVLEKMGATITWGDDFIACTRGELHAIDMDMNHIP---DAAMTIATTALFAKGT 328
Cdd:cd01554 235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554 313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
|
410
....*....|....*.
gi 446367334 408 CTAKTFPDYFEQLARM 423
Cdd:cd01554 393 AINTSYPSFFDDLESL 408
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-420 |
2.29e-162 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 463.31 E-value: 2.29e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 7 QPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGI-NYTLSADRTRCDITGNGGALRAP 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 86 GALELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGfTGGDIEVD 165
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 166 GSVSSQFLTALLMTAPLAPEDTTIRVkgELVSKPYIDITLNLMKTFGVEITNHHY-QQFVVKGGQQYHSpGRYLVEGDAS 244
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIE--NLASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGEKLPG-QEYRVEGDRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 245 SASYFLAAGAIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDF-IACTRGELHAIDMDMNHIPDAAMTIATTAL 323
Cdd:pfam00275 237 SAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 324 FAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAK-LHHADIGTYNDHRMAMCFSLVAL-SDTPV 401
Cdd:pfam00275 317 FAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGET 396
|
410
....*....|....*....
gi 446367334 402 TILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 397 IIDDIECTDRSFPDFEEKL 415
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-423 |
5.06e-159 |
|
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: 454.43 E-value: 5.06e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 14 GAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTRcdITGNGGALraPGAlELFLG 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAV--IEGVGGKE--PQA-ELDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 94 NAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGFTGGDIEVDGSVSSQFL 173
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 174 TALLMTAPLAPEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPGrYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 254 AIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIACTRG-ELHAIDMDMNHIPDAAMTIATTALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 333 NIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 446367334 412 TFPDYFEQLARM 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
1-427 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 597.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 1 MESLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTRcdITGNGG 80
Cdd:PRK11860 4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGAlELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860 82 QFPVKQA-DLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 159 GGDIEVDGSVSSQFLTALLMTAPL-APEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPGRY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIACTRGE--LHAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 315 AMTIATTALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAK---LHHADIGTYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 446367334 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARMSTPA 427
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVAQAD 438
|
|
| 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: 592.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 1 MESLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSaDRTRCDITGNGG 80
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEEL-DGGTLRVTGVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGAlELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128 80 GLKEPDA-VLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 160 GDIEVDGSVSSQFLTALLMTAPLAPEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHsPGRYLV 239
Cdd:COG0128 158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 240 EGDASSASYFLAAGAIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIACTRGELHAIDMDMNHIPDAAMTIA 319
Cdd:COG0128 237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 320 TTALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGTYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128 317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
|
410 420
....*....|....*....|....*
gi 446367334 399 TPVTILDPKCTAKTFPDYFEQLARM 423
Cdd:COG0128 397 GPVTIDDAECVAKSFPDFFELLESL 421
|
|
| 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: 575.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 1 MESLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYtlsaDRTRCDITGNGG 80
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI----EDDEVVVEGVGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGALELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYlEQENYPPLRLRGGFTGG 160
Cdd:PRK02427 78 GGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRGGKKGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 161 DIEVDGSVSSQFLTALLMTAPL-APEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNH---HYQQFVVKGGQQYHsPGR 236
Cdd:PRK02427 157 PIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVegwGYRRIVIKGGQRLR-GQD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 237 YLVEGDASSASYFLAAGAIKGG-TVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDF--------IACTRGELHAIDMD 307
Cdd:PRK02427 236 ITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEReggepvgdIRVRSSELKGIDID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 308 MNHIPDAAMTIATTALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKlhHADIGTYNDHRM 387
Cdd:PRK02427 316 IPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPL--AGVVDSYGDHRI 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 446367334 388 AMCFSLVAL-SDTPVTILDPKCTAKTFPDYFEQLARMS 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: 550.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 1 MESLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTRCDITGNGG 80
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGA----LELFLGNAGTAMRPLAAALCL--GQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRL- 153
Cdd:PLN02338 81 KFPVSGDskedVELFLGNAGTAMRPLTAAVTAagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVn 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 154 -RGGFTGGDIEVDGSVSSQFLTALLMTAPLAPEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNHH-YQQFVVKGGQQY 231
Cdd:PLN02338 161 aAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDsWDRFFIKGGQKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 232 HSPGRYLVEGDASSASYFLAAGAIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIACTR--------GELHA 303
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGpprdafggKHLKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 304 IDMDMNHIPDAAMTIATTALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGTYN 383
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYD 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446367334 384 DHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARMST 425
Cdd:PLN02338 401 DHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAK 442
|
|
| 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: 546.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 12 VDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSAdrTRCDITGNGGALRAPGALELF 91
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 92 LGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGFTGGDIEVDGSVSSQ 171
Cdd:cd01554 79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 172 FLTALLMTAPLAPEDTTIRVKgelVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPgRYLVEGDASSASYFLA 251
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 252 AGAIKGGTVKVTGIGRKSmqGDIRFADVLEKMGATITWGDDFIACTRGELHAIDMDMNHIP---DAAMTIATTALFAKGT 328
Cdd:cd01554 235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554 313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
|
410
....*....|....*.
