NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|757131949|ref|WP_042686217|]
View 

3-phosphoshikimate 1-carboxyvinyltransferase [Methermicoccus shengliensis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 4-416 0e+00

5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


:

Pssm-ID: 439898  Cd Length: 421  Bit Score: 518.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   4 VIEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDG--LMVHGVAGEPKTP 80
Cdd:COG0128    5 TIAPPSPLKGTVRVPGSKSISHRALLLAALAEgESTIRNLLESDDTLATLEALRALGAEIEELDGgtLRVTGVGGGLKEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  81 DDIINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGAlAFSTKGDGTAPIVVCGGrrGLVGGECT 160
Cdd:COG0128   85 DAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGA-RIESRGGGYLPLTIRGG--PLKGGEYE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 161 IAGHISSQFISALLMACPLASKDSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEE-DAFFVPSGQQYSLKSYTVPADFS 239
Cdd:COG0128  162 IPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGyRRFTVPGGQRYRPGDYTVPGDIS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 240 SAGYLIAAACITGCAIELSGL-TSTTQADAKIVDIAERMGATLSWNGDTLKVhEGCELFGIELDCSQTPDLVPTIAAMAA 318
Cdd:COG0128  242 SAAFFLAAAAITGSEVTVEGVgLNSTQGDTGILDILKEMGADIEIENDGITV-RGSPLKGIDIDLSDIPDEAPTLAVLAA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 319 HAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGG-SPRRAVVQSWDDHRIAMALAVAGLTCG--VE 395
Cdd:COG0128  321 FAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGpKLKGAEVDSYGDHRIAMAFAVAGLRAEgpVT 400

                        410       420
                 ....*....|....*....|.
gi 757131949 396 IEGAEAVDVSYPAFFDDLARL 416
Cdd:COG0128  401 IDDAECVAKSFPDFFELLESL 421
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 4-416 0e+00

5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439898  Cd Length: 421  Bit Score: 518.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   4 VIEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDG--LMVHGVAGEPKTP 80
Cdd:COG0128    5 TIAPPSPLKGTVRVPGSKSISHRALLLAALAEgESTIRNLLESDDTLATLEALRALGAEIEELDGgtLRVTGVGGGLKEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  81 DDIINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGAlAFSTKGDGTAPIVVCGGrrGLVGGECT 160
Cdd:COG0128   85 DAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGA-RIESRGGGYLPLTIRGG--PLKGGEYE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 161 IAGHISSQFISALLMACPLASKDSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEE-DAFFVPSGQQYSLKSYTVPADFS 239
Cdd:COG0128  162 IPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGyRRFTVPGGQRYRPGDYTVPGDIS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 240 SAGYLIAAACITGCAIELSGL-TSTTQADAKIVDIAERMGATLSWNGDTLKVhEGCELFGIELDCSQTPDLVPTIAAMAA 318
Cdd:COG0128  242 SAAFFLAAAAITGSEVTVEGVgLNSTQGDTGILDILKEMGADIEIENDGITV-RGSPLKGIDIDLSDIPDEAPTLAVLAA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 319 HAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGG-SPRRAVVQSWDDHRIAMALAVAGLTCG--VE 395
Cdd:COG0128  321 FAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGpKLKGAEVDSYGDHRIAMAFAVAGLRAEgpVT 400

                        410       420
                 ....*....|....*....|.
gi 757131949 396 IEGAEAVDVSYPAFFDDLARL 416
Cdd:COG0128  401 IDDAECVAKSFPDFFELLESL 421
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 1-421 6.65e-168

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 478.10  E-value: 6.65e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   1 MRVVIEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHvDDGLMVHGVAGEP-K 78
Cdd:PRK02427   3 MMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEgETTITNLLRSEDTLATLNALRALGVEIE-DDEVVVEGVGGGGlK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  79 TPDDIINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGAlAFSTKGDGTAPIVVCGGRRGlvgGE 158
Cdd:PRK02427  82 EPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGA-KIEGRDEGYLPLTIRGGKKG---GP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 159 CTIAGHISSQFISALLMACPLASK-DSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEEDA----FFVPSGQQYSLKSYT 233
Cdd:PRK02427 158 IEYDGPVSSQFVKSLLLLAPLFAEgDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWgyrrIVIKGGQRLRGQDIT 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 234 VPADFSSAGYLIAAACIT-GCAIELSGL-TSTTQADAKIVDIAERMGATLSW--------NGDTLKVhEGCELFGIELDC 303
Cdd:PRK02427 238 VPGDPSSAAFFLAAAAITgGSEVTITNVgLNSTQGGKAIIDVLEKMGADIEIenereggePVGDIRV-RSSELKGIDIDI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 304 SQTPDLVPTIAAMAAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGsPRRAVVQSWDDHRIAM 383
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGG-PLAGVVDSYGDHRIAM 395

