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Conserved domains on  [gi|918229393|ref|WP_052362525|]
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3-phosphoshikimate 1-carboxyvinyltransferase [Geminisphaera colitermitum]

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
Gene Ontology:  GO:0009073|GO:0008652|GO:0003866|GO:0009423
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]; ...
 20-494 3.27e-136

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: 399.85  E-value: 3.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  20 DLLPIKPfRHPVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEAaGTARVEGQEN 99
Cdd:COG0128    2 SSLTIAP-PSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 100 ALKgngvggggeardtqeVQAVELFVGLAGTAARFLTALCAAArGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGE 179
Cdd:COG0128   80 GLK---------------EPDAVLDCGNSGTTMRLLTGLLALQ-PGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 180 eGFFPIEIHARGLRGGPVTIDASESSQMLSAVLMVAPLADAPVEVTIAGG-VRWPFVQMTTRLMEHFGQPaVQRLADDRL 258
Cdd:COG0128  144 -GYLPLTIRGGPLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGElESKPYRDHTERMLRAFGVE-VEVEGYRRF 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 259 RVVSGHPwgLQAAAaggrrgernavYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVVTE 338
Cdd:COG0128  222 TVPGGQR--YRPGD-----------YTVPGDISSAAFFLAAAAITGSEV--TVEGVGLNSTQGDTGILDILKEMGADIEI 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 339 TEGGggrgLHVAfsveklaggataGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELR 418
Cdd:COG0128  287 ENDG----ITVR------------GSPLKGIDIDLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELR 350

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 918229393 419 RLGQQVIEEEDSLEIHPRPLLAGQEIETYGDHRFAMSFGILGchdLHGDGrpWLSIKDPACCAKTFPHFFELLESL 494
Cdd:COG0128  351 KLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAG---LRAEG--PVTIDDAECVAKSFPDFFELLESL 421
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 20-494 3.27e-136

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: 399.85  E-value: 3.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  20 DLLPIKPfRHPVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEAaGTARVEGQEN 99
Cdd:COG0128    2 SSLTIAP-PSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 100 ALKgngvggggeardtqeVQAVELFVGLAGTAARFLTALCAAArGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGE 179
Cdd:COG0128   80 GLK---------------EPDAVLDCGNSGTTMRLLTGLLALQ-PGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 180 eGFFPIEIHARGLRGGPVTIDASESSQMLSAVLMVAPLADAPVEVTIAGG-VRWPFVQMTTRLMEHFGQPaVQRLADDRL 258
Cdd:COG0128  144 -GYLPLTIRGGPLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGElESKPYRDHTERMLRAFGVE-VEVEGYRRF 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 259 RVVSGHPwgLQAAAaggrrgernavYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVVTE 338
Cdd:COG0128  222 TVPGGQR--YRPGD-----------YTVPGDISSAAFFLAAAAITGSEV--TVEGVGLNSTQGDTGILDILKEMGADIEI 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 339 TEGGggrgLHVAfsveklaggataGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELR 418
Cdd:COG0128  287 ENDG----ITVR------------GSPLKGIDIDLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELR 350

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 918229393 419 RLGQQVIEEEDSLEIHPRPLLAGQEIETYGDHRFAMSFGILGchdLHGDGrpWLSIKDPACCAKTFPHFFELLESL 494
Cdd:COG0128  351 KLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAG---LRAEG--PVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 31-494 2.64e-123

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: 366.50  E-value: 2.64e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  31 VRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEadEAAGTARVEGQENALkgngvgggg 110
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIE--EEGGTVEIVGGGGLG--------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 111 eardtqEVQAVELFVGLAGTAARFLTALcAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIeIHAR 190
Cdd:cd01556   70 ------LPPEAVLDCGNSGTTMRLLTGL-LALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL-IGGG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 191 GLRGGPVTIDASESSQMLSAVLMVAPLADAPVEVTIAGGVRWPFVQMTTRLMEHFGQPaVQRLADDRLRVVSGHPWglqa 270
Cdd:cd01556  142 GLKGGEVEIPGAVSSQFKSALLLAAPLAEGPTTIIIGELESKPYIDHTERMLRAFGAE-VEVDGYRTITVKGGQKY---- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 271 aaaggrrgeRNAVYAIEPDATAASYFLALPLVTGGELdlpgLRGPGGGLQGDTRFVSVLQRVGAVVTETEGGGGRglhva 350
Cdd:cd01556  217 ---------KGPEYTVEGDASSAAFFLAAAAITGSEI----VIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVV----- 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 351 fsveklaggATAGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIEEEDS 430
Cdd:cd01556  279 ---------VESGGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDG 349