gi 446367334 408 CTAKTFPDYFEQLARM 423
Cdd:cd01554 393 AINTSYPSFFDDLESL 408
|
|
| 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: 532.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 12 VDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSADRtrCDITGNGGALRAPGAlELF 91
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGT--VEIVGGGGLGLPPEA-VLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 92 LGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGFTGGDIEVDGSVSSQ 171
Cdd:cd01556 78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 172 FLTALLMTAPLAPEDTTIRVkGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPgRYLVEGDASSASYFLA 251
Cdd:cd01556 158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 252 AGAIKGGTVKVTGIGRKSmqGDIRFADVLEKMGATITWGD-DFIACTR-GELHAIDMDMNHIPDAAMTIATTALFAKGTT 329
Cdd:cd01556 236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 330 TLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITP-PAKLHHADIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01556 314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
|
410
....*....|....*.
gi 446367334 408 CTAKTFPDYFEQLARM 423
Cdd:cd01556 394 CVAKSFPNFFEDLESL 409
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-420 |
2.29e-162 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 463.31 E-value: 2.29e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 7 QPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGI-NYTLSADRTRCDITGNGGALRAP 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 86 GALELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGfTGGDIEVD 165
Cdd:pfam00275 81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 166 GSVSSQFLTALLMTAPLAPEDTTIRVkgELVSKPYIDITLNLMKTFGVEITNHHY-QQFVVKGGQQYHSpGRYLVEGDAS 244
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIE--NLASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGEKLPG-QEYRVEGDRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 245 SASYFLAAGAIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDF-IACTRGELHAIDMDMNHIPDAAMTIATTAL 323
Cdd:pfam00275 237 SAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 324 FAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAK-LHHADIGTYNDHRMAMCFSLVAL-SDTPV 401
Cdd:pfam00275 317 FAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGET 396
|
410
....*....|....*....
gi 446367334 402 TILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 397 IIDDIECTDRSFPDFEEKL 415
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-423 |
5.06e-159 |
|
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: 454.43 E-value: 5.06e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 14 GAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTRcdITGNGGALraPGAlELFLG 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAV--IEGVGGKE--PQA-ELDLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 94 NAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGFTGGDIEVDGSVSSQFL 173
Cdd:TIGR01356 76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 174 TALLMTAPLAPEDTTIRVKGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPGrYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 254 AIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIACTRG-ELHAIDMDMNHIPDAAMTIATTALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 333 NIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
|
410
....*....|..