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 757131949 384 ALAVAGLTC--GVEIEGAEAVDVSYPAFFDDLARLGVGVR 421
Cdd:PRK02427 396 AFAIAGLAAegPVTIDDPECVAKSFPDFFEDLASLGANIE 435
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 11-416 2.20e-164

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: 468.19  E-value: 2.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  11 ISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDG-LMVHGVAGEPKTPDDIINAQN 88
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEgESRIENLLDSDDTLATLEALRALGAKIEEEGGtVEIVGGGGLGLPPEAVLDCGN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  89 SGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVvcgGRRGLVGGECTIAGHISSQ 168
Cdd:cd01556   81 SGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLI---GGGGLKGGEVEIPGAVSSQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 169 FISALLMACPLASKDSTIYVeGRMRSRPYVELTLELLRHSGVHVEVEE-DAFFVPSGQQYSLKSYTVPADFSSAGYLIAA 247
Cdd:cd01556  158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGyRTITVKGGQKYKGPEYTVEGDASSAAFFLAA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 248 ACITGCAIELSGLTSTTqADAKIVDIAERMGATLSW-NGDTLKVHEGCELFGIELDCSQTPDLVPTIAAMAAHAKGKTLI 326
Cdd:cd01556  237 AAITGSEIVIKNVGLNS-GDTGIIDVLKEMGADIEIgNEDTVVVESGGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPTRI 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 327 KNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGSPRRAVVQS--WDDHRIAMALAVAGLTC--GVEIEGAEAV 402
Cdd:cd01556  316 RNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPLKGAGVEVytYGDHRIAMSFAIAGLVAegGVTIEDPECV 395

                        410
                 ....*....|....
gi 757131949 403 DVSYPAFFDDLARL 416
Cdd:cd01556  396 AKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 13-417 2.11e-144

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: 417.45  E-value: 2.11e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   13 GAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDGLM-VHGVAGepKTPDDIINAQNSG 90
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEgETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAvIEGVGG--KEPQAELDLGNSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   91 TTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVCGGRRGlvgGECTIAGHISSQFI 170
Cdd:TIGR01356  79 TTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPG---GIVYISGSASSQYK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  171 SALLMACPLASKDSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEED-AFFVPSGQQYSLKSYTVPADFSSAGYLIAAAC 249
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGrKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  250 ITGCAIELSGLTS-TTQADAKIVDIAERMGATLSWNGDTLKVHEGCELFGIELDCSQTPDLVPTIAAMAAHAKGKTLIKN 328
Cdd:TIGR01356 236 ITGGRVTLENLGInPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRITG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  329 IAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGG-SPRRAVVQSWDDHRIAMALAVAGLTC--GVEIEGAEAVDVS 405
Cdd:TIGR01356 316 AEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKkELKGAVVDTFGDHRIAMAFAVAGLVAegEVLIDDPECVAKS 395

                         410
                  ....*....|..
gi 757131949  406 YPAFFDDLARLG 417
Cdd:TIGR01356 396 FPSFFDVLERLG 407
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
6-413 5.38e-110

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 329.64  E-value: 5.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949    6 EPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDG----LMVHGVAGEPKTP 80
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAgESTITNLLDSDDTLTMLEALRALGAEIIKLDDeksvVIVEGLGGSFEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   81 -DDIINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVcggrRGLVGGEC 159
Cdd:pfam00275  81 eDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKV----RGLRLGGI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  160 TIAGHISSQFISALLMACPLASKDSTIYVEgrMRSRPYVELTLELLRHSGVHVEV--EEDAFFVPSGQQYSLKSYTVPAD 237
Cdd:pfam00275 157 HIDGDVSSQFVTSLLMLAALLAEGTTTIEN--LASEPYIDDTENMLKKFGAKIEGsgTELSITVKGGEKLPGQEYRVEGD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  238 FSSAGYLIAAACITGCAIELSGL-TSTTQADAKIVDIAERMGATLSWNGDTLKVHEGCELFGIELDCSQTPDLVPTIAAM 316
Cdd:pfam00275 235 RSSAAYFLVAAAITGGTVTVENVgINSLQGDEALLEILEKMGAEITQEEDADIVVGPPGLRGKAVDIRTAPDPAPTTAVL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  317 AAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGSPR--RAVVQSWDDHRIAMALAVAGL--TC 392
Cdd:pfam00275 315 AAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKElkGAEVDSYGDHRIAMALALAGLvaEG 394

