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Conserved domains on  [gi|489125971|ref|WP_003035768|]
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MULTISPECIES: 3-phosphoshikimate 1-carboxyvinyltransferase [Citrobacter]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11860 super family cl29626
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
1-424 0e+00

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


The actual alignment was detected with superfamily member PRK11860:

Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 600.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTRceIIGNGG 80
Cdd:PRK11860   4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 ALhAQGSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860  82 QF-PVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 159 GGQVEVDGSVSSQFLTALLMTAPL-APQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPGAY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTRGE--LNAVDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPA---TLQFADIATYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAqaaDWKAAAIHTYDDHRMAMCF 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 489125971 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVA 435
 
Name Accession Description Interval E-value
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: 600.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTRceIIGNGG 80
Cdd:PRK11860   4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 ALhAQGSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860  82 QF-PVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 159 GGQVEVDGSVSSQFLTALLMTAPL-APQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPGAY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTRGE--LNAVDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPA---TLQFADIATYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAqaaDWKAAAIHTYDDHRMAMCF 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 489125971 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVA 435
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: 593.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSaDRTRCEIIGNGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEEL-DGGTLRVTGVGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 ALHAQgSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128   80 GLKEP-DAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 160 GQVEVDGSVSSQFLTALLMTAPLAPQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQsPGAYLV 239
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTRGELNAVDMDMNHIPDAAMTIA 319
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQFADIATYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
                        410       420
                 ....*....|....*....|....*
gi 489125971 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: 551.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSAdrTRCEIIGNGGALHAQGSVELF 91
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  92 LGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGFTGGQVEVDGSVSSQ 171
Cdd:cd01554   79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 172 FLTALLMTAPLAPQDTTIAIKgdlVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPgAYLVEGDASSASYFLA 251
Cdd:cd01554  159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 252 AGAIKGGTVKVTGIGRNSmqGDIRFADVLEKMGATITWGNDFIACTRGELNAVDMDMNHIP---DAAMTIATAALFAKGT 328
Cdd:cd01554  235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQFADIATYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554  313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
                        410
                 ....*....|....*.
gi 489125971 408 CTAKTFPDYFEQLARI 423
Cdd:cd01554  393 AINTSYPSFFDDLESL 408
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-423 4.58e-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: 457.12  E-value: 4.58e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   14 GTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTrcEIIGNGGAlhaQGSVELFLG 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGK---EPQAELDLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   94 NAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGFTGGQVEVDGSVSSQFL 173
Cdd:TIGR01356  76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  174 TALLMTAPLAPQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPGaYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  254 AIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTRG-ELNAVDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  333 NIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQFADIATYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
                         410
                  ....*....|..
gi 489125971  412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-420 1.17e-159