gi 446367334 412 TFPDYFEQLARM 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-424 |
1.92e-154 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 452.62 E-value: 1.92e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 1 MESLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINytLSADRTRCDITGNGG 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVK--LSRDGGTCVVGGTRG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGAlELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDYLEQENYPPLRLRGGFTGG 160
Cdd:PRK11861 318 AFTAKTA-DLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 161 D--IEVDGSVSSQFLTALLMTAPLAPED---TTIRVKGELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHSPG 235
Cdd:PRK11861 397 DapIRVRGDVSSQFLTALLMTLPLVKAKdgaSVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPG 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 236 RYLVEGDASSASYFLAAGAIKGGTVKVTGIGRKSMQGDIRFADVLEKMGATITWGDDFIAC-----TRGELHAIDMDMNH 310
Cdd:PRK11861 477 TIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVrgighDHGRLAPIDMDFNL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 311 IPDAAMTIATTALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLH-HADIGTYNDHRMAM 389
Cdd:PRK11861 557 IPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTpNASIDTYDDHRMAM 636
|
410 420 430
....*....|....*....|....*....|....*
gi 446367334 390 CFSLVALSDTPVTILDPKCTAKTFPDYFEQLARMS 424
Cdd:PRK11861 637 CFSLVSLGGVPVRINDPKCVGKTFPDYFDRFLALA 671
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
240-423 |
1.67e-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: 182.86 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 240 EGDASSASYFLAAGAIKGGTVKVTGIGRKSM-----QGDIRFADVLEKM-GATITWG---DDFIACTRGELHAIDMDMNH 310
Cdd:cd01553 7 KGGGQILRSFLVLAAISGGPITVTGIRPDRAkpgllRQHLTFLKALEKIcGATVEGGelgSDRISFRPGTVRGGDVRFAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 311 -----IPDAAMTIATTALFAKGTTTLRNIYNWRV----KETDRLFAMATELRKVGAEVEEGHD------------YIRIT 369
Cdd:cd01553 87 gsagsCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEVS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446367334 370 PPAKLHHADIgtyndhRMAMCFSLVAlsdTPVTILDPKCTAKTFPDYFEQLARM 423
Cdd:cd01553 167 PVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
3-422 |
2.02e-36 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 141.67 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 3 SLTLQPIARVDGAINLPGSKSVSNRALLLAALACGKTVLTNLLDSDDVRHMLNALSALGINYT-LSADRTRcdITGNG-G 80
Cdd:PRK14806 303 SYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEgPHNGRVT--IHGVGlH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 81 ALRAPGAlELFLGNAGTAMRPLAAALCLGQNEIVLTGEPRMKERPIGHLVDSLRQGGANIDyLEQENYPPLRLRGGFTGG 160
Cdd:PRK14806 381 GLKAPPG-PLYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIE-TGEEGRPPLSIRGGQRLK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 161 DIEVDGSV-SSQFLTALLMTAPLAPEDTTIRvkgELvsKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQyhSPGRYLV 239
Cdd:PRK14806 459 GIHYDLPMaSAQVKSCLLLAGLYAEGETSVT---EP--APTRDHTERMLRGFGYPVKVEGNTISVEGGGKL--TATDIEV 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 240 EGDASSASYFLAAGAIKGG---TVKVTGIGRKSmqgdIRFADVLEKMGATIT------WGDDFIACTR---GELHAIDMD 307
Cdd:PRK14806 532 PADISSAAFFLVAASIAEGselTLEHVGINPTR----TGVIDILKLMGADITlenereVGGEPVADIRvrgARLKGIDIP 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 308 MNHIPDA-----AMTIAttALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITpPAKLHHADIGTY 382
Cdd:PRK14806 608 EDQVPLAidefpVLFVA--AACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIE-GGIFGGGEVESH 684
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446367334 383 NDHRMAMCFSLVAL-SDTPVTILDPKCTAKTFPDyFEQLAR 422
