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Conserved domains on  [gi|489512065|ref|WP_003416914|]
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MULTISPECIES: 3-phosphoshikimate 1-carboxyvinyltransferase [Mycobacterium]

Protein Classification

3-phosphoshikimate 1-carboxyvinyltransferase( domain architecture ID 11414790)

3-phosphoshikimate 1- carboxyvinyltransferase catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate; 3-phosphoshikimate 1-carboxyvinyltransferase catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate

EC:  2.5.1.19
PubMed:  8973316|17348837
SCOP:  4001425

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
8-422 7.76e-138

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: 402.16  E-value: 7.76e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   8 TAPTPVRATVTVPGSKSQTNRALVLAAlaaaQGRGASTISGALRSRDTELMLDALQTLGLRVDGV-GSELTVSGRIE--P 84
Cdd:COG0128    7 APPSPLKGTVRVPGSKSISHRALLLAA----LAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGVGGglK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  85 GPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTG---LPFRVRGnGSLAGGTVA 161
Cdd:COG0128   83 EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGggyLPLTIRG-GPLKGGEYE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 162 IDASASSQFVSGLLLSAASFTDGLTVQHTGsSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVR-PGPVAARRWDIEPDL 240
Cdd:COG0128  162 IPGSASSQFKSALLLAGPLAEGGLEITVTG-ELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPgGQRYRPGDYTVPGDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 241 TNAVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGpTGYDGFDVDLRAVGELTPSVAALA 320
Cdd:COG0128  241 SSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRG-SPLKGIDIDLSDIPDEAPTLAVLA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 321 ALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVIT-ATPLRPGIWRAYADHRMAMAGAIIGLRVAG 399
Cdd:COG0128  320 AFAE--GTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEgGPKLKGAEVDSYGDHRIAMAFAVAGLRAEG 397
                        410       420
                 ....*....|....*....|....
gi 489512065 400 -VEVDDIAATTKTLPEFPRLWAEM 422
Cdd:COG0128  398 pVTIDDAECVAKSFPDFFELLESL 421
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
8-422 7.76e-138

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: 402.16  E-value: 7.76e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   8 TAPTPVRATVTVPGSKSQTNRALVLAAlaaaQGRGASTISGALRSRDTELMLDALQTLGLRVDGV-GSELTVSGRIE--P 84
Cdd:COG0128    7 APPSPLKGTVRVPGSKSISHRALLLAA----LAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGVGGglK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  85 GPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTG---LPFRVRGnGSLAGGTVA 161
Cdd:COG0128   83 EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGggyLPLTIRG-GPLKGGEYE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 162 IDASASSQFVSGLLLSAASFTDGLTVQHTGsSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVR-PGPVAARRWDIEPDL 240
Cdd:COG0128  162 IPGSASSQFKSALLLAGPLAEGGLEITVTG-ELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPgGQRYRPGDYTVPGDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 241 TNAVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGpTGYDGFDVDLRAVGELTPSVAALA 320
Cdd:COG0128  241 SSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRG-SPLKGIDIDLSDIPDEAPTLAVLA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 321 ALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVIT-ATPLRPGIWRAYADHRMAMAGAIIGLRVAG 399
Cdd:COG0128  320 AFAE--GTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEgGPKLKGAEVDSYGDHRIAMAFAVAGLRAEG 397
                        410       420
                 ....*....|....*....|....
gi 489512065 400 -VEVDDIAATTKTLPEFPRLWAEM 422
Cdd:COG0128  398 pVTIDDAECVAKSFPDFFELLESL 421
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-424 3.04e-136