                         410       420
                  ....*....|....*....|.
gi 757131949  393 GVEIEGAEAVDVSYPAFFDDL 413
Cdd:pfam00275 395 ETIIDDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 4-416 0e+00

5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439898  Cd Length: 421  Bit Score: 518.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   4 VIEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDG--LMVHGVAGEPKTP 80
Cdd:COG0128    5 TIAPPSPLKGTVRVPGSKSISHRALLLAALAEgESTIRNLLESDDTLATLEALRALGAEIEELDGgtLRVTGVGGGLKEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  81 DDIINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGAlAFSTKGDGTAPIVVCGGrrGLVGGECT 160
Cdd:COG0128   85 DAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGA-RIESRGGGYLPLTIRGG--PLKGGEYE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 161 IAGHISSQFISALLMACPLASKDSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEE-DAFFVPSGQQYSLKSYTVPADFS 239
Cdd:COG0128  162 IPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGyRRFTVPGGQRYRPGDYTVPGDIS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 240 SAGYLIAAACITGCAIELSGL-TSTTQADAKIVDIAERMGATLSWNGDTLKVhEGCELFGIELDCSQTPDLVPTIAAMAA 318
Cdd:COG0128  242 SAAFFLAAAAITGSEVTVEGVgLNSTQGDTGILDILKEMGADIEIENDGITV-RGSPLKGIDIDLSDIPDEAPTLAVLAA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 319 HAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGG-SPRRAVVQSWDDHRIAMALAVAGLTCG--VE 395
Cdd:COG0128  321 FAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGpKLKGAEVDSYGDHRIAMAFAVAGLRAEgpVT 400

                        410       420
                 ....*....|....*....|.
gi 757131949 396 IEGAEAVDVSYPAFFDDLARL 416
Cdd:COG0128  401 IDDAECVAKSFPDFFELLESL 421
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 1-421 6.65e-168

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 478.10  E-value: 6.65e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   1 MRVVIEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHvDDGLMVHGVAGEP-K 78
Cdd:PRK02427   3 MMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEgETTITNLLRSEDTLATLNALRALGVEIE-DDEVVVEGVGGGGlK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  79 TPDDIINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGAlAFSTKGDGTAPIVVCGGRRGlvgGE 158
Cdd:PRK02427  82 EPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGA-KIEGRDEGYLPLTIRGGKKG---GP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 159 CTIAGHISSQFISALLMACPLASK-DSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEEDA----FFVPSGQQYSLKSYT 233
Cdd:PRK02427 158 IEYDGPVSSQFVKSLLLLAPLFAEgDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWgyrrIVIKGGQRLRGQDIT 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 234 VPADFSSAGYLIAAACIT-GCAIELSGL-TSTTQADAKIVDIAERMGATLSW--------NGDTLKVhEGCELFGIELDC 303
Cdd:PRK02427 238 VPGDPSSAAFFLAAAAITgGSEVTITNVgLNSTQGGKAIIDVLEKMGADIEIenereggePVGDIRV-RSSELKGIDIDI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 304 SQTPDLVPTIAAMAAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGsPRRAVVQSWDDHRIAM 383
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGG-PLAGVVDSYGDHRIAM 395

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 757131949 384 ALAVAGLTC--GVEIEGAEAVDVSYPAFFDDLARLGVGVR 421
Cdd:PRK02427 396 AFAIAGLAAegPVTIDDPECVAKSFPDFFEDLASLGANIE 435
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 11-416 2.20e-164

