NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488911987|ref|WP_002823062|]
View 

3-phosphoshikimate 1-carboxyvinyltransferase [Oenococcus oeni]

Protein Classification

3-phosphoshikimate 1-carboxyvinyltransferase( domain architecture ID 11479797)

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:  17348837

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-432 6.66e-160

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


:

Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 458.07  E-value: 6.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKygRDLIVYGSGLDA 80
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIED--DEVVVEGVGGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  81 FKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFD 160
Cdd:PRK02427  80 LKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKGGPIE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 161 YHLPIASAQVKSALIFSALQADEPSIIF--EKEATRNHLEI---MLNDFGADIK----TNGLCITVMPRPKLSGRTISIP 231
Cdd:PRK02427 160 YDGPVSSQFVKSLLLLAPLFAEGDTETTviEPLPSRPHTEItlrMLRAFGVEVEnvegWGYRRIVIKGGQRLRGQDITVP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 232 GDISSAAFFMVAASLLPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEItakEI 309
Cdd:PRK02427 240 GDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVRSSELKGIDI---DI 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 310 PNVIDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPklqiPENNLATHGDHR 389
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP----LAGVVDSYGDHR 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 488911987 390 IGMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:PRK02427 393 IAMAFAIAGLAAE--GPVTIDDPECVAKSFPDFFEDLASLGAN 433
 
Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-432 6.66e-160

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 458.07  E-value: 6.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKygRDLIVYGSGLDA 80
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIED--DEVVVEGVGGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  81 FKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFD 160
Cdd:PRK02427  80 LKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKGGPIE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 161 YHLPIASAQVKSALIFSALQADEPSIIF--EKEATRNHLEI---MLNDFGADIK----TNGLCITVMPRPKLSGRTISIP 231
Cdd:PRK02427 160 YDGPVSSQFVKSLLLLAPLFAEGDTETTviEPLPSRPHTEItlrMLRAFGVEVEnvegWGYRRIVIKGGQRLRGQDITVP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 232 GDISSAAFFMVAASLLPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEItakEI 309
Cdd:PRK02427 240 GDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVRSSELKGIDI---DI 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 310 PNVIDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPklqiPENNLATHGDHR 389
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP----LAGVVDSYGDHR 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 488911987 390 IGMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:PRK02427 393 IAMAFAIAGLAAE--GPVTIDDPECVAKSFPDFFEDLASLGAN 433
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-429 1.38e-156

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: 449.15  E-value: 1.38e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKY-GRDLIVYGSGlD 79
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGVG-G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  80 AFKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAF 159
Cdd:COG0128   80 GLKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGP-LKGG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 160 DYHLP-IASAQVKSALIFSALQADEPSIIF-----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPG 232
Cdd:COG0128  159 EYEIPgSASSQFKSALLLAGPLAEGGLEITvtgelESKPYRDHTERMLRAFGVEVEVEGYrRFTVPGGQRYRPGDYTVPG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 233 DISSAAFFMVAASLLpNSCICLKKVGLNPT--RIGIISVLKRMNANIEVKKTSneaeaygdIIVRSSNLHAVEITAKEIP 310
Cdd:COG0128  239 DISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG--------ITVRGSPLKGIDIDLSDIP 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 311 nviDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQipENNLATHGDHRI 390
Cdd:COG0128  310 ---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLK--GAEVDSYGDHRI 384
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 488911987 391 GMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYL 429
Cdd:COG0128  385 AMAFAVAGLRAE--GPVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-429 1.61e-145