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918229393 431 LEIHPRPL-LAGQEIETYGDHRFAMSFGILGCHDLHGdgrpwLSIKDPACCAKTFPHFFELLESL 494
Cdd:cd01556  350 LIIEGGPLkGAGVEVYTYGDHRIAMSFAIAGLVAEGG-----VTIEDPECVAKSFPNFFEDLESL 409
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 17-499 2.05e-111

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 336.73  E-value: 2.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  17 SLPDLLPIKPfrHPVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADeaagTARVEG 96
Cdd:PRK02427   1 MMMMLLIIPP--SPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIEDD----EVVVEG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  97 QENalkgngvggggeaRDTQEVQAVeLFVGLAGTAARFLTALcAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRC 176
Cdd:PRK02427  75 VGG-------------GGLKEPEDV-LDCGNSGTTMRLLTGL-LALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 177 tGEEGFFPIEIHArGLRGGPVTIDASESSQMLSAVLMVAPL-ADAPVEVTIAGGV--RwPFVQMTTRLMEHFGqpaVQRL 253
Cdd:PRK02427 140 -RDEGYLPLTIRG-GKKGGPIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLpsR-PHTEITLRMLRAFG---VEVE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 254 ADDRLRVVSGHPWGLQAAAAGgrrgernaVYAIEPDATAASYFLALPLVTGGElDLPGLRGPGGGLQGDTRFVSVLQRVG 333
Cdd:PRK02427 214 NVEGWGYRRIVIKGGQRLRGQ--------DITVPGDPSSAAFFLAAAAITGGS-EVTITNVGLNSTQGGKAIIDVLEKMG 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 334 AVVTETEGGGGRglhvafsvEKLAGGATAGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGM 413
Cdd:PRK02427 285 ADIEIENEREGG--------EPVGDIRVRSSELKGIDIDIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAM 356

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 414 ARELRRLGQQVIEEEDSLEIHPRPLLAGqeIETYGDHRFAMSFGILGCHDLHGdgrpwLSIKDPACCAKTFPHFFELLES 493
Cdd:PRK02427 357 ATELRKLGAEVEETEDGLIITGGPLAGV--VDSYGDHRIAMAFAIAGLAAEGP-----VTIDDPECVAKSFPDFFEDLAS 429


                 ....*.
gi 918229393 494 LRKKSS 499
Cdd:PRK02427 430 LGANIE 435
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 33-494 1.38e-101

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: 310.75  E-value: 1.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393   33 GEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEadEAAGTARVEGQENALKgngvggggea 112
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIE--DGGEVAVIEGVGGKEP---------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  113 rdtqevqAVELFVGLAGTAARFLTALcAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIEIHArGL 192
Cdd:TIGR01356  69 -------QAELDLGNSGTTARLLTGV-LALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISG-PL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  193 RGGPVTIDASESSQMLSAVLMVAPlADAPVEVTIAGG--VRWPFVQMTTRLMEHFGqpAVQRLADDRLRVVSGhpwglqa 270
Cdd:TIGR01356 140 PGGIVYISGSASSQYKSALLLAAP-ALQAVGITIVGEplKSRPYIEITLDLLGSFG--VEVERSDGRKIVVPG------- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  271 aaAGGRRGERnavYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVVTETEGGGGRGLHVA 350
Cdd:TIGR01356 210 --GQKYGPQG---YDVPGDYSSAAFFLAAAAITGGRV--TLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASG 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  351 FSveklaggataggtrtGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIEEEDS 430
Cdd:TIGR01356 283 LK---------------GIKIDMDDMIDELPTLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDG 347

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918229393  431 LEIHPRPLLAGQEIETYGDHRFAMSFGILGchdLHGDGRpwLSIKDPACCAKTFPHFFELLESL 494
Cdd:TIGR01356 348 LYIRGKKELKGAVVDTFGDHRIAMAFAVAG---LVAEGE--VLIDDPECVAKSFPSFFDVLERL 406
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
30-491 5.93e-84