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 456.37  E-value: 1.17e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971    7 QPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGIS-YTLSADRTRCEIIGNGGALHAQ 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEiIKLDDEKSVVIVEGLGGSFEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   86 GSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGfTGGQVEVD 165
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  166 GSVSSQFLTALLMTAPLAPQDTTIaIKGdLVSKPYIDITLNLMKTFGVEIENQNY-QRFVVKGQQqyQSPGA-YLVEGDA 243
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTT-IEN-LASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGE--KLPGQeYRVEGDR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  244 SSASYFLAAGAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDF-IACTRGELNAVDMDMNHIPDAAMTIATAA 322
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  323 LFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPA-TLQFADIATYNDHRMAMCFSLVAL-SDTP 400
Cdd:pfam00275 316 AFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYGDHRIAMALALAGLvAEGE 395
                         410       420
                  ....*....|....*....|
gi 489125971  401 VTILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 396 TIIDDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
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: 600.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTRceIIGNGG 80
Cdd:PRK11860   4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 ALhAQGSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860  82 QF-PVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 159 GGQVEVDGSVSSQFLTALLMTAPL-APQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPGAY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTRGE--LNAVDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPA---TLQFADIATYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAqaaDWKAAAIHTYDDHRMAMCF 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 489125971 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVA 435
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: 593.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSaDRTRCEIIGNGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEEL-DGGTLRVTGVGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 ALHAQgSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128   80 GLKEP-DAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 160 GQVEVDGSVSSQFLTALLMTAPLAPQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQsPGAYLV 239
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTRGELNAVDMDMNHIPDAAMTIA 319
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQFADIATYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
                        410       420
                 ....*....|....*....|....*
gi 489125971 399 TPVTILDPKCTAKTFPDYFEQLARI 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: 579.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYtlsaDRTRCEIIGNGG 80
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI----EDDEVVVEGVGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 ALHAQGSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYlEQENYPPLRLRGGFTGG 160
Cdd:PRK02427  78 GGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRGGKKGG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 161 QVEVDGSVSSQFLTALLMTAPL-APQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQ---NYQRFVVKGQQQYQsPGA 236
Cdd:PRK02427 157 PIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVegwGYRRIVIKGGQRLR-GQD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 237 YLVEGDASSASYFLAAGAIKGG-TVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDF--------IACTRGELNAVDMD 307
Cdd:PRK02427 236 ITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEReggepvgdIRVRSSELKGIDID 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 308 MNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLqfADIATYNDHRM 387
Cdd:PRK02427 316 IPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHRI 393
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 489125971 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: 557.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTRCEIIGNGG 80
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 AL----HAQGSVELFLGNAGTAMRPLAAALCL--GSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRL- 153
Cdd:PLN02338  81 KFpvsgDSKEDVELFLGNAGTAMRPLTAAVTAagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVn 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 154 -RGGFTGGQVEVDGSVSSQFLTALLMTAPLAPQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQN-YQRFVVKGQQQY 231
Cdd:PLN02338 161 aAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDsWDRFFIKGGQKY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 232 QSPGAYLVEGDASSASYFLAAGAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTR--------GELNA 303
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGpprdafggKHLKA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 304 VDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQFADIATYN 383
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYD 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 489125971 384 DHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARIST 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: 551.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSAdrTRCEIIGNGGALHAQGSVELF 91
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  92 LGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGFTGGQVEVDGSVSSQ 171
Cdd:cd01554   79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 172 FLTALLMTAPLAPQDTTIAIKgdlVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPgAYLVEGDASSASYFLA 251
Cdd:cd01554  159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 252 AGAIKGGTVKVTGIGRNSmqGDIRFADVLEKMGATITWGNDFIACTRGELNAVDMDMNHIP---DAAMTIATAALFAKGT 328
Cdd:cd01554  235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQFADIATYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554  313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
                        410
                 ....*....|....*.
gi 489125971 408 CTAKTFPDYFEQLARI 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: 541.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRtrCEIIGNGGALHAQgSVELF 91
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGT--VEIVGGGGLGLPP-EAVLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  92 LGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGFTGGQVEVDGSVSSQ 171
Cdd:cd01556   78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 172 FLTALLMTAPLAPQDTTIaIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPgAYLVEGDASSASYFLA 251
Cdd:cd01556  158 FKSALLLAAPLAEGPTTI-IIGELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 252 AGAIKGGTVKVTGIGRNSmqGDIRFADVLEKMGATITWGN-DFIACTR-GELNAVDMDMNHIPDAAMTIATAALFAKGTT 329
Cdd:cd01556  236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 330 TLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITP-PATLQFADIATYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01556  314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
                        410
                 ....*....|....*.
gi 489125971 408 CTAKTFPDYFEQLARI 423
Cdd:cd01556  394 CVAKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-423 4.58e-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: 457.12  E-value: 4.58e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   14 GTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTrcEIIGNGGAlhaQGSVELFLG 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGK---EPQAELDLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   94 NAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGFTGGQVEVDGSVSSQFL 173
Cdd:TIGR01356  76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  174 TALLMTAPLAPQDTTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPGaYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  254 AIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIACTRG-ELNAVDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  333 NIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQFADIATYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
                         410
                  ....*....|..
gi 489125971  412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-420 1.17e-159