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 398.36  E-value: 3.04e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   1 MKTWPAPTAPTPVRATVTVPGSKSQTNRALVLAAlaaaQGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELT-VS 79
Cdd:PRK02427   1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAA----LAEGETTITNLLRSEDTLATLNALRALGVEIEDDEVVVEgVG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  80 GRIEPGPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGT---GLPFRVRGngSLA 156
Cdd:PRK02427  77 GGGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRdegYLPLTIRG--GKK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 157 GGTVAIDASASSQFVSGLLLSAASFTDGLTVQHTGSSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQV----RPGPVAAR 232
Cdd:PRK02427 155 GGPIEYDGPVSSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYRRivikGGQRLRGQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 233 RWDIEPDLTNAVAFLSAAVVSGG-TVRITGWPRVSVQPADHILAILRQLNAVVIHAD--------SSLEVRGPTgYDGFD 303
Cdd:PRK02427 235 DITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENereggepvGDIRVRSSE-LKGID 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 304 VDLRAVGELTPSVAALAALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATPLRPGIwRAYAD 383
Cdd:PRK02427 314 IDIPDIIDEAPTLAVLAAFAE--GTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLAGVV-DSYGD 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 489512065 384 HRMAMAGAIIGLRV-AGVEVDDIAATTKTLPEFPRLWAEMVG 424
Cdd:PRK02427 391 HRIAMAFAIAGLAAeGPVTIDDPECVAKSFPDFFEDLASLGA 432
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-419 7.00e-130

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 381.65  E-value: 7.00e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065    8 TAPTPVRATVTVPGSKSQTNRALVLAALaaaqGRGASTISGALRSRDTELMLDALQTLG---LRVDGVGSELTVSGRI-- 82
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAAL----AAGESTITNLLDSDDTLTMLEALRALGaeiIKLDDEKSVVIVEGLGgs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   83 -EPGPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDG----TGLPFRVRGngsLAG 157
Cdd:pfam00275  77 fEAPEDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGregyNYAPLKVRG---LRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  158 GTVAIDASASSQFVSGLLLSAASFTDGlTVQHTGssLPSAPHIAMTAAMLRQAGVDID-DSTPNRWQVRPGPVAAR-RWD 235
Cdd:pfam00275 154 GGIHIDGDVSSQFVTSLLMLAALLAEG-TTTIEN--LASEPYIDDTENMLKKFGAKIEgSGTELSITVKGGEKLPGqEYR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  236 IEPDLTNAVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGPTGYDGFDVDLRAVGELTPS 315
Cdd:pfam00275 231 VEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPPGLRGKAVDIRTAPDPAPT 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  316 VAALAALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGL-VITATP-LRPGIWRAYADHRMAMAGAII 393
Cdd:pfam00275 311 TAVLAAFAE--GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKeLKGAEVDSYGDHRIAMALALA 388
                         410       420
                  ....*....|....*....|....*..
gi 489512065  394 GLRVAG-VEVDDIAATTKTLPEFPRLW 419
Cdd:pfam00275 389 GLVAEGeTIIDDIECTDRSFPDFEEKL 415
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
13-422 6.58e-126

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: 371.12  E-value: 6.58e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  13 VRATVTVPGSKSQTNRALVLAAlaaaQGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPG--PGARV 90
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAA----LAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGlpPEAVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  91 DCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTGLPFR--VRGNGSLAGGTVAIDASASS 168
Cdd:cd01556   77 DCGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYppLIGGGGLKGGEVEIPGAVSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 169 QFVSGLLLsAASFTDGLTVQHTGsSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVRPG-PVAARRWDIEPDLTNAVAFL 247
Cdd:cd01556  157 QFKSALLL-AAPLAEGPTTIIIG-ELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGqKYKGPEYTVEGDASSAAFFL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 248 SAAVVSGGTVRITGWPRVSvqPADHILAILRQLNA-VVIHADSSLEVRGPTGYDGFDVDLRAVGELTPSVAALAALASpg 326
Cdd:cd01556  235 AAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGAdIEIGNEDTVVVESGGKLKGIDIDGNDIPDEAPTLAVLAAFAE-- 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 327 SVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATPLRPGIWRAY--ADHRMAMAGAIIGLR-VAGVEVD 403
Cdd:cd01556  311 GPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPLKGAGVEVYtyGDHRIAMSFAIAGLVaEGGVTIE 390
                        410
                 ....*....|....*....
gi 489512065 404 DIAATTKTLPEFPRLWAEM 422
Cdd:cd01556  391 DPECVAKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
17-424 2.75e-108