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 265.70  E-value: 5.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393   30 PVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEAAGTA-RVEGQENALKGNGVGG 108
Cdd:pfam00275   5 RLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVvIVEGLGGSFEAPEDLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  109 ggeardtqevqaveLFVGLAGTAARFLTALCAAARGGVYrIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIEIh 188
Cdd:pfam00275  85 --------------LDMGNSGTALRPLTGRLALQSGEVV-LPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKV- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  189 aRGLRGGPVTIDASESSQMLSAVLMVAPLAdAPVEVTIAGGVRWPFVQMTTRLMEHFGQPavqrladdrlrvVSGHPWGL 268
Cdd:pfam00275 149 -RGLRLGGIHIDGDVSSQFVTSLLMLAALL-AEGTTTIENLASEPYIDDTENMLKKFGAK------------IEGSGTEL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  269 QAAAAGGRRGERnAVYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVVTETEggggrglh 348
Cdd:pfam00275 215 SITVKGGEKLPG-QEYRVEGDRSSAAYFLVAAAITGGTV--TVENVGINSLQGDEALLEILEKMGAEITQEE-------- 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  349 vaFSVEKLAGGAtaggtRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIEEE 428
Cdd:pfam00275 284 --DADIVVGPPG-----LRGKAVDIRTAPDPAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELP 356

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918229393  429 DSLEIHP-RPLLAGQEIETYGDHRFAMSFGILGCHdLHGDGRpwlsIKDPACCAKTFPHFFELL 491
Cdd:pfam00275 357 DGLIIIPaVKELKGAEVDSYGDHRIAMALALAGLV-AEGETI----IDDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 20-494 3.27e-136

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: 399.85  E-value: 3.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  20 DLLPIKPfRHPVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEAaGTARVEGQEN 99
Cdd:COG0128    2 SSLTIAP-PSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 100 ALKgngvggggeardtqeVQAVELFVGLAGTAARFLTALCAAArGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGE 179
Cdd:COG0128   80 GLK---------------EPDAVLDCGNSGTTMRLLTGLLALQ-PGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 180 eGFFPIEIHARGLRGGPVTIDASESSQMLSAVLMVAPLADAPVEVTIAGG-VRWPFVQMTTRLMEHFGQPaVQRLADDRL 258
Cdd:COG0128  144 -GYLPLTIRGGPLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGElESKPYRDHTERMLRAFGVE-VEVEGYRRF 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 259 RVVSGHPwgLQAAAaggrrgernavYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVVTE 338
Cdd:COG0128  222 TVPGGQR--YRPGD-----------YTVPGDISSAAFFLAAAAITGSEV--TVEGVGLNSTQGDTGILDILKEMGADIEI 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 339 TEGGggrgLHVAfsveklaggataGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELR 418
Cdd:COG0128  287 ENDG----ITVR------------GSPLKGIDIDLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELR 350

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 918229393 419 RLGQQVIEEEDSLEIHPRPLLAGQEIETYGDHRFAMSFGILGchdLHGDGrpWLSIKDPACCAKTFPHFFELLESL 494
Cdd:COG0128  351 KLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAG---LRAEG--PVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 31-494 2.64e-123

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: 366.50  E-value: 2.64e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  31 VRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEadEAAGTARVEGQENALkgngvgggg 110
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIE--EEGGTVEIVGGGGLG--------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 111 eardtqEVQAVELFVGLAGTAARFLTALcAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIeIHAR 190
Cdd:cd01556   70 ------LPPEAVLDCGNSGTTMRLLTGL-LALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL-IGGG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 191 GLRGGPVTIDASESSQMLSAVLMVAPLADAPVEVTIAGGVRWPFVQMTTRLMEHFGQPaVQRLADDRLRVVSGHPWglqa 270
Cdd:cd01556  142 GLKGGEVEIPGAVSSQFKSALLLAAPLAEGPTTIIIGELESKPYIDHTERMLRAFGAE-VEVDGYRTITVKGGQKY---- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 271 aaaggrrgeRNAVYAIEPDATAASYFLALPLVTGGELdlpgLRGPGGGLQGDTRFVSVLQRVGAVVTETEGGGGRglhva 350
Cdd:cd01556  217 ---------KGPEYTVEGDASSAAFFLAAAAITGSEI----VIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVV----- 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 351 fsveklaggATAGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIEEEDS 430
Cdd:cd01556  279 ---------VESGGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDG 349

