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Conserved domains on  [gi|2335315089|ref|WP_265857882|]
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3-phosphoshikimate 1-carboxyvinyltransferase [Bombilactobacillus mellis]

Protein Classification

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

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

EC:  2.5.1.19
PubMed:  17348837

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-434 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


:

Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 523.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   1 MIMQLISKPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNneTVIIHGQGLQ 80
Cdd:PRK02427    1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIEDD--EVVVEGVGGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  81 SWHAPAHALDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHL-THGHLPMTISG-QPLHSL 158
Cdd:PRK02427   79 GLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGrDEGYLPLTIRGgKKGGPI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 159 CYQMPLASAQVKSALILAALQASDAS--TIMEKLPTRDHTE---RLLRQFGAHLTTSDD--YYKINIQPAHQLQGQTIQI 231
Cdd:PRK02427  159 EYDGPVSSQFVKSLLLLAPLFAEGDTetTVIEPLPSRPHTEitlRMLRAFGVEVENVEGwgYRRIVIKGGQRLRGQDITV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 232 PADLSSAAFFLTAASIIPHSQLQLTNVGLNPTRTG--FLKVLQRMGGQVKITAQSqENGEPRGNLEVSAAKLHPIVItat 309
Cdd:PRK02427  239 PGDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENER-EGGEPVGDIRVRSSELKGIDI--- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 310 EIPNIIDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSVInphlDSHGD 389
Cdd:PRK02427  315 DIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLAGVV----DSYGD 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2335315089 390 HRIGMMLAIAALKCSAPLHLKNAAVVNISYPNFFQDLNNLLSQEE 434
Cdd:PRK02427  391 HRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANIE 435
 
Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-434 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 523.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   1 MIMQLISKPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNneTVIIHGQGLQ 80
Cdd:PRK02427    1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIEDD--EVVVEGVGGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  81 SWHAPAHALDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHL-THGHLPMTISG-QPLHSL 158
Cdd:PRK02427   79 GLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGrDEGYLPLTIRGgKKGGPI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 159 CYQMPLASAQVKSALILAALQASDAS--TIMEKLPTRDHTE---RLLRQFGAHLTTSDD--YYKINIQPAHQLQGQTIQI 231
Cdd:PRK02427  159 EYDGPVSSQFVKSLLLLAPLFAEGDTetTVIEPLPSRPHTEitlRMLRAFGVEVENVEGwgYRRIVIKGGQRLRGQDITV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 232 PADLSSAAFFLTAASIIPHSQLQLTNVGLNPTRTG--FLKVLQRMGGQVKITAQSqENGEPRGNLEVSAAKLHPIVItat 309
Cdd:PRK02427  239 PGDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENER-EGGEPVGDIRVRSSELKGIDI--- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 310 EIPNIIDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSVInphlDSHGD 389
Cdd:PRK02427  315 DIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLAGVV----DSYGD 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2335315089 390 HRIGMMLAIAALKCSAPLHLKNAAVVNISYPNFFQDLNNLLSQEE 434
Cdd:PRK02427  391 HRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANIE 435
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
4-429 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: 511.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   4 QLISKPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQ-NNETVIIHGQGlQSW 82
Cdd:COG0128     3 SLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEElDGGTLRVTGVG-GGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  83 HAPAHALDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVI-HLTHGHLPMTISGQPLHSLCYQ 161
Cdd:COG0128    82 KEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIeSRGGGYLPLTIRGGPLKGGEYE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 162 MPL-ASAQVKSALILAALQASDASTI-----MEKLPTRDHTERLLRQFGAHLTTsDDYYKINIQPAHQLQGQTIQIPADL 235
Cdd:COG0128   162 IPGsASSQFKSALLLAGPLAEGGLEItvtgeLESKPYRDHTERMLRAFGVEVEV-EGYRRFTVPGGQRYRPGDYTVPGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 236 SSAAFFLTAASIIPhSQLQLTNVGLNPT--RTGFLKVLQRMGGQVKITAQSqengeprgnLEVSAAKLHPIVITATEIPn 313
Cdd:COG0128   241 SSAAFFLAAAAITG-SEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG---------ITVRGSPLKGIDIDLSDIP- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 314 iiDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSviNPHLDSHGDHRIG 393
Cdd:COG0128   310 --DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLK--GAEVDSYGDHRIA 385
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2335315089 394 MMLAIAALKCSAPLHLKNAAVVNISYPNFFQDLNNL 429
Cdd:COG0128   386 MAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
13-429 1.54e-167