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: 420.81  E-value: 1.61e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGlDAFKDPKKPLNMG 91
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  92 NSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAFDYHLPIA-SAQV 170
Cdd:cd01556   80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGG-LKGGEVEIPGAvSSQF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 171 KSALIFSALQADEPSIIF----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAAS 245
Cdd:cd01556  159 KSALLLAAPLAEGPTTIIigelESKPYIDHTERMLRAFGAEVEVDGYrTITVKGGQKYKGPEYTVEGDASSAAFFLAAAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 246 LLPnSCICLKKVGLNPTRIGIISVLKRMNANIEVKKTsneaeayGDIIVRSSN-LHAVEITAKEIPnviDELPILTLAAS 324
Cdd:cd01556  239 ITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNE-------DTVVVESGGkLKGIDIDGNDIP---DEAPTLAVLAA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 325 LAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCP-KLQIPENNlaTHGDHRIGMMLAVAALLVDT 403
Cdd:cd01556  308 FAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPlKGAGVEVY--TYGDHRIAMSFAIAGLVAEG 385
                        410       420
                 ....*....|....*....|....*.
gi 488911987 404 SktITLNNPEAIKISYPNFFRDLDYL 429
Cdd:cd01556  386 G--VTIEDPECVAKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-432 6.36e-116

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: 345.41  E-value: 6.36e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   14 GSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGldaFKDPKKPLNMGNS 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVG---GKEPQAELDLGNS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   94 GTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEF-SLTGNGTLPITVIGHPSLkAFDYHLPIASAQVKS 172
Cdd:TIGR01356  78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEIsSLEGGGSLPLTISGPLPG-GIVYISGSASSQYKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  173 ALIFSA--LQADEPSIIFEKEATRNHLEIMLNDFGADI----KTNGLCITVMPRPKLSGRTISIPGDISSAAFFMVAAsL 246
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFGveveRSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAA-A 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  247 LPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKtsneaeayGDIIVR-SSNLHAVEItakEIPNVIDELPILTLAA 323
Cdd:TIGR01356 236 ITGGRVTLENLGINPTQGDkaIIIVLEEMGADIEVEE--------DDLIVEgASGLKGIKI---DMDDMIDELPTLAVLA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  324 SLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATHGDHRIGMMLAVAALLVDt 403
Cdd:TIGR01356 305 AFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAV--VDTFGDHRIAMAFAVAGLVAE- 381
                         410       420
                  ....*....|....*....|....*....
gi 488911987  404 sKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:TIGR01356 382 -GEVLIDDPECVAKSFPSFFDVLERLGAN 409
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
12-426 5.17e-98

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 299.60  E-value: 5.17e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRD---LIVYGSGLDAFKDPKKPL 88
Cdd:pfam00275   6 LSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEksvVIVEGLGGSFEAPEDLVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   89 NMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGE-FSLTGNGTLPITVIGHPsLKAFDYHLPIAS 167
Cdd:pfam00275  86 DMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEiEGREGYNYAPLKVRGLR-LGGIHIDGDVSS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  168 AQVKSALIFSALQADEPSII--FEKEATRNHLEIMLNDFGADIKTNG--LCITVMPRPKLSGRTISIPGDISSAAFFMVA 243
Cdd:pfam00275 165 QFVTSLLMLAALLAEGTTTIenLASEPYIDDTENMLKKFGAKIEGSGteLSITVKGGEKLPGQEYRVEGDRSSAAYFLVA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  244 ASLLPnSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSneaeaygDIIVRSSNLHAVEItakEIPNVIDELPILTL 321
Cdd:pfam00275 245 AAITG-GTVTVENVGINSLQGDeaLLEILEKMGAEITQEEDA-------DIVVGPPGLRGKAV---DIRTAPDPAPTTAV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  322 AASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGM-VIDGCPKLQIPEnnLATHGDHRIGMMLAVAALL 400
Cdd:pfam00275 314 LAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAE--VDSYGDHRIAMALALAGLV 391
                         410       420
                  ....*....|....*....|....*.
gi 488911987  401 VDTSKTItlNNPEAIKISYPNFFRDL 426
Cdd:pfam00275 392 AEGETII--DDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-432 6.66e-160