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 456.37  E-value: 1.17e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971    7 QPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGIS-YTLSADRTRCEIIGNGGALHAQ 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEiIKLDDEKSVVIVEGLGGSFEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   86 GSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGfTGGQVEVD 165
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  166 GSVSSQFLTALLMTAPLAPQDTTIaIKGdLVSKPYIDITLNLMKTFGVEIENQNY-QRFVVKGQQqyQSPGA-YLVEGDA 243
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTT-IEN-LASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGE--KLPGQeYRVEGDR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  244 SSASYFLAAGAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDF-IACTRGELNAVDMDMNHIPDAAMTIATAA 322
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  323 LFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPA-TLQFADIATYNDHRMAMCFSLVAL-SDTP 400
Cdd:pfam00275 316 AFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYGDHRIAMALALAGLvAEGE 395
                         410       420
                  ....*....|....*....|
gi 489125971  401 VTILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 396 TIIDDIECTDRSFPDFEEKL 415
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-426 1.03e-153

bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 450.70  E-value: 1.03e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISytLSADRTRCEIIGNGG 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVK--LSRDGGTCVVGGTRG 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  81 ALHAQgSVELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDYLEQENYPPLRLRGGFTG- 159
Cdd:PRK11861 318 AFTAK-TADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISv 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 160 -GQVEVDGSVSSQFLTALLMTAPLAPQD---TTIAIKGDLVSKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQSPG 235
Cdd:PRK11861 397 dAPIRVRGDVSSQFLTALLMTLPLVKAKdgaSVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPG 476
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 236 AYLVEGDASSASYFLAAGAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATITWGNDFIAC-----TRGELNAVDMDMNH 310
Cdd:PRK11861 477 TIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVrgighDHGRLAPIDMDFNL 556
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 311 IPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITPPATLQ-FADIATYNDHRMAM 389
Cdd:PRK11861 557 IPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTpNASIDTYDDHRMAM 636
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 489125971 390 CFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISTS 426
Cdd:PRK11861 637 CFSLVSLGGVPVRINDPKCVGKTFPDYFDRFLALANA 673
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
240-423 5.30e-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: 186.72  E-value: 5.30e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSM-----QGDIRFADVLEKM-GATITWGN---DFIACTRGELNAVDMDMNH 310
Cdd:cd01553    7 KGGGQILRSFLVLAAISGGPITVTGIRPDRAkpgllRQHLTFLKALEKIcGATVEGGElgsDRISFRPGTVRGGDVRFAI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 311 -----IPDAAMTIATAALFAKGTTTLRNIYNWRV----KETDRLFAMATELRKVGAEVEEGHD------------FIRIT 369
Cdd:cd01553   87 gsagsCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEVS 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489125971 370 PPATLQFADIatyndhRMAMCFSLVAlsdTPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:cd01553  167 PVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
3-422 2.33e-38

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 147.45  E-value: 2.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971   3 SLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALNVLGISYT-LSADRTRCEIIGNGGA 81
Cdd:PRK14806 303 SYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEgPHNGRVTIHGVGLHGL 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  82 LHAQGSveLFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAKIDyLEQENYPPLRLRGGFTGGQ 161
Cdd:PRK14806 383 KAPPGP--LYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIE-TGEEGRPPLSIRGGQRLKG 459
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 162 VEVDGSV-SSQFLTALLMTAPLAPQDTTiaikgdlVSKPYI--DITLNLMKTFGVEIEnqnyqrfvVKGQQQYQSPGAYL 238
Cdd:PRK14806 460 IHYDLPMaSAQVKSCLLLAGLYAEGETS-------VTEPAPtrDHTERMLRGFGYPVK--------VEGNTISVEGGGKL 524
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 239 ------VEGDASSASYFLAAGAIKGGT-VKVTGIGRNSMQgdIRFADVLEKMGATITWGNDFIActRGE------LNAVD 305
Cdd:PRK14806 525 tatdieVPADISSAAFFLVAASIAEGSeLTLEHVGINPTR--TGVIDILKLMGADITLENEREV--GGEpvadirVRGAR 600
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 306 MDMNHIPDAAMTIA--------TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDFIRITpPATLQFA 377
Cdd:PRK14806 601 LKGIDIPEDQVPLAidefpvlfVAAACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIE-GGIFGGG 679
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 489125971 378 DIATYNDHRMAMCFSLVAL-SDTPVTILDPKCTAKTFPDyFEQLAR 422
Cdd:PRK14806 680 EVESHGDHRIAMSFSVASLrASGPITIHDCANVATSFPN-FLELAN 724
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
36-363 1.61e-09