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918229393 431 LEIHPRPL-LAGQEIETYGDHRFAMSFGILGCHDLHGdgrpwLSIKDPACCAKTFPHFFELLESL 494
Cdd:cd01556  350 LIIEGGPLkGAGVEVYTYGDHRIAMSFAIAGLVAEGG-----VTIEDPECVAKSFPNFFEDLESL 409
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 17-499 2.05e-111

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 336.73  E-value: 2.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  17 SLPDLLPIKPfrHPVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADeaagTARVEG 96
Cdd:PRK02427   1 MMMMLLIIPP--SPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIEDD----EVVVEG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  97 QENalkgngvggggeaRDTQEVQAVeLFVGLAGTAARFLTALcAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRC 176
Cdd:PRK02427  75 VGG-------------GGLKEPEDV-LDCGNSGTTMRLLTGL-LALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 177 tGEEGFFPIEIHArGLRGGPVTIDASESSQMLSAVLMVAPL-ADAPVEVTIAGGV--RwPFVQMTTRLMEHFGqpaVQRL 253
Cdd:PRK02427 140 -RDEGYLPLTIRG-GKKGGPIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLpsR-PHTEITLRMLRAFG---VEVE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 254 ADDRLRVVSGHPWGLQAAAAGgrrgernaVYAIEPDATAASYFLALPLVTGGElDLPGLRGPGGGLQGDTRFVSVLQRVG 333
Cdd:PRK02427 214 NVEGWGYRRIVIKGGQRLRGQ--------DITVPGDPSSAAFFLAAAAITGGS-EVTITNVGLNSTQGGKAIIDVLEKMG 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 334 AVVTETEGGGGRglhvafsvEKLAGGATAGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGM 413
Cdd:PRK02427 285 ADIEIENEREGG--------EPVGDIRVRSSELKGIDIDIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAM 356

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 414 ARELRRLGQQVIEEEDSLEIHPRPLLAGqeIETYGDHRFAMSFGILGCHDLHGdgrpwLSIKDPACCAKTFPHFFELLES 493
Cdd:PRK02427 357 ATELRKLGAEVEETEDGLIITGGPLAGV--VDSYGDHRIAMAFAIAGLAAEGP-----VTIDDPECVAKSFPDFFEDLAS 429


                 ....*.
gi 918229393 494 LRKKSS 499
Cdd:PRK02427 430 LGANIE 435
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 33-494 1.38e-101

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: 310.75  E-value: 1.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393   33 GEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEadEAAGTARVEGQENALKgngvggggea 112
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIE--DGGEVAVIEGVGGKEP---------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  113 rdtqevqAVELFVGLAGTAARFLTALcAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIEIHArGL 192
Cdd:TIGR01356  69 -------QAELDLGNSGTTARLLTGV-LALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISG-PL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  193 RGGPVTIDASESSQMLSAVLMVAPlADAPVEVTIAGG--VRWPFVQMTTRLMEHFGqpAVQRLADDRLRVVSGhpwglqa 270
Cdd:TIGR01356 140 PGGIVYISGSASSQYKSALLLAAP-ALQAVGITIVGEplKSRPYIEITLDLLGSFG--VEVERSDGRKIVVPG------- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  271 aaAGGRRGERnavYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVVTETEGGGGRGLHVA 350
Cdd:TIGR01356 210 --GQKYGPQG---YDVPGDYSSAAFFLAAAAITGGRV--TLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASG 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  351 FSveklaggataggtrtGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIEEEDS 430
Cdd:TIGR01356 283 LK---------------GIKIDMDDMIDELPTLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDG 347

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918229393  431 LEIHPRPLLAGQEIETYGDHRFAMSFGILGchdLHGDGRpwLSIKDPACCAKTFPHFFELLESL 494
Cdd:TIGR01356 348 LYIRGKKELKGAVVDTFGDHRIAMAFAVAG---LVAEGE--VLIDDPECVAKSFPSFFDVLERL 406
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
 21-496 6.23e-97