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: 476.66  E-value: 1.54e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  13 LHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNNETVIIHGQGLQsWHAPAHALDMG 92
Cdd:cd01556     1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGL-GLPPEAVLDCG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  93 NSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHLTH-GHLPMTISGQPLHSLCYQMPLA-SAQVK 170
Cdd:cd01556    80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREgGGYPPLIGGGGLKGGEVEIPGAvSSQFK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 171 SALILAALQASDASTI----MEKLPTRDHTERLLRQFGAHLTTsDDYYKINIQPAHQLQGQTIQIPADLSSAAFFLTAAS 246
Cdd:cd01556   160 SALLLAAPLAEGPTTIiigeLESKPYIDHTERMLRAFGAEVEV-DGYRTITVKGGQKYKGPEYTVEGDASSAAFFLAAAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 247 IIPhSQLQLTNVGLNPTRTGFLKVLQRMGGQVKITAQSQENGEPRGnlevsaaKLHPIVITATEIPniiDEIPLIALLAA 326
Cdd:cd01556   239 ITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVVVESGG-------KLKGIDIDGNDIP---DEAPTLAVLAA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 327 TADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRqPWSVINPHLDSHGDHRIGMMLAIAALKCSAP 406
Cdd:cd01556   308 FAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGG-PLKGAGVEVYTYGDHRIAMSFAIAGLVAEGG 386
                         410       420
                  ....*....|....*....|...
gi 2335315089 407 LHLKNAAVVNISYPNFFQDLNNL 429
Cdd:cd01556   387 VTIEDPECVAKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
15-430 2.95e-143

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: 414.75  E-value: 2.95e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  15 GTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNNETVIIHGQGLQswhAPAHALDMGNS 94
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGK---EPQAELDLGNS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  95 GTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIH--LTHGHLPMTISGqPLHSLC-YQMPLASAQVKS 171
Cdd:TIGR01356  78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISslEGGGSLPLTISG-PLPGGIvYISGSASSQYKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 172 ALILAA--LQASDASTIMEKLPTRDHTERLLRQFGAHLT--TSDDYYKINIQPAHQLQGQTIQIPADLSSAAFFLTAASI 247
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFGVevERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAAI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 248 IPhSQLQLTNVGLNPTRTG--FLKVLQRMGGQVKITAQSqengeprgnLEVSAA-KLHPIVItatEIPNIIDEIPLIALL 324
Cdd:TIGR01356 237 TG-GRVTLENLGINPTQGDkaIIIVLEEMGADIEVEEDD---------LIVEGAsGLKGIKI---DMDDMIDELPTLAVL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 325 AATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSviNPHLDSHGDHRIGMMLAIAALKCS 404
Cdd:TIGR01356 304 AAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELK--GAVVDTFGDHRIAMAFAVAGLVAE 381
                         410       420
                  ....*....|....*....|....*.
gi 2335315089 405 APLHLKNAAVVNISYPNFFQDLNNLL 430
Cdd:TIGR01356 382 GEVLIDDPECVAKSFPSFFDVLERLG 407
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-426 1.69e-122

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 362.39  E-value: 1.69e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   8 KPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDI---SQNNETVIIHGQGlQSWHA 84
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIiklDDEKSVVIVEGLG-GSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  85 PAHA-LDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHLTHGH--LPMTISGQPLHSLCYQ 161
Cdd:pfam00275  80 PEDLvLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYnyAPLKVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 162 MPLASAQVKSALILAALQASDASTIME--KLPTRDHTERLLRQFGAHLTTSDDYYKINIQPAHQLQGQTIQIPADLSSAA 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENlaSEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 240 FFLTAASIIPhSQLQLTNVGLNPTRTGF--LKVLQRMGGQVKitaqsqenGEPRGNLEVSAAKLHPIvitATEIPNIIDE 317
Cdd:pfam00275 240 YFLVAAAITG-GTVTVENVGINSLQGDEalLEILEKMGAEIT--------QEEDADIVVGPPGLRGK---AVDIRTAPDP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 318 IPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIdgRQPWSVINP-HLDSHGDHRIGMML 396
Cdd:pfam00275 308 APTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLII--IPAVKELKGaEVDSYGDHRIAMAL 385
                         410       420       430
                  ....*....|....*....|....*....|
gi 2335315089 397 AIAALKCSAPLHLKNAAVVNISYPNFFQDL 426
Cdd:pfam00275 386 ALAGLVAEGETIIDDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-434 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 523.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   1 MIMQLISKPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNneTVIIHGQGLQ 80
Cdd:PRK02427    1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIEDD--EVVVEGVGGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  81 SWHAPAHALDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHL-THGHLPMTISG-QPLHSL 158
Cdd:PRK02427   79 GLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGrDEGYLPLTIRGgKKGGPI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 159 CYQMPLASAQVKSALILAALQASDAS--TIMEKLPTRDHTE---RLLRQFGAHLTTSDD--YYKINIQPAHQLQGQTIQI 231
Cdd:PRK02427  159 EYDGPVSSQFVKSLLLLAPLFAEGDTetTVIEPLPSRPHTEitlRMLRAFGVEVENVEGwgYRRIVIKGGQRLRGQDITV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 232 PADLSSAAFFLTAASIIPHSQLQLTNVGLNPTRTG--FLKVLQRMGGQVKITAQSqENGEPRGNLEVSAAKLHPIVItat 309
Cdd:PRK02427  239 PGDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENER-EGGEPVGDIRVRSSELKGIDI--- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 310 EIPNIIDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSVInphlDSHGD 389
Cdd:PRK02427  315 DIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLAGVV----DSYGD 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2335315089 390 HRIGMMLAIAALKCSAPLHLKNAAVVNISYPNFFQDLNNLLSQEE 434
Cdd:PRK02427  391 HRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANIE 435
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
4-429 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: 511.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   4 QLISKPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQ-NNETVIIHGQGlQSW 82
Cdd:COG0128     3 SLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEElDGGTLRVTGVG-GGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  83 HAPAHALDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVI-HLTHGHLPMTISGQPLHSLCYQ 161
Cdd:COG0128    82 KEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIeSRGGGYLPLTIRGGPLKGGEYE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 162 MPL-ASAQVKSALILAALQASDASTI-----MEKLPTRDHTERLLRQFGAHLTTsDDYYKINIQPAHQLQGQTIQIPADL 235
Cdd:COG0128   162 IPGsASSQFKSALLLAGPLAEGGLEItvtgeLESKPYRDHTERMLRAFGVEVEV-EGYRRFTVPGGQRYRPGDYTVPGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 236 SSAAFFLTAASIIPhSQLQLTNVGLNPT--RTGFLKVLQRMGGQVKITAQSqengeprgnLEVSAAKLHPIVITATEIPn 313
Cdd:COG0128   241 SSAAFFLAAAAITG-SEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG---------ITVRGSPLKGIDIDLSDIP- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 314 iiDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSviNPHLDSHGDHRIG 393
Cdd:COG0128   310 --DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLK--GAEVDSYGDHRIA 385
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2335315089 394 MMLAIAALKCSAPLHLKNAAVVNISYPNFFQDLNNL 429
Cdd:COG0128   386 MAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
13-429 1.54e-167

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: 476.66  E-value: 1.54e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  13 LHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNNETVIIHGQGLQsWHAPAHALDMG 92
Cdd:cd01556     1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGL-GLPPEAVLDCG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  93 NSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHLTH-GHLPMTISGQPLHSLCYQMPLA-SAQVK 170
Cdd:cd01556    80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREgGGYPPLIGGGGLKGGEVEIPGAvSSQFK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 171 SALILAALQASDASTI----MEKLPTRDHTERLLRQFGAHLTTsDDYYKINIQPAHQLQGQTIQIPADLSSAAFFLTAAS 246
Cdd:cd01556   160 SALLLAAPLAEGPTTIiigeLESKPYIDHTERMLRAFGAEVEV-DGYRTITVKGGQKYKGPEYTVEGDASSAAFFLAAAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 247 IIPhSQLQLTNVGLNPTRTGFLKVLQRMGGQVKITAQSQENGEPRGnlevsaaKLHPIVITATEIPniiDEIPLIALLAA 326
Cdd:cd01556   239 ITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVVVESGG-------KLKGIDIDGNDIP---DEAPTLAVLAA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 327 TADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRqPWSVINPHLDSHGDHRIGMMLAIAALKCSAP 406
Cdd:cd01556   308 FAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGG-PLKGAGVEVYTYGDHRIAMSFAIAGLVAEGG 386
                         410       420
                  ....*....|....*....|...
gi 2335315089 407 LHLKNAAVVNISYPNFFQDLNNL 429
Cdd:cd01556   387 VTIEDPECVAKSFPNFFEDLESL 409
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
9-422 2.00e-147

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 436.73  E-value: 2.00e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   9 PQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQ-NNETVIIHGQGLQSWHAPAH 87
Cdd:PRK14806  308 PGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEGpHNGRVTIHGVGLHGLKAPPG 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  88 ALDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHL-THGHLPMTISG-QPLHSLCYQMPLA 165
Cdd:PRK14806  388 PLYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIETgEEGRPPLSIRGgQRLKGIHYDLPMA 467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 166 SAQVKSALILAALQASDASTIMEKLPTRDHTERLLRQFGAHLTTSDDyyKINIQPAHQLQGQTIQIPADLSSAAFFLTAA 245
Cdd:PRK14806  468 SAQVKSCLLLAGLYAEGETSVTEPAPTRDHTERMLRGFGYPVKVEGN--TISVEGGGKLTATDIEVPADISSAAFFLVAA 545
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 246 SIIPHSQLQLTNVGLNPTRTGFLKVLQRMGGQVKITAQSQENGEPRGNLEVSAAKLHPIVITATEIPNIIDEIPLIALLA 325
Cdd:PRK14806  546 SIAEGSELTLEHVGINPTRTGVIDILKLMGADITLENEREVGGEPVADIRVRGARLKGIDIPEDQVPLAIDEFPVLFVAA 625
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 326 ATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSvinPHLDSHGDHRIGMMLAIAALKCSA 405
Cdd:PRK14806  626 ACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGGIFGG---GEVESHGDHRIAMSFSVASLRASG 702
                         410
                  ....*....|....*..
gi 2335315089 406 PLHLKNAAVVNISYPNF 422
Cdd:PRK14806  703 PITIHDCANVATSFPNF 719
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
15-430 2.95e-143

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: 414.75  E-value: 2.95e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  15 GTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNNETVIIHGQGLQswhAPAHALDMGNS 94
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGK---EPQAELDLGNS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  95 GTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIH--LTHGHLPMTISGqPLHSLC-YQMPLASAQVKS 171
Cdd:TIGR01356  78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISslEGGGSLPLTISG-PLPGGIvYISGSASSQYKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 172 ALILAA--LQASDASTIMEKLPTRDHTERLLRQFGAHLT--TSDDYYKINIQPAHQLQGQTIQIPADLSSAAFFLTAASI 247
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFGVevERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAAI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 248 IPhSQLQLTNVGLNPTRTG--FLKVLQRMGGQVKITAQSqengeprgnLEVSAA-KLHPIVItatEIPNIIDEIPLIALL 324
Cdd:TIGR01356 237 TG-GRVTLENLGINPTQGDkaIIIVLEEMGADIEVEEDD---------LIVEGAsGLKGIKI---DMDDMIDELPTLAVL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 325 AATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSviNPHLDSHGDHRIGMMLAIAALKCS 404
Cdd:TIGR01356 304 AAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELK--GAVVDTFGDHRIAMAFAVAGLVAE 381
                         410       420
                  ....*....|....*....|....*.
gi 2335315089 405 APLHLKNAAVVNISYPNFFQDLNNLL 430
Cdd:TIGR01356 382 GEVLIDDPECVAKSFPSFFDVLERLG 407
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-426 1.69e-122

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 362.39  E-value: 1.69e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   8 KPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDI---SQNNETVIIHGQGlQSWHA 84
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIiklDDEKSVVIVEGLG-GSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  85 PAHA-LDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHLTHGH--LPMTISGQPLHSLCYQ 161
Cdd:pfam00275  80 PEDLvLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYnyAPLKVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 162 MPLASAQVKSALILAALQASDASTIME--KLPTRDHTERLLRQFGAHLTTSDDYYKINIQPAHQLQGQTIQIPADLSSAA 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENlaSEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 240 FFLTAASIIPhSQLQLTNVGLNPTRTGF--LKVLQRMGGQVKitaqsqenGEPRGNLEVSAAKLHPIvitATEIPNIIDE 317
Cdd:pfam00275 240 YFLVAAAITG-GTVTVENVGINSLQGDEalLEILEKMGAEIT--------QEEDADIVVGPPGLRGK---AVDIRTAPDP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 318 IPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIdgRQPWSVINP-HLDSHGDHRIGMML 396
Cdd:pfam00275 308 APTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLII--IPAVKELKGaEVDSYGDHRIAMAL 385
                         410       420       430
                  ....*....|....*....|....*....|
gi 2335315089 397 AIAALKCSAPLHLKNAAVVNISYPNFFQDL 426
Cdd:pfam00275 386 ALAGLVAEGETIIDDIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
13-429 2.14e-99

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: 302.99  E-value: 2.14e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  13 LHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNNETVIIHGQGLQSWHAPAHALDMG 92
Cdd:cd01554     1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  93 NSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHLTHGHL--PMTISGQPLHSLCYQMPLASAQVK 170
Cdd:cd01554    81 NSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDlpPLLKGGKNLGPIHYEDPIASAQVK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 171 SALILAALQASDASTIMEKL--PTRDHTERLLRQFGAHLtTSDDYYKINIQPAHQLQGQTIQIPADLSSAAFFLTAASII 248
Cdd:cd01554   161 SALMFAALLAKGETVIIEAAkePTINHTENMLQTFGGHI-SVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAIA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 249 PhSQLQLTNVGLNPTRTGFLKVLQRMGGQVKITAQ--SQENGEPRGnlevsaaklhpIVITATEIPNIIDEIPLIALLAA 326
Cdd:cd01554   240 P-GRLVLQNVGINETRTGIIDVLRAMGAKIEIGEDtiSVESSDLKA-----------TEICGALIPRLIDELPIIALLAL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 327 TADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIDGRQPWSviNPHLDSHGDHRIGMMLAIAALKCSAP 406
Cdd:cd01554   308 QAQGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLH--GARVNTFGDHRIGMMTALAALVADGE 385
                         410       420
                  ....*....|....*....|...
gi 2335315089 407 LHLKNAAVVNISYPNFFQDLNNL 429
Cdd:cd01554   386 VELDRAEAINTSYPSFFDDLESL 408
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
9-426 2.34e-41

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 155.59  E-value: 2.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   9 PQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNNETVIIHGQGLQSWHAPAhA 88
Cdd:PRK11860   11 PLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYRITGLGGQFPVKQA-D 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  89 LDMGNSGTTTRLLAGLLAgrpfttTLIGDQSLS------QRPMQRIQHPLQKMGAVIHLT--HGHLPMTISGQPLHSlcy 160
Cdd:PRK11860   90 LFLGNAGTAMRPLTAALA------LLGGEYELSgvprmhERPIGDLVDALRQLGCDIDYLgnEGFPPLRIGPAPLRL--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 161 QMPLA-----SAQVKSALILA-ALQASDASTI--MEKLPTRDHTE---RLLRQFGAHLtTSDDYYKINIQPAHQLQGQ-T 228
Cdd:PRK11860  161 DAPIRvrgdvSSQFLTALLMAlPLVARRDITIevVGELISKPYIEitlNLLARFGIAV-QREGWQRFTIPAGSRYRSPgE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 229 IQIPADLSSAAFFLTAASIIPHSQLQLTNVGLNPTR--TGFLKVLQRMGGQVKITAQSqengeprgnLEVS--AAKLHPI 304
Cdd:PRK11860  240 IHVEGDASSASYFIAAGAIAGGAPVRIEGVGRDSIQgdIRFAEAARAMGAQVTSGPNW---------LEVRrgAWPLKAI 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 305 VITATEIPniiDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADgFIIDGRQPWSVINPH- 383
Cdd:PRK11860  311 DLDCNHIP---DAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGAD-YIRVTPPAQAADWKAa 386
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2335315089 384 -LDSHGDHRIGMMLAIAAL-KCSAPLHLKNAAVVNISYPNFFQDL 426
Cdd:PRK11860  387 aIHTYDDHRMAMCFSLAAFnPAGLPVRINDPKCVAKTFPDYFEAL 431
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
4-432 8.89e-39

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 145.28  E-value: 8.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   4 QLISKPQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQN--NETVIIHGQGLQs 81
Cdd:PLN02338    3 EITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDseNNRAVVEGCGGK- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  82 WHAPAHA-----LDMGNSGTTTRLLAGLL--AGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHLTHGH--LPMTI-- 150
Cdd:PLN02338   82 FPVSGDSkedveLFLGNAGTAMRPLTAAVtaAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTncPPVRVna 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 151 -SGQP--LHSLCYQMplaSAQVKSALILAALQASDASTI--MEKL---PTRDHTERLLRQFGAHLTTSDDYYKINIQpah 222
Cdd:PLN02338  162 aGGLPggKVKLSGSI---SSQYLTALLMAAPLALGDVEIeiVDKLisvPYVEMTLKLMERFGVSVEHSDSWDRFFIK--- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 223 qlQGQTIQIP------ADLSSAAFFLTAASIIPHSqlqLTNVGLNPTR----TGFLKVLQRMGGQVKITAQSQE-NGEPR 291
Cdd:PLN02338  236 --GGQKYKSPgnayveGDASSASYFLAGAAITGGT---VTVEGCGTTSlqgdVKFAEVLEKMGAKVEWTENSVTvTGPPR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 292 GnlEVSAAKLHPIVITATEIPniiDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFII 371
Cdd:PLN02338  311 D--AFGGKHLKAIDVNMNKMP---DVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCII 385
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2335315089 372 dgRQPWSVINPHLDSHGDHRIGMMLAIAAlkCS-APLHLKNAAVVNISYPNFFQDLNNLLSQ 432
Cdd:PLN02338  386 --TPPKKLKPAEIDTYDDHRMAMAFSLAA--CGdVPVTINDPGCTRKTFPTYFDVLESIAKH 443
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
9-423 2.92e-36

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 141.00  E-value: 2.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089   9 PQQGLHGTIQVPGDKSISHRALIIGAMGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQNNETVIIHGQgLQSWHAPAHA 88
Cdd:PRK11861  247 PFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGT-RGAFTAKTAD 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  89 LDMGNSGTTTRLLAGLLAGRPFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHL--THGHLPMTIsgQPLhSLCYQMPL-- 164
Cdd:PRK11861  326 LFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYegNEGFPPLRI--RPA-TISVDAPIrv 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 165 ---ASAQVKSALI--LAALQASDASTIME------KLPTRDHTERLLRQFGahLTTSDDYYKINIQPA---HQLQGqTIQ 230
Cdd:PRK11861  403 rgdVSSQFLTALLmtLPLVKAKDGASVVEidgeliSKPYIEITIKLMARFG--VTVERDGWQRFTVPAgvrYRSPG-TIM 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 231 IPADLSSAAFFLtAASIIPHSQLQLTNVGLNPTR--TGFLKVLQRMGGQVKItaqSQENGEPRGnLEVSAAKLHPIVITA 308
Cdd:PRK11861  480 VEGDASSASYFL-AAGALGGGPLRVEGVGRASIQgdVGFANALMQMGANVTM---GDDWIEVRG-IGHDHGRLAPIDMDF 554
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 309 TEIPniiDEIPLIALLAATADGRSKITGAGELRVKETDRIHTTVEELSKLGIAITELADGFIIdgrQPWSVINPH--LDS 386
Cdd:PRK11861  555 NLIP---DAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVV---TPPAQLTPNasIDT 628
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2335315089 387 HGDHRIGMMLAIAALKcSAPLHLKNAAVVNISYPNFF 423
Cdd:PRK11861  629 YDDHRMAMCFSLVSLG-GVPVRINDPKCVGKTFPDYF 664
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
13-401 4.61e-08

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: 54.99  E-value: 4.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  13 LHGTIQVPGDK-SishrAL-IIGA--MGLGTTTIHNFLFSQDCLTTLQALKNFGVDISQN-NETVIIHGQGLQSWHAPAH 87
Cdd:COG0766    12 LSGEVRISGAKnA----ALpILAAalLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdGGTLTIDASNINSTEAPYE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089  88 AldmgnsGTTTR---LLAG-LLA--GRpFTTTLIGDQSLSQRPMQRIQHPLQKMGAVIHLTHGHlpMTISGQPLHSLCYQ 161
Cdd:COG0766    88 L------VRKMRasiLVLGpLLArfGE-ARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGY--IEARAGRLKGARIY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 162 MPLASAQVKSALILAALQASDASTI----MEklPtrdhtE-----RLLRQFGAHLT---TSddyyKINIQPAHQLQGQTI 229
Cdd:COG0766   159 LDFPSVGATENIMMAAVLAEGTTVIenaaRE--P-----EivdlaNFLNAMGAKIEgagTD----TITIEGVEKLHGAEH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 230 QIPADLSSAAFFLTAAsIIPHSQLQLTNVGLNPTRTgFLKVLQRMGGQVKITAQSqengeprgnLEVSAA-KLHPIVITA 308
Cdd:COG0766   228 TVIPDRIEAGTFLVAA-AITGGDVTVKNVIPEHLEA-VLAKLREAGVEIEEGDDG---------IRVRGPgRLKAVDIKT 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315089 309 TEIPNI-IDEIPLIALLAATADGRSKITgagelrvkET---DR-IHttVEELSKLGiaitelADgFIIDGRQpwSVIN-- 381
Cdd:COG0766   297 APYPGFpTDLQAQFMALLTQAEGTSVIT--------ETvfeNRfMH--VDELNRMG------AD-IKLDGHT--AIVRgv 357
                         410       420
                  ....*....|....*....|....*.
gi 2335315089 382 PHLdsHG------DHRIGMMLAIAAL 401
Cdd:COG0766   358 TKL--SGapvmatDLRAGAALVLAGL 381
 
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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