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 458.07  E-value: 6.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKygRDLIVYGSGLDA 80
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIED--DEVVVEGVGGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  81 FKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFD 160
Cdd:PRK02427  80 LKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKGGPIE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 161 YHLPIASAQVKSALIFSALQADEPSIIF--EKEATRNHLEI---MLNDFGADIK----TNGLCITVMPRPKLSGRTISIP 231
Cdd:PRK02427 160 YDGPVSSQFVKSLLLLAPLFAEGDTETTviEPLPSRPHTEItlrMLRAFGVEVEnvegWGYRRIVIKGGQRLRGQDITVP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 232 GDISSAAFFMVAASLLPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEItakEI 309
Cdd:PRK02427 240 GDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVRSSELKGIDI---DI 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 310 PNVIDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPklqiPENNLATHGDHR 389
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP----LAGVVDSYGDHR 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 488911987 390 IGMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:PRK02427 393 IAMAFAIAGLAAE--GPVTIDDPECVAKSFPDFFEDLASLGAN 433
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-429 1.38e-156

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: 449.15  E-value: 1.38e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKY-GRDLIVYGSGlD 79
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGVG-G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  80 AFKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAF 159
Cdd:COG0128   80 GLKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGP-LKGG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 160 DYHLP-IASAQVKSALIFSALQADEPSIIF-----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPG 232
Cdd:COG0128  159 EYEIPgSASSQFKSALLLAGPLAEGGLEITvtgelESKPYRDHTERMLRAFGVEVEVEGYrRFTVPGGQRYRPGDYTVPG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 233 DISSAAFFMVAASLLpNSCICLKKVGLNPT--RIGIISVLKRMNANIEVKKTSneaeaygdIIVRSSNLHAVEITAKEIP 310
Cdd:COG0128  239 DISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG--------ITVRGSPLKGIDIDLSDIP 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 311 nviDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQipENNLATHGDHRI 390
Cdd:COG0128  310 ---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLK--GAEVDSYGDHRI 384
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 488911987 391 GMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYL 429
Cdd:COG0128  385 AMAFAVAGLRAE--GPVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-429 1.61e-145

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: 420.81  E-value: 1.61e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGlDAFKDPKKPLNMG 91
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  92 NSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAFDYHLPIA-SAQV 170
Cdd:cd01556   80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGG-LKGGEVEIPGAvSSQF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 171 KSALIFSALQADEPSIIF----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAAS 245
Cdd:cd01556  159 KSALLLAAPLAEGPTTIIigelESKPYIDHTERMLRAFGAEVEVDGYrTITVKGGQKYKGPEYTVEGDASSAAFFLAAAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 246 LLPnSCICLKKVGLNPTRIGIISVLKRMNANIEVKKTsneaeayGDIIVRSSN-LHAVEITAKEIPnviDELPILTLAAS 324
Cdd:cd01556  239 ITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNE-------DTVVVESGGkLKGIDIDGNDIP---DEAPTLAVLAA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 325 LAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCP-KLQIPENNlaTHGDHRIGMMLAVAALLVDT 403
Cdd:cd01556  308 FAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPlKGAGVEVY--TYGDHRIAMSFAIAGLVAEG 385
                        410       420
                 ....*....|....*....|....*.
gi 488911987 404 SktITLNNPEAIKISYPNFFRDLDYL 429
Cdd:cd01556  386 G--VTIEDPECVAKSFPNFFEDLESL 409
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
12-422 6.11e-134