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 300.13  E-value: 6.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  21 LLPIKPfrhpVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEAAGTARVEGQENA 100
Cdd:PLN02338   6 LQPIKE----ISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGGK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 101 LKGNgvggggeardTQEVQAVELFVGLAGTAARFLTA-LCAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGE 179
Cdd:PLN02338  82 FPVS----------GDSKEDVELFLGNAGTAMRPLTAaVTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 180 EGFFPIEIHAR-GLRGGPVTIDASESSQMLSAVLMVAPLADAPVEVTIAGG-VRWPFVQMTTRLMEHFGQpAVQRLAD-D 256
Cdd:PLN02338 152 TNCPPVRVNAAgGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKlISVPYVEMTLKLMERFGV-SVEHSDSwD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 257 RLRVVSGHPWglqaaaaggrRGERNAVyaIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVV 336
Cdd:PLN02338 231 RFFIKGGQKY----------KSPGNAY--VEGDASSASYFLAGAAITGGTV--TVEGCGTTSLQGDVKFAEVLEKMGAKV 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 337 TETEGgggrglhvAFSVEKLAGGATAGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARE 416
Cdd:PLN02338 297 EWTEN--------SVTVTGPPRDAFGGKHLKAIDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTE 368

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 417 LRRLGQQVIEEEDSLEIHPRPLLAGQEIETYGDHRFAMSFGILGCHDLHgdgrpwLSIKDPACCAKTFPHFFELLESLRK 496
Cdd:PLN02338 369 LRKLGATVEEGPDYCIITPPKKLKPAEIDTYDDHRMAMAFSLAACGDVP------VTINDPGCTRKTFPTYFDVLESIAK 442
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
30-491 5.93e-84

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 265.70  E-value: 5.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393   30 PVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEAAGTA-RVEGQENALKGNGVGG 108
Cdd:pfam00275   5 RLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVvIVEGLGGSFEAPEDLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  109 ggeardtqevqaveLFVGLAGTAARFLTALCAAARGGVYrIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIEIh 188
Cdd:pfam00275  85 --------------LDMGNSGTALRPLTGRLALQSGEVV-LPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKV- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  189 aRGLRGGPVTIDASESSQMLSAVLMVAPLAdAPVEVTIAGGVRWPFVQMTTRLMEHFGQPavqrladdrlrvVSGHPWGL 268
Cdd:pfam00275 149 -RGLRLGGIHIDGDVSSQFVTSLLMLAALL-AEGTTTIENLASEPYIDDTENMLKKFGAK------------IEGSGTEL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  269 QAAAAGGRRGERnAVYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGAVVTETEggggrglh 348
Cdd:pfam00275 215 SITVKGGEKLPG-QEYRVEGDRSSAAYFLVAAAITGGTV--TVENVGINSLQGDEALLEILEKMGAEITQEE-------- 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  349 vaFSVEKLAGGAtaggtRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIEEE 428
Cdd:pfam00275 284 --DADIVVGPPG-----LRGKAVDIRTAPDPAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELP 356

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918229393  429 DSLEIHP-RPLLAGQEIETYGDHRFAMSFGILGCHdLHGDGRpwlsIKDPACCAKTFPHFFELL 491
Cdd:pfam00275 357 DGLIIIPaVKELKGAEVDSYGDHRIAMALALAGLV-AEGETI----IDDIECTDRSFPDFEEKL 415
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
31-494 3.46e-78

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 257.28  E-value: 3.46e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  31 VRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEadEAAGTARVEGQENALKgngvgggg 110
Cdd:PRK11860  15 AGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVE--QLGDTYRITGLGGQFP-------- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 111 eardtqeVQAVELFVGLAGTAARFLTALCAAArGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIEIHAR 190
Cdd:PRK11860  85 -------VKQADLFLGNAGTAMRPLTAALALL-GGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 191 GLR-GGPVTIDASESSQMLSAVLMVAPLAdAPVEVTIA--GG-VRWPFVQMTTRLMEHFGQpAVQRLADDRLRVvsghpw 266
Cdd:PRK11860 157 PLRlDAPIRVRGDVSSQFLTALLMALPLV-ARRDITIEvvGElISKPYIEITLNLLARFGI-AVQREGWQRFTI------ 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 267 glqaaAAGGRRGERNAVYaIEPDATAASYFLALPLVTGGElDLPGLRGPGGGLQGDTRFVSVLQRVGAVVTETEGgggrg 346
Cdd:PRK11860 229 -----PAGSRYRSPGEIH-VEGDASSASYFIAAGAIAGGA-PVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPN----- 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 347 lhvAFSVEKLAGGATAggtrtgVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIE 426
Cdd:PRK11860 297 ---WLEVRRGAWPLKA------IDLDCNHIPDAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEE 367