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: 59.23  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  36 NGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTrCEIigNGGALHaqgSVELFLGNAGTaMRplAAALCLGSndivL 115
Cdd:COG0766   36 DGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGT-LTI--DASNIN---STEAPYELVRK-MR--ASILVLGP----L 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 116 TGepRMKE-------------RPIG-HLvDALRQGGAKIDYlEQENYpplRLR-GGFTGGQVEVDG-SVssqflTA---L 176
Cdd:COG0766  103 LA--RFGEarvslpggcaigaRPIDlHL-KGLEALGAEIEI-EHGYI---EARaGRLKGARIYLDFpSV-----GAtenI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 177 LMTAPLAPQDTTI---AIKgdlvskPYID--IT-LNLMktfGVEIENQNYQRFVVKGQQQYqSPGAYLVEGD---ASSas 247
Cdd:COG0766  171 MMAAVLAEGTTVIenaARE------PEIVdlANfLNAM---GAKIEGAGTDTITIEGVEKL-HGAEHTVIPDrieAGT-- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 248 yFLAAGAIKGGTVKVTGIGRNSMQGdirFADVLEKMGATITWGNDFIACTR-GELNAVDM----------DMNHIpdaAM 316
Cdd:COG0766  239 -FLVAAAITGGDVTVKNVIPEHLEA---VLAKLREAGVEIEEGDDGIRVRGpGRLKAVDIktapypgfptDLQAQ---FM 311
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 489125971 317 TIATaalFAKGTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGH 363
Cdd:COG0766  312 ALLT---QAEGTSVITeTVFENR-------FMHVDELNRMGADIKlDGH 350
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
36-405 4.36e-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: 51.71  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  36 NGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTrCEIIgnggALHAQgSVELFLGNAGTaMRplAAALCLGsndiVL 115
Cdd:cd01555   25 DEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENT-LVID----ASNIN-STEAPYELVRK-MR--ASILVLG----PL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 116 TGepRMKE-------------RPIG-HLVdALRQGGAKIDylEQENYPPLRLRGGFTGGQVEVD-GSVssqflTA---LL 177
Cdd:cd01555   92 LA--RFGEarvslpggcaigaRPVDlHLK-GLEALGAKIE--IEDGYVEAKAAGRLKGARIYLDfPSV-----GAtenIM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 178 MTAPLAPQDTTI---AIkgdlvsKPYIDITLNLMKTFGVEIENQNYQRFVVKGQQQYQsPGAYLVEGDASSASYFLAAGA 254
Cdd:cd01555  162 MAAVLAEGTTVIenaAR------EPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLH-GAEHTVIPDRIEAGTFLVAAA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 255 IKGGTVKVTGIGRNSMqgdIRFADVLEKMGATITWGNDFIACTR--GELNAVDMDMNHIP----DAAMTIATAALFAKGT 328
Cdd:cd01555  235 ITGGDITVENVIPEHL---EAVLAKLREMGAKIEIGEDGIRVDGdgGRLKAVDIETAPYPgfptDLQAQFMALLTQAEGT 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 329 TTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGHDFIrITPPATLQFADI-ATynDHRMAMCFSLVALSDTPVTILD 405
Cdd:cd01555  312 SVITeTIFENR-------FMHVDELNRMGADIKvEGNTAI-IRGVTKLSGAPVmAT--DLRAGAALVLAGLAAEGETIIS 381
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
277-381 6.03e-06

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: 48.06  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 277 ADVLEKMGATITW-GNDFIACT-RGELNAVDMDMnhIPD--AAMTIATAALFAKGTTTLRNIynwrvkETDRLFAMATEL 352
Cdd:COG0766  196 ANFLNAMGAKIEGaGTDTITIEgVEKLHGAEHTV--IPDriEAGTFLVAAAITGGDVTVKNV------IPEHLEAVLAKL 267
                         90       100
                 ....*....|....*....|....*....
gi 489125971 353 RKVGAEVEEGHDFIRITPPATLQFADIAT 381
Cdd:COG0766  268 REAGVEIEEGDDGIRVRGPGRLKAVDIKT 296
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
36-363 4.05e-05