Cdd:PRK14806 685 GDHRIAMSFSVASLrASGPITIHDCANVATSFPN-FLELAN 724
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
37-379 |
4.62e-13 |
|
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: 70.40 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 37 GKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTrcdITGNGGALR---APGALelflgnaGTAMRplAAALCLGqnei 113
Cdd:COG0766 37 GPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGT---LTIDASNINsteAPYEL-------VRKMR--ASILVLG---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 114 VLTGepRMKE-------------RPIG-HLvDSLRQGGANIDYlEQENYpplRLR-GGFTGGDIEVDG-SVssqflTA-- 175
Cdd:COG0766 101 PLLA--RFGEarvslpggcaigaRPIDlHL-KGLEALGAEIEI-EHGYI---EARaGRLKGARIYLDFpSV-----GAte 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 176 -LLMTAPLAPEDTTIrvkgELVSK-PYID--IT-LNLMktfGVEI----TNHhyqqFVVKGGQQYHsPGRYLVEGD---A 243
Cdd:COG0766 169 nIMMAAVLAEGTTVI----ENAARePEIVdlANfLNAM---GAKIegagTDT----ITIEGVEKLH-GAEHTVIPDrieA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 244 SSasyFLAAGAIKGGTVKVTGIGRKSMQGdirFADVLEKMGATITWGDDFIACTR-GELHAIDM----------DMNHIp 312
Cdd:COG0766 237 GT---FLVAAAITGGDVTVKNVIPEHLEA---VLAKLREAGVEIEEGDDGIRVRGpGRLKAVDIktapypgfptDLQAQ- 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446367334 313 daAMTIATTalfAKGTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGHdYIRITPPAKLHHADI 379
Cdd:COG0766 310 --FMALLTQ---AEGTSVITeTVFENR-------FMHVDELNRMGADIKlDGH-TAIVRGVTKLSGAPV 365
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
37-379 |
1.73e-10 |
|
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: 62.49 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 37 GKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTRCDITGNGGALRAPGALE-------LFLGnagtamrPLAAAlcLG 109
Cdd:cd01555 26 EPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINSTEAPYELVrkmrasiLVLG-------PLLAR--FG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 110 QNEIVLTGEPRMKERPIG-HLVdSLRQGGANIDylEQENYPPLRLRGGFTGGDIEVD-GSVssqflTA---LLMTAPLAP 184
Cdd:cd01555 97 EARVSLPGGCAIGARPVDlHLK-GLEALGAKIE--IEDGYVEAKAAGRLKGARIYLDfPSV-----GAtenIMMAAVLAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 185 EDTTIRvkgELVSKPYIDITLNLMKTFGVEITNHHYQQFVVKGGQQYHsPGRYLVEGDASSASYFLAAGAIKGGTVKVTG 264
Cdd:cd01555 169 GTTVIE---NAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLH-GAEHTVIPDRIEAGTFLVAAAITGGDITVEN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 265 IGRKSMqgdIRFADVLEKMGATITWGDDFIACTR--GELHAIDMDMNHIP----DAAMTIATTALFAKGTTTLR-NIYNW 337
Cdd:cd01555 245 VIPEHL---EAVLAKLREMGAKIEIGEDGIRVDGdgGRLKAVDIETAPYPgfptDLQAQFMALLTQAEGTSVITeTIFEN 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446367334 338 RvketdrlFAMATELRKVGA--EVEEGHdyIRITPPAKLHHADI 379
Cdd:cd01555 322 R-------FMHVDELNRMGAdiKVEGNT--AIIRGVTKLSGAPV 356
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
37-379 |
2.45e-06 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 49.26 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 37 GKTVLTNLLDSDDVRHMLNALSALGINYTLSADRTrCDITGNG-----------GALRAPgalELFLGnagtamrPLAAA 105
Cdd:PRK09369 37 EPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGT-VTIDASNinnteapyelvKKMRAS---ILVLG-------PLLAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 106 LclGQNEIVLTGEPRMKERPIG-HLvDSLRQGGANIDylEQENYPPLRLRGGFTGGDIEVDG-SVssqflTA---LLMTA 180
Cdd:PRK09369 106 F--GEAKVSLPGGCAIGARPVDlHL-KGLEALGAEIE--IEHGYVEAKADGRLKGAHIVLDFpSV-----GAtenILMAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 181 PLAPEDTTIR-VKGElvskPYI-DIT--LNLMktfGVEITNHHYQQFVVKGGQQYHsPGRYLVEGDASSASYFLAAGAIK 256