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: 326.15  E-value: 2.75e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   17 VTVPGSKSQTNRALVLAALaaaqGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPGPGARVDCGLAG 96
Cdd:TIGR01356   3 IRAPGSKSITHRALILAAL----AEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGKEPQAELDLGNSG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   97 TVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTG----LPFRVRGNgsLAGGTVAIDASASSQFVS 172
Cdd:TIGR01356  79 TTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEgggsLPLTISGP--LPGGIVYISGSASSQYKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  173 GLLLsAASFTDGLTVQHTGSSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVRPG-PVAARRWDIEPDLTNAVAFLSAAV 251
Cdd:TIGR01356 157 ALLL-AAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGqKYGPQGYDVPGDYSSAAFFLAAAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  252 VSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGPTGYDGFDVDLRAVGELTPSVAALAALASPgsVSRL 331
Cdd:TIGR01356 236 ITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASGLKGIKIDMDDMIDELPTLAVLAAFAEG--VTRI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  332 SGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATP-LRPGIWRAYADHRMAMAGAIIGLRVAG-VEVDDIAATT 409
Cdd:TIGR01356 314 TGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKeLKGAVVDTFGDHRIAMAFAVAGLVAEGeVLIDDPECVA 393
                         410
                  ....*....|....*
gi 489512065  410 KTLPEFPRLWAEMVG 424
Cdd:TIGR01356 394 KSFPSFFDVLERLGA 408
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
8-422 7.76e-138

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: 402.16  E-value: 7.76e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   8 TAPTPVRATVTVPGSKSQTNRALVLAAlaaaQGRGASTISGALRSRDTELMLDALQTLGLRVDGV-GSELTVSGRIE--P 84
Cdd:COG0128    7 APPSPLKGTVRVPGSKSISHRALLLAA----LAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGVGGglK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  85 GPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTG---LPFRVRGnGSLAGGTVA 161
Cdd:COG0128   83 EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGggyLPLTIRG-GPLKGGEYE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 162 IDASASSQFVSGLLLSAASFTDGLTVQHTGsSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVR-PGPVAARRWDIEPDL 240
Cdd:COG0128  162 IPGSASSQFKSALLLAGPLAEGGLEITVTG-ELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPgGQRYRPGDYTVPGDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 241 TNAVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGpTGYDGFDVDLRAVGELTPSVAALA 320
Cdd:COG0128  241 SSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRG-SPLKGIDIDLSDIPDEAPTLAVLA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 321 ALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVIT-ATPLRPGIWRAYADHRMAMAGAIIGLRVAG 399
Cdd:COG0128  320 AFAE--GTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEgGPKLKGAEVDSYGDHRIAMAFAVAGLRAEG 397
                        410       420
                 ....*....|....*....|....
gi 489512065 400 -VEVDDIAATTKTLPEFPRLWAEM 422
Cdd:COG0128  398 pVTIDDAECVAKSFPDFFELLESL 421
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-424 3.04e-136

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 398.36  E-value: 3.04e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   1 MKTWPAPTAPTPVRATVTVPGSKSQTNRALVLAAlaaaQGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELT-VS 79
Cdd:PRK02427   1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAA----LAEGETTITNLLRSEDTLATLNALRALGVEIEDDEVVVEgVG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  80 GRIEPGPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGT---GLPFRVRGngSLA 156
Cdd:PRK02427  77 GGGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRdegYLPLTIRG--GKK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 157 GGTVAIDASASSQFVSGLLLSAASFTDGLTVQHTGSSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQV----RPGPVAAR 232
Cdd:PRK02427 155 GGPIEYDGPVSSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYRRivikGGQRLRGQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 233 RWDIEPDLTNAVAFLSAAVVSGG-TVRITGWPRVSVQPADHILAILRQLNAVVIHAD--------SSLEVRGPTgYDGFD 303
Cdd:PRK02427 235 DITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENereggepvGDIRVRSSE-LKGID 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 304 VDLRAVGELTPSVAALAALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATPLRPGIwRAYAD 383
Cdd:PRK02427 314 IDIPDIIDEAPTLAVLAAFAE--GTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLAGVV-DSYGD 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 489512065 384 HRMAMAGAIIGLRV-AGVEVDDIAATTKTLPEFPRLWAEMVG 424
Cdd:PRK02427 391 HRIAMAFAIAGLAAeGPVTIDDPECVAKSFPDFFEDLASLGA 432
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-419 7.00e-130