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 402.07  E-value: 6.11e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIK--KYGRdLIVYGSGLDAFKDPKKPLN 89
Cdd:PRK14806 312 VKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEgpHNGR-VTIHGVGLHGLKAPPGPLY 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  90 MGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFDYHLPIASAQ 169
Cdd:PRK14806 391 MGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIETGEEGRPPLSIRGGQRLKGIHYDLPMASAQ 470
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 170 VKSALIFSALQADEPSIIFEKEATRNHLEIMLNDFGADIKTNGLCITVMPRPKLSGRTISIPGDISSAAFFMVAASLLPN 249
Cdd:PRK14806 471 VKSCLLLAGLYAEGETSVTEPAPTRDHTERMLRGFGYPVKVEGNTISVEGGGKLTATDIEVPADISSAAFFLVAASIAEG 550
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 250 SCICLKKVGLNPTRIGIISVLKRMNANIEVkktSNEAEAYG----DIIVRSSNLHAVEITAKEIPNVIDELPILTLAASL 325
Cdd:PRK14806 551 SELTLEHVGINPTRTGVIDILKLMGADITL---ENEREVGGepvaDIRVRGARLKGIDIPEDQVPLAIDEFPVLFVAAAC 627
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 326 AKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCpklQIPENNLATHGDHRIGMMLAVAALlvDTSK 405
Cdd:PRK14806 628 AEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGG---IFGGGEVESHGDHRIAMSFSVASL--RASG 702
                        410
                 ....*....|....*..
gi 488911987 406 TITLNNPEAIKISYPNF 422
Cdd:PRK14806 703 PITIHDCANVATSFPNF 719
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-432 6.36e-116

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: 345.41  E-value: 6.36e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   14 GSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGldaFKDPKKPLNMGNS 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVG---GKEPQAELDLGNS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   94 GTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEF-SLTGNGTLPITVIGHPSLkAFDYHLPIASAQVKS 172
Cdd:TIGR01356  78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEIsSLEGGGSLPLTISGPLPG-GIVYISGSASSQYKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  173 ALIFSA--LQADEPSIIFEKEATRNHLEIMLNDFGADI----KTNGLCITVMPRPKLSGRTISIPGDISSAAFFMVAAsL 246
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFGveveRSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAA-A 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  247 LPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKtsneaeayGDIIVR-SSNLHAVEItakEIPNVIDELPILTLAA 323
Cdd:TIGR01356 236 ITGGRVTLENLGINPTQGDkaIIIVLEEMGADIEVEE--------DDLIVEgASGLKGIKI---DMDDMIDELPTLAVLA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  324 SLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATHGDHRIGMMLAVAALLVDt 403
Cdd:TIGR01356 305 AFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAV--VDTFGDHRIAMAFAVAGLVAE- 381
                         410       420
                  ....*....|....*....|....*....
gi 488911987  404 sKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:TIGR01356 382 -GEVLIDDPECVAKSFPSFFDVLERLGAN 409
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
12-426 5.17e-98

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 299.60  E-value: 5.17e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRD---LIVYGSGLDAFKDPKKPL 88
Cdd:pfam00275   6 LSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEksvVIVEGLGGSFEAPEDLVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   89 NMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGE-FSLTGNGTLPITVIGHPsLKAFDYHLPIAS 167
Cdd:pfam00275  86 DMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEiEGREGYNYAPLKVRGLR-LGGIHIDGDVSS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  168 AQVKSALIFSALQADEPSII--FEKEATRNHLEIMLNDFGADIKTNG--LCITVMPRPKLSGRTISIPGDISSAAFFMVA 243
Cdd:pfam00275 165 QFVTSLLMLAALLAEGTTTIenLASEPYIDDTENMLKKFGAKIEGSGteLSITVKGGEKLPGQEYRVEGDRSSAAYFLVA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  244 ASLLPnSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSneaeaygDIIVRSSNLHAVEItakEIPNVIDELPILTL 321
Cdd:pfam00275 245 AAITG-GTVTVENVGINSLQGDeaLLEILEKMGAEITQEEDA-------DIVVGPPGLRGKAV---DIRTAPDPAPTTAV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  322 AASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGM-VIDGCPKLQIPEnnLATHGDHRIGMMLAVAALL 400
Cdd:pfam00275 314 LAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAE--VDSYGDHRIAMALALAGLV 391
                         410       420
                  ....*....|....*....|....*.
gi 488911987  401 VDTSKTItlNNPEAIKISYPNFFRDL 426
Cdd:pfam00275 392 AEGETII--DDIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-429 1.88e-94