Cdd:PRK09369 176 VLAEGTTVIEnAARE----PEIvDLAnfLNKM---GAKISGAGTDTITIEGVERLH-GAEHTVIPDRIEAGTFLVAAAIT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 257 GGTVKVTGIGRKSMQGdirFADVLEKMGATITWGDDFIACTR-GELHAIDM----------DMNHIpdaAMTIATTalfA 325
Cdd:PRK09369 248 GGDVTIRGARPEHLEA---VLAKLREAGAEIEEGEDGIRVDMpGRLKAVDIktapypgfptDMQAQ---FMALLTQ---A 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446367334 326 KGTTTlrniynwrVKET---DRLFaMATELRKVGAEVE-EGHDYIrITPPAKLHHADI 379
Cdd:PRK09369 319 EGTSV--------ITETifeNRFM-HVPELIRMGADIEvDGHTAV-VRGVEKLSGAPV 366
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
160-375 |
1.67e-05 |
|
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: 46.70 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 160 GDIEVDGSVSSqfLTALLMTAPLAPEDTTIRVKGELVSkpyIDITLNLMKTFGVEITNHHYQQFVV--KGGQQYHSPGRY 237
Cdd:cd01555 3 GEVRISGAKNA--ALPILAAALLTDEPVTLRNVPDLLD---VETMIELLRSLGAKVEFEGENTLVIdaSNINSTEAPYEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 238 lvegdASS--ASyFLAAGAI--KGGTVKVTG-----IGRKSMQGDIRfadVLEKMGATITWGDDFI-ACTRGELHA--ID 305
Cdd:cd01555 78 -----VRKmrAS-ILVLGPLlaRFGEARVSLpggcaIGARPVDLHLK---GLEALGAKIEIEDGYVeAKAAGRLKGarIY 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446367334 306 MDMnhiPD--AAMTIATTALFAKGTTTLRNIYnwrvKE---TDrlfaMATELRKVGAEVE-EGHDYIRITPPAKLH 375
Cdd:cd01555 149 LDF---PSvgATENIMMAAVLAEGTTVIENAA----REpeiVD----LANFLNKMGAKIEgAGTDTIRIEGVERLH 213
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
277-381 |
1.83e-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: 46.52 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 277 ADVLEKMGATITW-GDDFIACT-RGELHAIDMDMnhIPD--AAMTIATTALFAKGTTTLRNIynwrvkETDRLFAMATEL 352
Cdd:COG0766 196 ANFLNAMGAKIEGaGTDTITIEgVEKLHGAEHTV--IPDriEAGTFLVAAAITGGDVTVKNV------IPEHLEAVLAKL 267
|
90 100
....*....|....*....|....*....
gi 446367334 353 RKVGAEVEEGHDYIRITPPAKLHHADIGT 381
Cdd:COG0766 268 REAGVEIEEGDDGIRVRGPGRLKAVDIKT 296
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
278-382 |
3.79e-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: 45.75 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 278 DVLEKMGATITWGDDFIACTRGELHA--IDMDM-------NhipdaAMTIATtalFAKGTTTLRNIynwrvketdrlfam 348
Cdd:COG0766 129 KGLEALGAEIEIEHGYIEARAGRLKGarIYLDFpsvgateN-----IMMAAV---LAEGTTVIENA-------------- 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446367334 349 ATE---------LRKVGAEVE-EGHDYIRITPPAKLHHAD---------IGTY 382
Cdd:COG0766 187 AREpeivdlanfLNAMGAKIEgAGTDTITIEGVEKLHGAEhtvipdrieAGTF 239
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
236-377 |
1.01e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 44.46 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 236 RYLVEGDASSASYFLAAGAIKGGTVKVTGIGRKSMQGdirFADVLEKMGATITWGDDFI-ACTRGELHAIDMDMNHIP-- 312
Cdd:PRK12830 225 RHTVIPDRIEAGTYMILAAACGGGVTINNVIPEHLES---FIAKLEEMGVRVEVNEDSIfVEKQGNLKAVDIKTLPYPgf 301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446367334 313 --DAAMTIATTALFAKGTTTLR-NIYNWRVKETDrlfamatELRKVGAEVEEGHDYIRITPPAKLHHA 377
Cdd:PRK12830 302 atDLQQPLTPLLLKANGRSVVTdTIYEKRFKHVD-------ELKRMGANIKVEGRSAIITGPSKLTGA 362
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
277-381 |
2.54e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 43.10 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367334 277 ADVLEKMGATIT-WGDDFI---------ACTrgelHAIdmdmnhIPD----------AAMTiattalfaKGTTTLRNIyn 336
Cdd:PRK09369 197 ANFLNKMGAKISgAGTDTItiegverlhGAE----HTV------IPDrieagtflvaAAIT--------GGDVTIRGA-- 256
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446367334 337 wrvkETDRLFAMATELRKVGAEVEEGHDYIRITPPAKLHHADIGT 381
Cdd:PRK09369 257 ----RPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKT 297
|
|
| |