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 381.65  E-value: 7.00e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065    8 TAPTPVRATVTVPGSKSQTNRALVLAALaaaqGRGASTISGALRSRDTELMLDALQTLG---LRVDGVGSELTVSGRI-- 82
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAAL----AAGESTITNLLDSDDTLTMLEALRALGaeiIKLDDEKSVVIVEGLGgs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   83 -EPGPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDG----TGLPFRVRGngsLAG 157
Cdd:pfam00275  77 fEAPEDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGregyNYAPLKVRG---LRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  158 GTVAIDASASSQFVSGLLLSAASFTDGlTVQHTGssLPSAPHIAMTAAMLRQAGVDID-DSTPNRWQVRPGPVAAR-RWD 235
Cdd:pfam00275 154 GGIHIDGDVSSQFVTSLLMLAALLAEG-TTTIEN--LASEPYIDDTENMLKKFGAKIEgSGTELSITVKGGEKLPGqEYR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  236 IEPDLTNAVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGPTGYDGFDVDLRAVGELTPS 315
Cdd:pfam00275 231 VEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPPGLRGKAVDIRTAPDPAPT 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  316 VAALAALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGL-VITATP-LRPGIWRAYADHRMAMAGAII 393
Cdd:pfam00275 311 TAVLAAFAE--GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKeLKGAEVDSYGDHRIAMALALA 388
                         410       420
                  ....*....|....*....|....*..
gi 489512065  394 GLRVAG-VEVDDIAATTKTLPEFPRLW 419
Cdd:pfam00275 389 GLVAEGeTIIDDIECTDRSFPDFEEKL 415
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
13-422 6.58e-126

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: 371.12  E-value: 6.58e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  13 VRATVTVPGSKSQTNRALVLAAlaaaQGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPG--PGARV 90
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAA----LAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGlpPEAVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  91 DCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTGLPFR--VRGNGSLAGGTVAIDASASS 168
Cdd:cd01556   77 DCGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYppLIGGGGLKGGEVEIPGAVSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 169 QFVSGLLLsAASFTDGLTVQHTGsSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVRPG-PVAARRWDIEPDLTNAVAFL 247
Cdd:cd01556  157 QFKSALLL-AAPLAEGPTTIIIG-ELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGqKYKGPEYTVEGDASSAAFFL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 248 SAAVVSGGTVRITGWPRVSvqPADHILAILRQLNA-VVIHADSSLEVRGPTGYDGFDVDLRAVGELTPSVAALAALASpg 326
Cdd:cd01556  235 AAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGAdIEIGNEDTVVVESGGKLKGIDIDGNDIPDEAPTLAVLAAFAE-- 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 327 SVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATPLRPGIWRAY--ADHRMAMAGAIIGLR-VAGVEVD 403
Cdd:cd01556  311 GPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPLKGAGVEVYtyGDHRIAMSFAIAGLVaEGGVTIE 390
                        410
                 ....*....|....*....
gi 489512065 404 DIAATTKTLPEFPRLWAEM 422
Cdd:cd01556  391 DPECVAKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
17-424 2.75e-108

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: 326.15  E-value: 2.75e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   17 VTVPGSKSQTNRALVLAALaaaqGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPGPGARVDCGLAG 96
Cdd:TIGR01356   3 IRAPGSKSITHRALILAAL----AEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGKEPQAELDLGNSG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065   97 TVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTG----LPFRVRGNgsLAGGTVAIDASASSQFVS 172
Cdd:TIGR01356  79 TTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEgggsLPLTISGP--LPGGIVYISGSASSQYKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  173 GLLLsAASFTDGLTVQHTGSSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVRPG-PVAARRWDIEPDLTNAVAFLSAAV 251
Cdd:TIGR01356 157 ALLL-AAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGqKYGPQGYDVPGDYSSAAFFLAAAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  252 VSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGPTGYDGFDVDLRAVGELTPSVAALAALASPgsVSRL 331
Cdd:TIGR01356 236 ITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASGLKGIKIDMDDMIDELPTLAVLAAFAEG--VTRI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  332 SGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATP-LRPGIWRAYADHRMAMAGAIIGLRVAG-VEVDDIAATT 409
Cdd:TIGR01356 314 TGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKeLKGAVVDTFGDHRIAMAFAVAGLVAEGeVLIDDPECVA 393
                         410
                  ....*....|....*
gi 489512065  410 KTLPEFPRLWAEMVG 424
Cdd:TIGR01356 394 KSFPSFFDVLERLGA 408
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
16-415 6.09e-45

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 162.22  E-value: 6.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  16 TVTVPGSKSQTNRALVLAALAaaqgRGASTISGALRSRDTELMLDALQTLGLRV--DGVGSELTV---SGRIEPGPGARV 90
Cdd:PLN02338  15 TVKLPGSKSLSNRILLLAALS----EGTTVVDNLLDSDDIRYMLGALKTLGLNVeeDSENNRAVVegcGGKFPVSGDSKE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  91 DCGL----AGTVLRfvpPL-----AALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVD---GTGLP-FRVRGNGSLAG 157
Cdd:PLN02338  91 DVELflgnAGTAMR---PLtaavtAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVEctlGTNCPpVRVNAAGGLPG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 158 GTVAIDASASSQFVSGLLLSAASFTDGLTVQHTgSSLPSAPHIAMTAAMLRQAGVDIDDS-TPNRWQVRPG-----PVAA 231
Cdd:PLN02338 168 GKVKLSGSISSQYLTALLMAAPLALGDVEIEIV-DKLISVPYVEMTLKLMERFGVSVEHSdSWDRFFIKGGqkyksPGNA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 232 RrwdIEPDLTNAVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGPTGYD-------GFDV 304
Cdd:PLN02338 247 Y---VEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGPPRDAfggkhlkAIDV 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 305 DLRAVGELTPSVAALAALASPGSVSRlsGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATP-LRPGIWRAYAD 383
Cdd:PLN02338 324 NMNKMPDVAMTLAVVALFADGPTAIR--DVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKkLKPAEIDTYDD 401
                        410       420       430
                 ....*....|....*....|....*....|..
gi 489512065 384 HRMAMAGAIIGLRVAGVEVDDIAATTKTLPEF 415
Cdd:PLN02338 402 HRMAMAFSLAACGDVPVTINDPGCTRKTFPTY 433
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
13-415 7.93e-44

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 162.91  E-value: 7.93e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  13 VRATVTVPGSKSQTNRALVLAALAaaqgRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPGPGARVD- 91
Cdd:PRK11860  15 AGGTVRLPGSKSISNRVLLLAALS----EGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYRITGLGGQFPVKQADl 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  92 -CGLAGTVLRfvpPLAALGSVpvtFDGDQQARG------RPIAPLLDALRELGVAVDGTGL----PFRVRGNGSLAGGTV 160
Cdd:PRK11860  91 fLGNAGTAMR---PLTAALAL---LGGEYELSGvprmheRPIGDLVDALRQLGCDIDYLGNegfpPLRIGPAPLRLDAPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 161 AIDASASSQFVSGLLLS---AASFTdgLTVQHTGsSLPSAPHIAMTAAMLRQAGVDIDDstpNRWQ----------VRPG 227
Cdd:PRK11860 165 RVRGDVSSQFLTALLMAlplVARRD--ITIEVVG-ELISKPYIEITLNLLARFGIAVQR---EGWQrftipagsryRSPG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 228 PVAarrwdIEPDLTNAVAFLSAAVVSGGT-VRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGPTG-YDGFDVD 305
Cdd:PRK11860 239 EIH-----VEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAWpLKAIDLD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 306 LRAVGE--LTPSVAALAALASpgsvSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITAtPLRPGIWRA--- 380
Cdd:PRK11860 314 CNHIPDaaMTLAVMALYADGT----TTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTP-PAQAADWKAaai 388
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 489512065 381 --YADHRMAMAGAIIGLRVAG--VEVDDIAATTKTLPEF 415
Cdd:PRK11860 389 htYDDHRMAMCFSLAAFNPAGlpVRINDPKCVAKTFPDY 427
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
14-415 8.74e-35