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 45.41  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971  36 NGTTVLTNLLDSDDVRHMLNALNVLGISYTLSADRTRceIIGNGGALHAQGSVELflgnAGTaMRplAAALCLGsndivl 115
Cdd:PRK09369  36 EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTV--TIDASNINNTEAPYEL----VKK-MR--ASILVLG------ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 116 tgeP---RMKE-------------RPIG-HLvDALRQGGAKIDylEQENYPPLRLRGGFTGGQVEVDG-SVssqflTA-- 175
Cdd:PRK09369 101 ---PllaRFGEakvslpggcaigaRPVDlHL-KGLEALGAEIE--IEHGYVEAKADGRLKGAHIVLDFpSV-----GAte 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 176 -LLMTAPLAPQDTTI---AIKgdlvskPYI-DIT--LNLMktfGVEIENQNYQRFVVKGQQQYqSPGAYLVEGDASSASY 248
Cdd:PRK09369 170 nILMAAVLAEGTTVIenaARE------PEIvDLAnfLNKM---GAKISGAGTDTITIEGVERL-HGAEHTVIPDRIEAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 249 FLAAGAIKGGTVKVTGIGRNSMQGdirFADVLEKMGATITWGNDFIACTR-GELNAVDM----------DMNhipdaAMT 317
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEA---VLAKLREAGAEIEEGEDGIRVDMpGRLKAVDIktapypgfptDMQ-----AQF 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 489125971 318 IATAALfAKGTTTlrniynwrVKET---DRLFaMATELRKVGAEVE-EGH 363
Cdd:PRK09369 312 MALLTQ-AEGTSV--------ITETifeNRFM-HVPELIRMGADIEvDGH 351
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
160-369 1.10e-04

UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.


Pssm-ID: 238796  Cd Length: 400  Bit Score: 44.00  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 160 GQVEVDGSVSSqfLTALLMTAPLAPQDTTI----AIKgDlvskpyIDITLNLMKTFGVEIENQNYQRFVV--KGQQQYQS 233
Cdd:cd01555    3 GEVRISGAKNA--ALPILAAALLTDEPVTLrnvpDLL-D------VETMIELLRSLGAKVEFEGENTLVIdaSNINSTEA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 234 PGAYlvegdASS--ASyFLAAGAI--KGGTVKVTG-----IGRnsmqgdiRFAD----VLEKMGATITWGNDFI-ACTRG 299
Cdd:cd01555   74 PYEL-----VRKmrAS-ILVLGPLlaRFGEARVSLpggcaIGA-------RPVDlhlkGLEALGAKIEIEDGYVeAKAAG 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125971 300 ELNAVDMDMNHIPDAA-MTIATAALFAKGTTTLRNIYnwrvKE---TDrlfaMATELRKVGAEVE-EGHDFIRIT 369
Cdd:cd01555  141 RLKGARIYLDFPSVGAtENIMMAAVLAEGTTVIENAA----REpeiVD----LANFLNKMGAKIEgAGTDTIRIE 207
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
278-369 8.53e-04

UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440529  Cd Length: 416  Bit Score: 41.51  E-value: 8.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 278 DVLEKMGATITWGNDFIACTRGELNAVDMDMnhipD-----AAMTIATAALFAKGTTTLRNIynwrvketdrlfamATE- 351
Cdd:COG0766  129 KGLEALGAEIEIEHGYIEARAGRLKGARIYL----DfpsvgATENIMMAAVLAEGTTVIENA--------------AREp 190
                         90       100
                 ....*....|....*....|....*..
gi 489125971 352 --------LRKVGAEVE-EGHDFIRIT 369
Cdd:COG0766  191 eivdlanfLNAMGAKIEgAGTDTITIE 217
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
277-381 2.41e-03

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 40.01  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125971 277 ADVLEKMGATIT-WGNDFIacT-RG--ELNAVDmdmnH--IPD---AAmTIATAALFAKGTTTLRNIynwrvkETDRLFA 347
Cdd:PRK09369 197 ANFLNKMGAKISgAGTDTI--TiEGveRLHGAE----HtvIPDrieAG-TFLVAAAITGGDVTIRGA------RPEHLEA 263
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489125971 348 MATELRKVGAEVEEGHDFIRITPPATLQFADIAT 381
Cdd:PRK09369 264 VLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKT 297
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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