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: 468.19  E-value: 2.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  11 ISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDG-LMVHGVAGEPKTPDDIINAQN 88
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEgESRIENLLDSDDTLATLEALRALGAKIEEEGGtVEIVGGGGLGLPPEAVLDCGN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  89 SGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVvcgGRRGLVGGECTIAGHISSQ 168
Cdd:cd01556   81 SGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLI---GGGGLKGGEVEIPGAVSSQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 169 FISALLMACPLASKDSTIYVeGRMRSRPYVELTLELLRHSGVHVEVEE-DAFFVPSGQQYSLKSYTVPADFSSAGYLIAA 247
Cdd:cd01556  158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGyRTITVKGGQKYKGPEYTVEGDASSAAFFLAA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 248 ACITGCAIELSGLTSTTqADAKIVDIAERMGATLSW-NGDTLKVHEGCELFGIELDCSQTPDLVPTIAAMAAHAKGKTLI 326
Cdd:cd01556  237 AAITGSEIVIKNVGLNS-GDTGIIDVLKEMGADIEIgNEDTVVVESGGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPTRI 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 327 KNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGSPRRAVVQS--WDDHRIAMALAVAGLTC--GVEIEGAEAV 402
Cdd:cd01556  316 RNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPLKGAGVEVytYGDHRIAMSFAIAGLVAegGVTIEDPECV 395

                        410
                 ....*....|....
gi 757131949 403 DVSYPAFFDDLARL 416
Cdd:cd01556  396 AKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 13-417 2.11e-144

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: 417.45  E-value: 2.11e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   13 GAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDGLM-VHGVAGepKTPDDIINAQNSG 90
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEgETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAvIEGVGG--KEPQAELDLGNSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   91 TTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVCGGRRGlvgGECTIAGHISSQFI 170
Cdd:TIGR01356  79 TTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPG---GIVYISGSASSQYK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  171 SALLMACPLASKDSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEED-AFFVPSGQQYSLKSYTVPADFSSAGYLIAAAC 249
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGrKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  250 ITGCAIELSGLTS-TTQADAKIVDIAERMGATLSWNGDTLKVHEGCELFGIELDCSQTPDLVPTIAAMAAHAKGKTLIKN 328
Cdd:TIGR01356 236 ITGGRVTLENLGInPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRITG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  329 IAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGG-SPRRAVVQSWDDHRIAMALAVAGLTC--GVEIEGAEAVDVS 405
Cdd:TIGR01356 316 AEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKkELKGAVVDTFGDHRIAMAFAVAGLVAegEVLIDDPECVAKS 395

                         410
                  ....*....|..
gi 757131949  406 YPAFFDDLARLG 417
Cdd:TIGR01356 396 FPSFFDVLERLG 407
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
6-413 5.38e-110

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 329.64  E-value: 5.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949    6 EPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDG----LMVHGVAGEPKTP 80
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAgESTITNLLDSDDTLTMLEALRALGAEIIKLDDeksvVIVEGLGGSFEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   81 -DDIINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVcggrRGLVGGEC 159
Cdd:pfam00275  81 eDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKV----RGLRLGGI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  160 TIAGHISSQFISALLMACPLASKDSTIYVEgrMRSRPYVELTLELLRHSGVHVEV--EEDAFFVPSGQQYSLKSYTVPAD 237
Cdd:pfam00275 157 HIDGDVSSQFVTSLLMLAALLAEGTTTIEN--LASEPYIDDTENMLKKFGAKIEGsgTELSITVKGGEKLPGQEYRVEGD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  238 FSSAGYLIAAACITGCAIELSGL-TSTTQADAKIVDIAERMGATLSWNGDTLKVHEGCELFGIELDCSQTPDLVPTIAAM 316
Cdd:pfam00275 235 RSSAAYFLVAAAITGGTVTVENVgINSLQGDEALLEILEKMGAEITQEEDADIVVGPPGLRGKAVDIRTAPDPAPTTAVL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  317 AAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGSPR--RAVVQSWDDHRIAMALAVAGL--TC 392
Cdd:pfam00275 315 AAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKElkGAEVDSYGDHRIAMALALAGLvaEG 394

                         410       420
                  ....*....|....*....|.
gi 757131949  393 GVEIEGAEAVDVSYPAFFDDL 413
Cdd:pfam00275 395 ETIIDDIECTDRSFPDFEEKL 415
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
5-416 3.65e-82