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: 290.27  E-value: 1.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGLDAFKDPKKPLNMG 91
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  92 NSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFDYHLPIASAQVK 171
Cdd:cd01554   81 NSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQVK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 172 SALIFSALQADEPSIIFE--KEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAASLLP 248
Cdd:cd01554  161 SALMFAALLAKGETVIIEaaKEPTINHTENMLQTFGGHISVQGTkKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAIAP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 249 NSCIClKKVGLNPTRIGIISVLKRMNANIEVkktsneAEAYgdIIVRSSNLHAVEITAKEIPNVIDELPILTLAASLAKG 328
Cdd:cd01554  241 GRLVL-QNVGINETRTGIIDVLRAMGAKIEI------GEDT--ISVESSDLKATEICGALIPRLIDELPIIALLALQAQG 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 329 RTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATHGDHRIGMMLAVAALLVDTskTIT 408
Cdd:cd01554  312 TTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGAR--VNTFGDHRIGMMTALAALVADG--EVE 387
                        410       420
                 ....*....|....*....|.
gi 488911987 409 LNNPEAIKISYPNFFRDLDYL 429
Cdd:cd01554  388 LDRAEAINTSYPSFFDDLESL 408
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-423 9.20e-33

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 130.98  E-value: 9.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGrDLIVYGSGLDA 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDG-GTCVVGGTRGA 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  81 FKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIgHPSLKAFD 160
Cdd:PRK11861 319 FTAKTADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRI-RPATISVD 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 161 YHLPI---ASAQVKSALIFSA--LQADEPSIIFEKEA---TRNHLEI---MLNDFGADIKTNGLCITVMP---RPKLSGr 226
Cdd:PRK11861 398 APIRVrgdVSSQFLTALLMTLplVKAKDGASVVEIDGeliSKPYIEItikLMARFGVTVERDGWQRFTVPagvRYRSPG- 476
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 227 TISIPGDISSAAFFMvAASLLPNSCICLKKVGLNPTR--IGIISVLKRMNANIEVKKTSNEAEAYGDiivRSSNLHAVEI 304
Cdd:PRK11861 477 TIMVEGDASSASYFL-AAGALGGGPLRVEGVGRASIQgdVGFANALMQMGANVTMGDDWIEVRGIGH---DHGRLAPIDM 552
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 305 TAKEIPnviDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQiPENNLAT 384
Cdd:PRK11861 553 DFNLIP---DAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLT-PNASIDT 628
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 488911987 385 HGDHRIGMMLAVAALlvdTSKTITLNNPEAIKISYPNFF 423
Cdd:PRK11861 629 YDDHRMAMCFSLVSL---GGVPVRINDPKCVGKTFPDYF 664
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
8-426 4.79e-28

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 117.07  E-value: 4.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987   8 QFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGlDAFKDPKKP 87
Cdd:PRK11860  11 PLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYRITGLG-GQFPVKQAD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  88 LNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAfdyHLPIA- 166
Cdd:PRK11860  90 LFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLRL---DAPIRv 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 167 ----SAQVKSALIFSALQADEPSIIFE---KEATRNHLEIMLN---DFGADIKTNGLCITVMP---RPKLSGrTISIPGD 233
Cdd:PRK11860 167 rgdvSSQFLTALLMALPLVARRDITIEvvgELISKPYIEITLNllaRFGIAVQREGWQRFTIPagsRYRSPG-EIHVEGD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 234 ISSAAFFMVAASLLPNSCICLKKVGLNPTR--IGIISVLKRMNANIEVKKTSNEAEAygdiivRSSNLHAVEITAKEIPn 311
Cdd:PRK11860 246 ASSASYFIAAGAIAGGAPVRIEGVGRDSIQgdIRFAEAARAMGAQVTSGPNWLEVRR------GAWPLKAIDLDCNHIP- 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 312 viDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDgcPKLQIPENNLA---THGDH 388
Cdd:PRK11860 319 --DAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVT--PPAQAADWKAAaihTYDDH 394
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 488911987 389 RIGMMLAVAALlvDTSKT-ITLNNPEAIKISYPNFFRDL 426
Cdd:PRK11860 395 RMAMCFSLAAF--NPAGLpVRINDPKCVAKTFPDYFEAL 431
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
12-426 1.61e-21