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 137.14  E-value: 8.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  14 RATVTVPGSKSQTNRALVLAALaaaqGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPGPGARVDC- 92
Cdd:PRK11861 252 QGTVRLPGSKSISNRVLLLAAL----AEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAFTAKTADLf 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  93 -GLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTG----LPFRVRGNGSLAGGTVAIDASAS 167
Cdd:PRK11861 328 lGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGnegfPPLRIRPATISVDAPIRVRGDVS 407
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 168 SQFVSGLLLSA--ASFTDGLTVQHTGSSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVrPGPVAARRWD---IEPDLTN 242
Cdd:PRK11861 408 SQFLTALLMTLplVKAKDGASVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTV-PAGVRYRSPGtimVEGDASS 486
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 243 AVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGpTGYDG-----FDVDLRAVGELTPSVA 317
Cdd:PRK11861 487 ASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVRG-IGHDHgrlapIDMDFNLIPDAAMTIA 565
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 318 ALAALASpgSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATP-LRPGI-WRAYADHRMAMAGAIIGL 395
Cdd:PRK11861 566 VAALFAD--GPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAqLTPNAsIDTYDDHRMAMCFSLVSL 643
                        410       420
                 ....*....|....*....|
gi 489512065 396 RVAGVEVDDIAATTKTLPEF 415
Cdd:PRK11861 644 GGVPVRINDPKCVGKTFPDY 663
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
13-415 5.69e-32

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: 126.18  E-value: 5.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  13 VRATVTVPGSKSQTNRALVLAALaaaqGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPG---PGAR 89
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASL----AEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGlkaPQNA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  90 VDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVdgTGLPFRV----RGNGSLAGGTVAIDAS 165
Cdd:cd01554   77 LNLGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASI--SGQEERDlpplLKGGKNLGPIHYEDPI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 166 ASSQFVSGLLLsAASFTDGLTVQHTGSslpSAPHIAMTAAMLRQAGVDIDDSTPNRWQVR-PGPVAARRWDIEPDLTNAV 244
Cdd:cd01554  155 ASAQVKSALMF-AALLAKGETVIIEAA---KEPTINHTENMLQTFGGHISVQGTKKIVVQgPQKLTGQKYVVPGDISSAA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 245 AFLSAAVVSGGTVRITGWPRVSVQpaDHILAILRQLNAVVIHADSSLEVRGpTGYDGFDVDLRAVGELTPSVAALAALAS 324
Cdd:cd01554  231 FFLVAAAIAPGRLVLQNVGINETR--TGIIDVLRAMGAKIEIGEDTISVES-SDLKATEICGALIPRLIDELPIIALLAL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 325 PGS-VSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITA-TPLRPGIWRAYADHRMAMAGAIIGLRVAG-VE 401
Cdd:cd01554  308 QAQgTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGkEKLHGARVNTFGDHRIGMMTALAALVADGeVE 387
                        410
                 ....*....|....
gi 489512065 402 VDDIAATTKTLPEF 415
Cdd:cd01554  388 LDRAEAINTSYPSF 401
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
12-418 7.45e-18

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 86.20  E-value: 7.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  12 PVRATVTVPGSKSQTNRALVLAALAaaqgRGASTISGALRSRDTELMLDALQTLGLRVDGVGS-ELTVSG------RIEP 84
Cdd:PRK14806 311 AVKGTIRVPGDKSISHRSIMLGSLA----EGVTEVEGFLEGEDALATLQAFRDMGVVIEGPHNgRVTIHGvglhglKAPP 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  85 GPgarVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAV----DGTGlPFRVRGNGSLAGGTV 160
Cdd:PRK14806 387 GP---LYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIetgeEGRP-PLSIRGGQRLKGIHY 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 161 AIDAsASSQFVSGLLLSaasftdGLTVQHTGSSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVRPGPVAARRWDIEPDL 240
Cdd:PRK14806 463 DLPM-ASAQVKSCLLLA------GLYAEGETSVTEPAPTRDHTERMLRGFGYPVKVEGNTISVEGGGKLTATDIEVPADI 535
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 241 TNAVAFLSAAVVSGGTvRITgWPRVSVQPADH-ILAILRQlnavvIHADSSLEVRGPTGydGFDV-DLRAVG-------- 310
Cdd:PRK14806 536 SSAAFFLVAASIAEGS-ELT-LEHVGINPTRTgVIDILKL-----MGADITLENEREVG--GEPVaDIRVRGarlkgidi 606
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 311 --ELTP------SVAALAALASPGsVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATPLRPGIWRAYA 382
Cdd:PRK14806 607 peDQVPlaidefPVLFVAAACAEG-RTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGGIFGGGEVESHG 685
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 489512065 383 DHRMAMAGAIIGLRVAGV-EVDDIAATTKTLPEFPRL 418
Cdd:PRK14806 686 DHRIAMSFSVASLRASGPiTIHDCANVATSFPNFLEL 722
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
41-304 1.34e-07

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: 53.45  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  41 RGASTISGALRSRDTELMLDALQTLGLRVD-GVGSELTV-SGRIEpgpGARVDCGLAGTvLR----FVPPLAA-LGSVPV 113
Cdd:COG0766   36 DGPVTLRNVPDLSDVRTMLELLESLGVKVErDDGGTLTIdASNIN---STEAPYELVRK-MRasilVLGPLLArFGEARV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 114 TFDGdqqarG-----RPIAPLLDALRELGVAVDGTGLPFRVRGNGsLAGGTVAIDasassqFVS-G----LLLsAASFTD 183
Cdd:COG0766  112 SLPG-----GcaigaRPIDLHLKGLEALGAEIEIEHGYIEARAGR-LKGARIYLD------FPSvGatenIMM-AAVLAE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 184 GLTVqhtgssLPSA---PHIAMTAAMLRQAGVDIDDSTPNRWQVRP----GPVaarRWDIEPDLTNAVAFLSAAVVSGGT 256
Cdd:COG0766  179 GTTV------IENAarePEIVDLANFLNAMGAKIEGAGTDTITIEGveklHGA---EHTVIPDRIEAGTFLVAAAITGGD 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489512065 257 VRITGwprvsVQPaDH---ILAILRQLNAVVIHADSSLEVRGPTGYDGFDV 304
Cdd:COG0766  250 VTVKN-----VIP-EHleaVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDI 294
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
44-309 3.57e-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: 45.93  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065  44 STISGALRSRDTELMLDALQTLGLRVDGVGS-ELTV-SGRIEPGPgarVDCGLAGTvLR----FVPPLAA-LGSVPVTFD 116
Cdd:cd01555   28 VTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIdASNINSTE---APYELVRK-MRasilVLGPLLArFGEARVSLP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 117 GDQQARGRPIAPLLDALRELGVAVDGTGLPFRVRGNGSLAGGTVAIDasassqFVS-GL---LLSAASFTDGLTVqhtgs 192
Cdd:cd01555  104 GGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLD------FPSvGAtenIMMAAVLAEGTTV----- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512065 193 sLPSA---PHIAMTAAMLRQAGVDIDDSTPNRWQV----RPGPVaarRWDIEPDLTNAVAFLSAAVVSGGTVRITGwprv 265
Cdd:cd01555  173 -IENAarePEIVDLANFLNKMGAKIEGAGTDTIRIegveRLHGA---EHTVIPDRIEAGTFLVAAAITGGDITVEN---- 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489512065 266 sVQPaDH---ILAILRQLNAVVIHADSSLEVRGPTG-----------YDGFDVDLRAV 309
Cdd:cd01555  245 -VIP-EHleaVLAKLREMGAKIEIGEDGIRVDGDGGrlkavdietapYPGFPTDLQAQ 300
 
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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