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 265.37  E-value: 3.65e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   5 IEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARV-HVDDGLMVHGVAGEPKTPDD 82
Cdd:PRK11860   9 LPPLLSAGGTVRLPGSKSISNRVLLLAALSEgTTTVRDLLDSDDTRVMLDALRALGCGVeQLGDTYRITGLGGQFPVKQA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  83 IINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVcGGRRGLVGGECTIA 162
Cdd:PRK11860  89 DLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRI-GPAPLRLDAPIRVR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 163 GHISSQFISALLMACPL-ASKDSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEE-DAFFVPSGQQY-SLKSYTVPADFS 239
Cdd:PRK11860 168 GDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGwQRFTIPAGSRYrSPGEIHVEGDAS 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 240 SAGYLIAAACITGCA---IELSGLTSTtQADAKIVDIAERMGATLSWNGDTLKVHEGC-ELFGIELDCSQTPDLVPTIAA 315
Cdd:PRK11860 248 SASYFIAAGAIAGGApvrIEGVGRDSI-QGDIRFAEAARAMGAQVTSGPNWLEVRRGAwPLKAIDLDCNHIPDAAMTLAV 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 316 MAAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEI----EGGSPRRAVVQSWDDHRIAMALAVAGL- 390
Cdd:PRK11860 327 MALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVtppaQAADWKAAAIHTYDDHRMAMCFSLAAFn 406

                        410       420
                 ....*....|....*....|....*...
gi 757131949 391 --TCGVEIEGAEAVDVSYPAFFDDLARL 416
Cdd:PRK11860 407 paGLPVRINDPKCVAKTFPDYFEALFSV 434
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
 3-416 5.56e-81

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 256.21  E-value: 5.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   3 VVIEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVH---VDDGLMVHGVAGE-P 77
Cdd:PLN02338   4 ITLQPIKEISGTVKLPGSKSLSNRILLLAALSEgTTVVDNLLDSDDIRYMLGALKTLGLNVEedsENNRAVVEGCGGKfP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  78 KTPDDIINAQ----NSGTTLRLMTAILSLAPKSS--VLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVcGGR 151
Cdd:PLN02338  84 VSGDSKEDVElflgNAGTAMRPLTAAVTAAGGNAsyVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRV-NAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 152 RGLVGGECTIAGHISSQFISALLMACPLASKDSTIYVEGRMRSRPYVELTLELLRHSGVHVEVEE--DAFFVPSGQQY-S 228
Cdd:PLN02338 163 GGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDswDRFFIKGGQKYkS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 229 LKSYTVPADFSSAGYLIAAACITGCAIELSGL-TSTTQADAKIVDIAERMGATLSW-------NGDTLKVHEGCELFGIE 300
Cdd:PLN02338 243 PGNAYVEGDASSASYFLAGAAITGGTVTVEGCgTTSLQGDVKFAEVLEKMGAKVEWtensvtvTGPPRDAFGGKHLKAID 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 301 LDCSQTPDLVPTIAAMAAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEI---EGGSPrrAVVQSWD 377
Cdd:PLN02338 323 VNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIItppKKLKP--AEIDTYD 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 757131949 378 DHRIAMALAVAGltCG---VEIEGAEAVDVSYPAFFDDLARL 416
Cdd:PLN02338 401 DHRMAMAFSLAA--CGdvpVTINDPGCTRKTFPTYFDVLESI 440
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
 11-416 1.35e-69

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: 225.56  E-value: 1.35e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  11 ISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVDDGLM-VHGVAGEP-KTPDDIINAQ 87
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEgETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVItIQGVGMAGlKAPQNALNLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  88 NSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVCGGrrgLVGGECTIAGHISS 167
Cdd:cd01554   81 NSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGK---NLGPIHYEDPIASA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 168 QFISALLMACPLASKDSTIYVEGRmrsRPYVELTLELLRHSGVHVEVE-EDAFFVPSGQQYSLKSYTVPADFSSAGYLIA 246
Cdd:cd01554  158 QVKSALMFAALLAKGETVIIEAAK---EPTINHTENMLQTFGGHISVQgTKKIVVQGPQKLTGQKYVVPGDISSAAFFLV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 247 AACITGCAIELSGLTSTTQADAkIVDIAERMGATLSWNGDTLKVHEGcELFGIELDCSQTP---DLVPTIAAMAAHAKGK 323
Cdd:cd01554  235 AAAIAPGRLVLQNVGINETRTG-IIDVLRAMGAKIEIGEDTISVESS-DLKATEICGALIPrliDELPIIALLALQAQGT 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 324 TLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGSPRR-AVVQSWDDHRIAMALAVAGLTCG--VEIEGAE 400
Cdd:cd01554  313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHgARVNTFGDHRIGMMTALAALVADgeVELDRAE 392

                        410
                 ....*....|....*.
gi 757131949 401 AVDVSYPAFFDDLARL 416
Cdd:cd01554  393 AINTSYPSFFDDLESL 408
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 3-420 3.83e-55

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 194.44  E-value: 3.83e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   3 VVIEPTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVH-VDDG-LMVHGVA----G 75
Cdd:PRK14806 304 YSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEgVTEVEGFLEGEDALATLQAFRDMGVVIEgPHNGrVTIHGVGlhglK 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  76 EPKTPddiINAQNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGAlAFSTKGDGTAPIVVCGGRRgLV 155
Cdd:PRK14806 384 APPGP---LYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGA-VIETGEEGRPPLSIRGGQR-LK 458

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 156 GGE--CTIAghiSSQFISALLMAcplaskdsTIYVEGR---MRSRPYVELTLELLRHSGVHVEVEEDAFFVPSGQQYSLK 230
Cdd:PRK14806 459 GIHydLPMA---SAQVKSCLLLA--------GLYAEGEtsvTEPAPTRDHTERMLRGFGYPVKVEGNTISVEGGGKLTAT 527

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 231 SYTVPADFSSAGYLIAAACITGCA---IELSGLTSTTQAdakIVDIAERMGATLSWNGDT---------LKVhEGCELFG 298
Cdd:PRK14806 528 DIEVPADISSAAFFLVAASIAEGSeltLEHVGINPTRTG---VIDILKLMGADITLENERevggepvadIRV-RGARLKG 603

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 299 IELDCSQTP---DLVPTIAAMAAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEGGSPRRAVVQS 375
Cdd:PRK14806 604 IDIPEDQVPlaiDEFPVLFVAAACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGGIFGGGEVES 683

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 757131949 376 WDDHRIAMALAVAGL--TCGVEIEGAEAVDVSYPAFFDDLARLGVGV 420
Cdd:PRK14806 684 HGDHRIAMSFSVASLraSGPITIHDCANVATSFPNFLELANQVGIRI 730
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 7-411 2.15e-51

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 183.37  E-value: 2.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949   7 PTQHISGAITPPGSKSCTHRALVCGALSK-RAHILNPLISRDTRATLEAVEAMGARVHVD-DGLMVHGVAGE--PKTPDD 82
Cdd:PRK11861 247 PFSHAQGTVRLPGSKSISNRVLLLAALAEgETTVTNLLDSDDTRVMLDALTKLGVKLSRDgGTCVVGGTRGAftAKTADL 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  83 IINaqNSGTTLRLMTAILSLAPKSSVLTGDSSLRRRPNQPLLDAMGELGALAFSTKGDGTAPIVVCGGRRGlVGGECTIA 162
Cdd:PRK11861 327 FLG--NAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATIS-VDAPIRVR 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 163 GHISSQFISALLMACPLA-SKD--STIYVEGRMRSRPYVELTLELLRHSGVHVEVEE-DAFFVPSGQQY-SLKSYTVPAD 237
Cdd:PRK11861 404 GDVSSQFLTALLMTLPLVkAKDgaSVVEIDGELISKPYIEITIKLMARFGVTVERDGwQRFTVPAGVRYrSPGTIMVEGD 483

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 238 FSSAGYLIAAACITGCAIELSGL-TSTTQADAKIVDIAERMGATLSWNGDTLKV----HEGCELFGIELDCSQTPDLVPT 312
Cdd:PRK11861 484 ASSASYFLAAGALGGGPLRVEGVgRASIQGDVGFANALMQMGANVTMGDDWIEVrgigHDHGRLAPIDMDFNLIPDAAMT 563

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 313 IAAMAAHAKGKTLIKNIAHVRLKETDRIRAMACELSKMGIRCTEGKDFLEIEggSPRR----AVVQSWDDHRIAMALAVA 388
Cdd:PRK11861 564 IAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVT--PPAQltpnASIDTYDDHRMAMCFSLV 641

                        410       420
                 ....*....|....*....|....
gi 757131949 389 GL-TCGVEIEGAEAVDVSYPAFFD 411
Cdd:PRK11861 642 SLgGVPVRINDPKCVGKTFPDYFD 665
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
 11-416 2.70e-08

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: 55.56  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  11 ISGAITPPGSKSCTHRALVCGALSKRAHILN--PLIsRDTRATLEAVEAMGARVHVD--DGLMVHgvagepktPDDIINA 86
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRnvPDL-LDVETMIELLRSLGAKVEFEgeNTLVID--------ASNINST 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949  87 QNSGTTLRLMTA-ILSLAP------KSSV-LTGDSSLRRRPNQPLLDAMGELGAlAFSTKGDGtapiVVCGGRRGLVGGe 158
Cdd:cd01555   72 EAPYELVRKMRAsILVLGPllarfgEARVsLPGGCAIGARPVDLHLKGLEALGA-KIEIEDGY----VEAKAAGRLKGA- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 159 ctiagHISSQFISA-----LLMACPLASKDSTIY---VEgrmrsrPYVELTLELLRHSGVHVEVEEDAFFVPSGQQySLK 230
Cdd:cd01555  146 -----RIYLDFPSVgatenIMMAAVLAEGTTVIEnaaRE------PEIVDLANFLNKMGAKIEGAGTDTIRIEGVE-RLH 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 231 S--YTVPADFSSAGYLIAAACITGCAIELSG-----LTSttqadakIVDIAERMGATLSWNGDTLKV-HEGCELFGIELD 302
Cdd:cd01555  214 GaeHTVIPDRIEAGTFLVAAAITGGDITVENvipehLEA-------VLAKLREMGAKIEIGEDGIRVdGDGGRLKAVDIE 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 303 CSQTP----DLVPTIAAMAAHAKGKTLIkniahvrlkeTDRI---RAM-ACELSKMGIRCT-EGKDfLEIEGGSPRR-AV 372
Cdd:cd01555  287 TAPYPgfptDLQAQFMALLTQAEGTSVI----------TETIfenRFMhVDELNRMGADIKvEGNT-AIIRGVTKLSgAP 355

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 757131949 373 VQSwDDHRIAMALAVAGLTC-GV-EIEGAEAVDVSYPAFFDDLARL 416
Cdd:cd01555  356 VMA-TDLRAGAALVLAGLAAeGEtIISNIYHIDRGYERIEEKLRAL 400
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 231-422 3.32e-06

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


Pssm-ID: 440529  Cd Length: 416  Bit Score: 48.83  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 231 SYTVPADFSSAG-YLIAAAcITGCAIELSGltsttqADAKIVDIA----ERMGATLSWNGDTLKVHEGCELFGIELDCSQ 305
Cdd:COG0766  226 EHTVIPDRIEAGtFLVAAA-ITGGDVTVKN------VIPEHLEAVlaklREAGVEIEEGDDGIRVRGPGRLKAVDIKTAP 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 306 TP----DLVPTIAAMAAHAKGKTLIkniahvrlkeTDRI---RAM-ACELSKMG--IRctegkdfLE-----IEGGSPRR 370
Cdd:COG0766  299 YPgfptDLQAQFMALLTQAEGTSVI----------TETVfenRFMhVDELNRMGadIK-------LDghtaiVRGVTKLS 361

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 757131949 371 -AVVQSWdDHRIAMALAVAGLTC-GV-EIEGAEAVDVSYPAFFDDLARLGVGVRW 422
Cdd:COG0766  362 gAPVMAT-DLRAGAALVLAGLAAeGEtVIDNIYHIDRGYENLEEKLRALGADIER 415
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
 237-416 4.99e-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: 44.19  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 237 DFSSAGYLIAAACITGCAIELSGLTSTT------QADAKIVDIAERM-GATLSW---NGDTLKVHEGcELFGIELD---- 302
Cdd:cd01553    9 GGQILRSFLVLAAISGGPITVTGIRPDRakpgllRQHLTFLKALEKIcGATVEGgelGSDRISFRPG-TVRGGDVRfaig 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 303 -CSQTPDLVPTIAAMAAHAKGKTLIKNIAHVR----LKETDRIRAMACELSKMGIRCTEGKDFLEIEGGSP-----RRAV 372
Cdd:cd01553   88 sAGSCTDVLQTILPLLLFAKGPTRLTVTGGTDnpsaPPADFIRFVLEPELAKIGAHQEETLLRHGFYPAGGgvvatEVSP 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 757131949 373 VQSWDDHRIAMALAVAGLTCGVEIEGAEAVDVSYPAFFDDLARL 416
Cdd:cd01553  168 VEKLNTAQLRQLVLPMLLASGAVEFTVAHPSCHLLTNFAVLEAL 211
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 145-420 3.82e-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: 42.28  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 145 IVVCGGRRgLVGgECTIAGhiSSQFISALLMACPLASKDSTIY-VegrmrsrPY---VELTLELLRHSGVHVEVEED--A 218
Cdd:COG0766    4 LIIEGGKP-LSG-EVRISG--AKNAALPILAAALLTDGPVTLRnV-------PDlsdVRTMLELLESLGVKVERDDGgtL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 219 FFVPSGqqysLKSYTVPADFSS---AGYLIAA--------ACIT---GCAIE-------LSGLtsttqadakivdiaERM 277
Cdd:COG0766   73 TIDASN----INSTEAPYELVRkmrASILVLGpllarfgeARVSlpgGCAIGarpidlhLKGL--------------EAL 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 278 GATLSWNGDTLKVH----EGCElfgIELDcsqtpdlVP----TIAAM--AAHAKGKTLIKNIAhvrlKETDrIRAMACEL 347
Cdd:COG0766  135 GAEIEIEHGYIEARagrlKGAR---IYLD-------FPsvgaTENIMmaAVLAEGTTVIENAA----REPE-IVDLANFL 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 348 SKMGIRCT-EGKDFLEIEGGSPRRAVvqswdDHRI------AMALAVAGLTCG--VEIEGAEAVDVsyPAFFDDLARLGV 418
Cdd:COG0766  200 NAMGAKIEgAGTDTITIEGVEKLHGA-----EHTVipdrieAGTFLVAAAITGgdVTVKNVIPEHL--EAVLAKLREAGV 272


                 ..
gi 757131949 419 GV 420
Cdd:COG0766  273 EI 274
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
 198-421 2.41e-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: 39.76  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 198 VELTLELLRHSGVHVEVE-EDAFFVPSGqqySLKSYTVPADFSS---AGYLIAAACIT-----------GCAI------- 255
Cdd:cd01555   39 VETMIELLRSLGAKVEFEgENTLVIDAS---NINSTEAPYELVRkmrASILVLGPLLArfgearvslpgGCAIgarpvdl 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 256 ELSGLtsttqadakivdiaERMGATLSWNGDTLKVHEGCELFG--IELDCsqtPDLVPTIAAM--AAHAKGKTLIKNIAh 331
Cdd:cd01555  116 HLKGL--------------EALGAKIEIEDGYVEAKAAGRLKGarIYLDF---PSVGATENIMmaAVLAEGTTVIENAA- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 332 vrlKETDrIRAMACELSKMGIRCT-EGKDFLEIEGgsprravVQSW--DDHRI------AMALAVAGLTCG--VEIEGAE 400
Cdd:cd01555  178 ---REPE-IVDLANFLNKMGAKIEgAGTDTIRIEG-------VERLhgAEHTVipdrieAGTFLVAAAITGgdITVENVI 246

                        250       260
                 ....*....|....*....|.
gi 757131949 401 AVDVSypAFFDDLARLGVGVR 421
Cdd:cd01555  247 PEHLE--AVLAKLREMGAKIE 265
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
 145-420 5.75e-03

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 38.86  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 145 IVVCGGRRglVGGECTIAGhiSSQFISALLMACPLASKDSTIyvegrmRSRPY---VELTLELLRHSGVHVEVEEDA--F 219
Cdd:PRK09369   4 LVIEGGKP--LSGEVTISG--AKNAALPILAASLLAEEPVTL------TNVPDlsdVRTMIELLRSLGAKVEFDGNGtvT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 220 FVPSGqqysLKSYTVPADFSS--------AGYLIAA---ACIT---GCAI-------ELSGLtsttqadakivdiaERMG 278
Cdd:PRK09369  74 IDASN----INNTEAPYELVKkmrasilvLGPLLARfgeAKVSlpgGCAIgarpvdlHLKGL--------------EALG 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 279 ATLSWNGDTLKVHEGCELFG--IELDCsqtpdlvPTIAA-----MAA-HAKGKTLIKNIAhvrlKETDrIRAMACELSKM 350
Cdd:PRK09369 136 AEIEIEHGYVEAKADGRLKGahIVLDF-------PSVGAtenilMAAvLAEGTTVIENAA----REPE-IVDLANFLNKM 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131949 351 GIRCT-EGKDFLEIEGgsprravVQSWD--DHRI----------AMALAVAGltCGVEIEGAEAVDVSypAFFDDLARLG 417
Cdd:PRK09369 204 GAKISgAGTDTITIEG-------VERLHgaEHTVipdrieagtfLVAAAITG--GDVTIRGARPEHLE--AVLAKLREAG 272


                 ...
gi 757131949 418 VGV 420
Cdd:PRK09369 273 AEI 275
 
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