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918229393 427 EEDSLEIHPrPLLAGQ----EIETYGDHRFAMSFGILGCHDLHGDGRpwlsIKDPACCAKTFPHFFELLESL 494
Cdd:PRK11860 368 GADYIRVTP-PAQAADwkaaAIHTYDDHRMAMCFSLAAFNPAGLPVR----INDPKCVAKTFPDYFEALFSV 434
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 20-494 4.41e-56

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 198.39  E-value: 4.41e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  20 DLLPIKPFRHpVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADeaAGTARVEGQEN 99
Cdd:PRK11861 241 EHLDLGPFSH-AQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRD--GGTCVVGGTRG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 100 ALKgngvggggeardtqeVQAVELFVGLAGTAARFLTAlCAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGE 179
Cdd:PRK11861 318 AFT---------------AKTADLFLGNAGTAVRPLTA-ALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGN 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 180 EGFFPIEIHARGLR-GGPVTIDASESSQMLSAVLMVAPLA---DAPVEVTIAGG-VRWPFVQMTTRLMEHFGQpAVQRLA 254
Cdd:PRK11861 382 EGFPPLRIRPATISvDAPIRVRGDVSSQFLTALLMTLPLVkakDGASVVEIDGElISKPYIEITIKLMARFGV-TVERDG 460

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 255 DDRLRVvsghPWGLQAAAAGgrrgernaVYAIEPDATAASYFLALPLVTGGELdlPGLRGPGGGLQGDTRFVSVLQRVGA 334
Cdd:PRK11861 461 WQRFTV----PAGVRYRSPG--------TIMVEGDASSASYFLAAGALGGGPL--RVEGVGRASIQGDVGFANALMQMGA 526

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 335 VVTETEGGGgrglhvafsveKLAGGATAGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMA 414
Cdd:PRK11861 527 NVTMGDDWI-----------EVRGIGHDHGRLAPIDMDFNLIPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMA 595

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 415 RELRRLGQQVIEEEDSLEIHPRP-LLAGQEIETYGDHRFAMSFGILGChdlhgDGRPwLSIKDPACCAKTFPHFFELLES 493
Cdd:PRK11861 596 TELRKVGATVEEGADYLVVTPPAqLTPNASIDTYDDHRMAMCFSLVSL-----GGVP-VRINDPKCVGKTFPDYFDRFLA 669


                 .
gi 918229393 494 L 494
Cdd:PRK11861 670 L 670
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
 31-494 3.60e-52

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: 182.03  E-value: 3.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  31 VRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGfrVEADEAAGTARVEGQENALKGNGvgggg 110
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLG--VEIEDKDGVITIQGVGMAGLKAP----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 111 eardtqevqAVELFVGLAGTAARFLTALCAAARGGVyRIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEGFFPIEIHAR 190
Cdd:cd01554   74 ---------QNALNLGNSGTAIRLISGVLAGADFEV-ELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 191 gLRGGPVTIDASESSQMLSAVLMVAPLadAPVEVTIAGGVRWPFVQMTTRLMEHFGqpaVQRLADDRLRVVSGHPWGLQA 270
Cdd:cd01554  144 -NLGPIHYEDPIASAQVKSALMFAALL--AKGETVIIEAAKEPTINHTENMLQTFG---GHISVQGTKKIVVQGPQKLTG 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 271 aaaggrrgernAVYAIEPDATAASYFLALPLVTGGELdlpgLRGPGGGLQGDTRFVSVLQRVGAVVTETEGGGGRGLHVA 350
Cdd:cd01554  218 -----------QKYVVPGDISSAAFFLVAAAIAPGRL----VLQNVGINETRTGIIDVLRAMGAKIEIGEDTISVESSDL 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 351 FSVEklaggataggTRTGVTENFNEFSDTFLTLAAIApllDGPTRISGIAHTRKQETDRVAGMARELRRLGQQVIEEEDS 430
Cdd:cd01554  283 KATE----------ICGALIPRLIDELPIIALLALQA---QGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADG 349