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 96.36  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRD--LIVYGSG--LDAFKDPKKP 87
Cdd:PLN02338  12 ISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENnrAVVEGCGgkFPVSGDSKED 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987  88 --LNMGNSGTTTRLLLGLLAGQSFNTCLVGD--ASLSKRPMYRVTNPITEVGGEFSLT-GNGTLPITVIGHPSLKAFDYH 162
Cdd:PLN02338  92 veLFLGNAGTAMRPLTAAVTAAGGNASYVLDgvPRMRERPIGDLVDGLKQLGADVECTlGTNCPPVRVNAAGGLPGGKVK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 163 LP-IASAQVKSALIFSALQA--DEPSIIFEKEATRNHLEI---MLNDFGADIKTNGlcitVMPRPKLSG-------RTIS 229
Cdd:PLN02338 172 LSgSISSQYLTALLMAAPLAlgDVEIEIVDKLISVPYVEMtlkLMERFGVSVEHSD----SWDRFFIKGgqkykspGNAY 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 230 IPGDISSAAFFMVAASLLPNScICLKKVGLNPTR--IGIISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEITAK 307
Cdd:PLN02338 248 VEGDASSASYFLAGAAITGGT-VTVEGCGTTSLQgdVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKAIDVNMN 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 308 EIPNVidelpILTLA--ASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATH 385
Cdd:PLN02338 327 KMPDV-----AMTLAvvALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAE--IDTY 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 488911987 386 GDHRIGMMLAVAAlLVDTSktITLNNPEAIKISYPNFFRDL 426
Cdd:PLN02338 400 DDHRMAMAFSLAA-CGDVP--VTINDPGCTRKTFPTYFDVL 437
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
200-399 7.64e-09

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: 57.10  E-value: 7.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 200 MLNDFGADIK---TNGLCIT-VmprPKLSGRTISIPGDISSAAFFMVAASLLpNSCICLKKVglNPTRIG-IISVLKRMN 274
Cdd:cd01555  188 FLNKMGAKIEgagTDTIRIEgV---ERLHGAEHTVIPDRIEAGTFLVAAAIT-GGDITVENV--IPEHLEaVLAKLREMG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 275 ANIEVKKTSneaeaygdIIVRSS--NLHAVEITAKEIPNVI-DELPILTLAASLAKGRTIISgagelrvkET---DRISV 348
Cdd:cd01555  262 AKIEIGEDG--------IRVDGDggRLKAVDIETAPYPGFPtDLQAQFMALLTQAEGTSVIT--------ETifeNRFMH 325
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488911987 349 VAaELKKLGARIQEKSDGMVIDGCPKLQIPEnNLAThgDHRIGMMLAVAAL 399
Cdd:cd01555  326 VD-ELNRMGADIKVEGNTAIIRGVTKLSGAP-VMAT--DLRAGAALVLAGL 372
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
181-421 1.07e-05