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918229393 431 LEIHPRPLLAGQEIETYGDHRFAMSFGILGChdlHGDGRpwLSIKDPACCAKTFPHFFELLESL 494
Cdd:cd01554  350 MIIKGKEKLHGARVNTFGDHRIGMMTALAAL---VADGE--VELDRAEAINTSYPSFFDDLESL 408
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 30-490 2.44e-18

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 88.13  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  30 PVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEaAGTARVEGQE-NALKGNGVGg 108
Cdd:PRK14806 311 AVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEGPH-NGRVTIHGVGlHGLKAPPGP- 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 109 ggeardtqevqaveLFVGLAGTAARFLTALCAAARGGVyRIDGIAQMRKRPMRGLIEALRTLGADIRcTGEEGFFPIEIH 188
Cdd:PRK14806 389 --------------LYMGNSGTSMRLLSGLLAAQSFDS-VLTGDASLSKRPMERVAKPLREMGAVIE-TGEEGRPPLSIR 452

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 189 ArGLRGGPVTIDAS-ESSQMLSAVLMVAPLADAPVEVTIAGGVRwpfvQMTTRLMEHFGQPaVQRLAdDRLRVVSGHPwg 267
Cdd:PRK14806 453 G-GQRLKGIHYDLPmASAQVKSCLLLAGLYAEGETSVTEPAPTR----DHTERMLRGFGYP-VKVEG-NTISVEGGGK-- 523

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 268 LQAAAaggrrgernavYAIEPDATAASYFLALPLVTGGEldlpgLRGPGGGLQGDTR--FVSVLQRVGAVVTeteggggr 345
Cdd:PRK14806 524 LTATD-----------IEVPADISSAAFFLVAASIAEGS-----ELTLEHVGINPTRtgVIDILKLMGADIT-------- 579

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 346 glhvaFSVEKLAGGATAGGTRTG-------------VTENFNEFSDTFLTlAAIApllDGPTRISGIAHTRKQETDRVAG 412
Cdd:PRK14806 580 -----LENEREVGGEPVADIRVRgarlkgidipedqVPLAIDEFPVLFVA-AACA---EGRTVLTGAEELRVKESDRIQV 650

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918229393 413 MARELRRLGQQVIEEEDSLEIHPRpLLAGQEIETYGDHRFAMSFGILGchdLHGDGRpwLSIKDPACCAKTFPHFFEL 490
Cdd:PRK14806 651 MADGLKTLGIDCEPTPDGIIIEGG-IFGGGEVESHGDHRIAMSFSVAS---LRASGP--ITIHDCANVATSFPNFLEL 722
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
 287-494 3.77e-05

This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.


Pssm-ID: 238794  Cd Length: 211  Bit Score: 44.96  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 287 EPDATAASYFLALPLVTGGEL---DLPGLRGPGGGLQGDTRFVSVLQRV-GAVVTETEGGGGRGLHVafsveklAGGATA 362
Cdd:cd01553    7 KGGGQILRSFLVLAAISGGPItvtGIRPDRAKPGLLRQHLTFLKALEKIcGATVEGGELGSDRISFR-------PGTVRG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 363 GGTRT--GVTENFNEFSDTFLTLAAIApllDGPTRISGIAHTRKQE----TDRVAGMARELRRLGQQVIEEEDSL----- 431
Cdd:cd01553   80 GDVRFaiGSAGSCTDVLQTILPLLLFA---KGPTRLTVTGGTDNPSappaDFIRFVLEPELAKIGAHQEETLLRHgfypa 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 432 -------EIHPRPLLAGQEIetygdhRFAMSFGILGCHDlhgdgrpwlSIKDPACCAKTFPHFFELLESL 494
Cdd:cd01553  157 gggvvatEVSPVEKLNTAQL------RQLVLPMLLASGA---------VEFTVAHPSCHLLTNFAVLEAL 211
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
 32-212 3.62e-04

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


Pssm-ID: 238796  Cd Length: 400  Bit Score: 42.85  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  32 RGEVLLPGSKsltNRAL-LLAA--LCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEaagtarvegqENALKGngvgg 108
Cdd:cd01555    2 SGEVRISGAK---NAALpILAAalLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEG----------ENTLVI----- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 109 ggearDTQEVQAVELFVGLAGTA-ARFLtaLCAA--ARGGVYRI-----DGIAqmrKRPMRGLIEALRTLGADIrcTGEE 180
Cdd:cd01555   64 -----DASNINSTEAPYELVRKMrASIL--VLGPllARFGEARVslpggCAIG---ARPVDLHLKGLEALGAKI--EIED 131

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 918229393 181 GFFPIEiHARGLRGGPVTID-----ASESSqMLSAVL 212
Cdd:cd01555  132 GYVEAK-AAGRLKGARIYLDfpsvgATENI-MMAAVL 166
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 29-219 8.75e-04

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


Pssm-ID: 440529  Cd Length: 416  Bit Score: 41.51  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  29 HPVRGEVLLPGSKsltNRAL-LLAA--LCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEaAGTARVegqenalkgng 105
Cdd:COG0766   10 KPLSGEVRISGAK---NAALpILAAalLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDD-GGTLTI----------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 106 vggggearDTQEVQAVELFVGLAGTA-ARFLtaLCAA--ARGGVYRI-----DGIAqmrKRPMRGLIEALRTLGADIrcT 177
Cdd:COG0766   75 --------DASNINSTEAPYELVRKMrASIL--VLGPllARFGEARVslpggCAIG---ARPIDLHLKGLEALGAEI--E 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 918229393 178 GEEGFfpIEIHARGLRGGPVTID-----ASESsqmlsaVLMVAPLAD 219
Cdd:COG0766  140 IEHGY--IEARAGRLKGARIYLDfpsvgATEN------IMMAAVLAE 178
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 22-440 1.61e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.40  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393   22 LPIKPFRHPVRGEVLLPGSKSLTNRALLLAALCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEAAGTARVEGQENAL 101
Cdd:COG3321   863 LPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAAL 942

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  102 KGNGVGGGGEARDTQEVQAVELFVGLAGTAARFltalcAAARGGVYRIDGIAQMRKRPMRGLIEALRTLGADIRCTGEEG 181
Cdd:COG3321   943 LALAAAAAAAAAALAAAEAGALLLLAAAAAAAA-----AAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  182 FFPIEIHARGLRGGPVTIDASESSQMLSAVLMVAPLADAPVEVTIAGGVRWPFVQMTTRLMEHFGQPAVQRLADDRLRVV 261
Cdd:COG3321  1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  262 SGHPWGLQAAAAGGRRGERNAVYAIEPDATAASYFLALPLVTGGELDLPGLRGPGGGLQGDTRFVSVLQRVGAVVTETEG 341
Cdd:COG3321  1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  342 GGGRGLHVAFSVEKLAGGATAGGTRTGVTENFNEFSDTFLTLAAIAPLLDGPTRISGIAHTRKQETDRVAGMARELRRLG 421
Cdd:COG3321  1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257

                         410
                  ....*....|....*....
gi 918229393  422 QQVIEEEDSLEIHPRPLLA 440
Cdd:COG3321  1258 ALAALALLAAAAGLAALAA 1276
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
 29-219 6.36e-03

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 38.86  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393  29 HPVRGEVLLPGSKsltNRAL-LLAA--LCREPVLLTGALFSEDTRLMAEALRRLGFRVEADEaAGTARVegqenalkgng 105
Cdd:PRK09369  10 KPLSGEVTISGAK---NAALpILAAslLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDG-NGTVTI----------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918229393 106 vggggearDTQEVQAVELFVGLAGTA-ARFLtaLCAA--ARGGVYRI-----DGIAqmrKRPMRGLIEALRTLGADIRCt 177
Cdd:PRK09369  75 --------DASNINNTEAPYELVKKMrASIL--VLGPllARFGEAKVslpggCAIG---ARPVDLHLKGLEALGAEIEI- 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 918229393 178 gEEGFfpIEIHA-RGLRGGPVTID-----ASESsqmlsaVLMVAPLAD 219
Cdd:PRK09369 141 -EHGY--VEAKAdGRLKGAHIVLDfpsvgATEN------ILMAAVLAE 179
 
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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