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 47.54  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 181 ADEPSIIfeKEATrnhleiMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAASllpnscICLKKVGL 259
Cdd:PRK12830 186 AKEPEII--DVAT------LLNNMGANIKGAGTdVIRIEGVDELHGCRHTVIPDRIEAGTYMILAA------ACGGGVTI 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 260 N---PTRI-GIISVLKRMNANIEVKKTSneaeaygdIIVRSS-NLHAVEITAKEIPNVIDEL--PILTLAaSLAKGRTII 332
Cdd:PRK12830 252 NnviPEHLeSFIAKLEEMGVRVEVNEDS--------IFVEKQgNLKAVDIKTLPYPGFATDLqqPLTPLL-LKANGRSVV 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 333 SGA-GELRVKETDrisvvaaELKKLGARIQEKSDGMVIDGCPKLQIPENNlAThgDHRIGMMLAVAALLVDTSKTITlnN 411
Cdd:PRK12830 323 TDTiYEKRFKHVD-------ELKRMGANIKVEGRSAIITGPSKLTGAKVK-AT--DLRAGAALVIAGLMAEGVTEIT--N 390
                        250
                 ....*....|
gi 488911987 412 PEAIKISYPN 421
Cdd:PRK12830 391 IEHIDRGYSN 400
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
267-390 1.13e-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: 44.21  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 267 ISVLKRMNANIEVKKtsneaeayGDIIVRSSNLHAVEI-------TAKEipNVIdelpiltLAASLAKGRTIISGAGelr 339
Cdd:COG0766  128 LKGLEALGAEIEIEH--------GYIEARAGRLKGARIyldfpsvGATE--NIM-------MAAVLAEGTTVIENAA--- 187
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488911987 340 vKE---TDrisvVAAELKKLGARIQ-EKSDGMVIDGCPKLqipennlatHG-DHRI 390
Cdd:COG0766  188 -REpeiVD----LANFLNAMGAKIEgAGTDTITIEGVEKL---------HGaEHTV 229
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
267-411 3.51e-04

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 42.71  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 267 ISVLKRMNANIEVKKTSNEAEAYGdiivrssNLHAVEI-------TAKEipNVIdelpiltLAASLAKGRTIISGAGelr 339
Cdd:PRK09369 128 LKGLEALGAEIEIEHGYVEAKADG-------RLKGAHIvldfpsvGATE--NIL-------MAAVLAEGTTVIENAA--- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 340 vKETDrisVV--AAELKKLGARIQ-EKSDGMVIDGCPKLqipennlatHG-DHRIG---------MMLAVAallvdTSKT 406
Cdd:PRK09369 189 -REPE---IVdlANFLNKMGAKISgAGTDTITIEGVERL---------HGaEHTVIpdrieagtfLVAAAI-----TGGD 250

                 ....*
gi 488911987 407 ITLNN 411
Cdd:PRK09369 251 VTIRG 255
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
195-361 1.84e-03

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


Pssm-ID: 440529  Cd Length: 416  Bit Score: 40.35  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 195 NHLEIMLN---DFGADIKTNGLCITVMPRPKLSgrtisiPGDISSA----------AFFMVAASLLPNSCICLKKVglNP 261
Cdd:COG0766  258 EHLEAVLAklrEAGVEIEEGDDGIRVRGPGRLK------AVDIKTApypgfptdlqAQFMALLTQAEGTSVITETV--FE 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 262 TRIGIISVLKRMNANIEVKKTSneaeaygdIIVR-SSNLHAVEITAkeipnvidelPI------LTLAASLAKGRTIISG 334
Cdd:COG0766  330 NRFMHVDELNRMGADIKLDGHT--------AIVRgVTKLSGAPVMA----------TDlragaaLVLAGLAAEGETVIDN 391
                        170       180       190
                 ....*....|....*....|....*....|.
gi 488911987 335 AGELrvketDR----IsvvAAELKKLGARIQ 361
Cdd:COG0766  392 IYHI-----DRgyenL---EEKLRALGADIE 414
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
267-376 5.23e-03

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


Pssm-ID: 238796  Cd Length: 400  Bit Score: 38.99  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 267 ISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEITAKEipNVIdelpiltLAASLAKGRTIISGAGelrvKETDrI 346
Cdd:cd01555  117 LKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATE--NIM-------MAAVLAEGTTVIENAA----REPE-I 182
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488911987 347 SVVAAELKKLGARIQ-EKSDGMVIDGCPKLQ 376
Cdd:cd01555  183 VDLANFLNKMGAKIEgAGTDTIRIEGVERLH 213
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH