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Conserved domains on  [gi|857999380|emb|CDT84338|]
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3-phosphoshikimate 1-carboxyvinyltransferase [Vibrio coralliirubri]

Protein Classification

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

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

EC:  2.5.1.19
Gene Ontology:  GO:0009073|GO:0008652|GO:0003866|GO:0009423
PubMed:  8973316|17348837
SCOP:  4001425

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 1-424 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: 626.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVcEVTGVGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTL-RVTGVGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKAlDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENeNYPPLKITGTGLKS 160
Cdd:COG0128   80 GLKEPDA-VLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGG-GYLPLTIRGGPLKG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 161 GAVSIDGSISSQFLTAFLMAAPLAEGEVTIKIDGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSaPGDFLV 240
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 241 EGDASSASYFLAAAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRCGELKGIDMDYNHIPDAAMTIA 320
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 321 TTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELTHAAIDTYDDHRMAMCFSLVAL-SD 399
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396

                        410       420
                 ....*....|....*....|....*
gi 857999380 400 TPVTINDPGCTSKTFPDYFDKLKML 424
Cdd:COG0128  397 GPVTIDDAECVAKSFPDFFELLESL 421
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 1-424 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: 626.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVcEVTGVGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTL-RVTGVGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKAlDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENeNYPPLKITGTGLKS 160
Cdd:COG0128   80 GLKEPDA-VLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGG-GYLPLTIRGGPLKG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 161 GAVSIDGSISSQFLTAFLMAAPLAEGEVTIKIDGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSaPGDFLV 240
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 241 EGDASSASYFLAAAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRCGELKGIDMDYNHIPDAAMTIA 320
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 321 TTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELTHAAIDTYDDHRMAMCFSLVAL-SD 399
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396

                        410       420
                 ....*....|....*....|....*
gi 857999380 400 TPVTINDPGCTSKTFPDYFDKLKML 424
Cdd:COG0128  397 GPVTIDDAECVAKSFPDFFELLESL 421
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
1-421 0e+00

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 612.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVceVTGVGG 80
Cdd:PRK11860   4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKAlDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKITGTGLK- 159
Cdd:PRK11860  82 QFPVKQA-DLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLRl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 160 SGAVSIDGSISSQFLTAFLMAAPLAEG-EVTIKIDGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPGDF 238
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLVARrDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 239 LVEGDASSASYFLAAAAIKGGE-IKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISR--CGELKGIDMDYNHIPDA 315
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRrgAWPLKAIDLDCNHIPDA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 316 AMTIATTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNP---VAELTHAAIDTYDDHRMAMCF 392
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPpaqAADWKAAAIHTYDDHRMAMCF 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 857999380 393 SLVAL--SDTPVTINDPGCTSKTFPDYFDKL 421
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEAL 431
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 12-424 0e+00

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: 553.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  12 VNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLsaDKTVCEVTGVGGAFSSDKAlDLF 91
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEE--EGGTVEIVGGGGLGLPPEA-VLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  92 LGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLkITGTGLKSGAVSIDGSISS 171
Cdd:cd01556   78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL-IGGGGLKGGEVEIPGAVSS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 172 QFLTAFLMAAPLAEGEVTIKIdGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPgDFLVEGDASSASYFL 251
Cdd:cd01556  157 QFKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 252 AAAAIKGGEIKVTGIGKNSiqGDIQFADALEKMGAEIEWGDDY--VISRCGELKGIDMDYNHIPDAAMTIATTALFAKGT 329
Cdd:cd01556  235 AAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNEDtvVVESGGKLKGIDIDGNDIPDEAPTLAVLAAFAEGP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 330 TAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPV-AELTHAAIDTYDDHRMAMCFSLVAL-SDTPVTINDP 407
Cdd:cd01556  313 TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGpLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDP 392

                        410
                 ....*....|....*..
gi 857999380 408 GCTSKTFPDYFDKLKML 424
Cdd:cd01556  393 ECVAKSFPNFFEDLESL 409
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-421 3.05e-174

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 493.35  E-value: 3.05e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380    7 QPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVD-YQLSADKTVCEVTGVGGAFSSD 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEiIKLDDEKSVVIVEGLGGSFEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   86 KALDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKITGtgLKSGAVSI 165
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRG--LRLGGIHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  166 DGSISSQFLTAFLMAAP-LAEGEVTIKidgELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPGDFLVEGDA 244
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAAlLAEGTTTIE---NLASEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPGQEYRVEGDR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  245 SSASYFLAAAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRCG-ELKGIDMDYNHIPDAAMTIATTA 323
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPpGLRGKAVDIRTAPDPAPTTAVLA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  324 LFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVA-ELTHAAIDTYDDHRMAMCFSLVAL-SDTP 401
Cdd:pfam00275 316 AFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYGDHRIAMALALAGLvAEGE 395

                         410       420
                  ....*....|....*....|
gi 857999380  402 VTINDPGCTSKTFPDYFDKL 421
Cdd:pfam00275 396 TIIDDIECTDRSFPDFEEKL 415
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 14-424 5.83e-167

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: 474.84  E-value: 5.83e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   14 GEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVceVTGVGGAFSSDKaldLFLG 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAV--IEGVGGKEPQAE---LDLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   94 NAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKITGtGLKSGAVSIDGSISSQF 173
Cdd:TIGR01356  76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISG-PLPGGIVYISGSASSQY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  174 LTAFLMAAPlAEGEVTIKIDGE-LVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYsAPGDFLVEGDASSASYFLA 252
Cdd:TIGR01356 155 KSALLLAAP-ALQAVGITIVGEpLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKY-GPQGYDVPGDYSSAAFFLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  253 AAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRCG-ELKGIDMDYNHIPDAAMTIATTALFAKGTTA 331
Cdd:TIGR01356 233 AAAITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTR 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  332 IRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELTHAAIDTYDDHRMAMCFSLVAL-SDTPVTINDPGCT 410
Cdd:TIGR01356 313 ITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECV 392

                         410
                  ....*....|....
gi 857999380  411 SKTFPDYFDKLKML 424
Cdd:TIGR01356 393 AKSFPSFFDVLERL 406
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 1-424 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: 626.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVcEVTGVGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTL-RVTGVGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKAlDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENeNYPPLKITGTGLKS 160
Cdd:COG0128   80 GLKEPDA-VLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGG-GYLPLTIRGGPLKG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 161 GAVSIDGSISSQFLTAFLMAAPLAEGEVTIKIDGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSaPGDFLV 240
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 241 EGDASSASYFLAAAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRCGELKGIDMDYNHIPDAAMTIA 320
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 321 TTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELTHAAIDTYDDHRMAMCFSLVAL-SD 399
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396

                        410       420
                 ....*....|....*....|....*
gi 857999380 400 TPVTINDPGCTSKTFPDYFDKLKML 424
Cdd:COG0128  397 GPVTIDDAECVAKSFPDFFELLESL 421
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
1-421 0e+00

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 612.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVceVTGVGG 80
Cdd:PRK11860   4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKAlDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKITGTGLK- 159
Cdd:PRK11860  82 QFPVKQA-DLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLRl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 160 SGAVSIDGSISSQFLTAFLMAAPLAEG-EVTIKIDGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPGDF 238
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLVARrDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 239 LVEGDASSASYFLAAAAIKGGE-IKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISR--CGELKGIDMDYNHIPDA 315
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRrgAWPLKAIDLDCNHIPDA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 316 AMTIATTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNP---VAELTHAAIDTYDDHRMAMCF 392
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPpaqAADWKAAAIHTYDDHRMAMCF 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 857999380 393 SLVAL--SDTPVTINDPGCTSKTFPDYFDKL 421
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEAL 431
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 1-425 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 602.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYqlsaDKTVCEVTGVGG 80
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI----EDDEVVVEGVGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKALDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYlENENYPPLKITGtGLKS 160
Cdd:PRK02427  78 GGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRG-GKKG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 161 GAVSIDGSISSQFLTAFLMAAPL-AEGEVTIKIDGELVSKPYIDITLHIMKQFGVDVINND---YQEFVIPTGQSYsAPG 236
Cdd:PRK02427 156 GPIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEgwgYRRIVIKGGQRL-RGQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 237 DFLVEGDASSASYFLAAAAIKGG-EIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDY--------VISRCGELKGIDM 307
Cdd:PRK02427 235 DITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEReggepvgdIRVRSSELKGIDI 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 308 DYNHIPDAAMTIATTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAelTHAAIDTYDDHR 387
Cdd:PRK02427 315 DIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP--LAGVVDSYGDHR 392

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 857999380 388 MAMCFSLVAL-SDTPVTINDPGCTSKTFPDYFDKLKMLS 425
Cdd:PRK02427 393 IAMAFAIAGLaAEGPVTIDDPECVAKSFPDFFEDLASLG 431
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
 1-425 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 574.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVCEVTGVGG 80
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKA----LDLFLGNAGTAMRPLAAALCL--GRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKIT 154
Cdd:PLN02338  81 KFPVSGDskedVELFLGNAGTAMRPLTAAVTAagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 155 GT-GLKSGAVSIDGSISSQFLTAFLMAAPLAEGEVTIKIDGELVSKPYIDITLHIMKQFGVDV-INNDYQEFVIPTGQSY 232
Cdd:PLN02338 161 AAgGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVeHSDSWDRFFIKGGQKY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 233 SAPGDFLVEGDASSASYFLAAAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYV--------ISRCGELKG 304
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVtvtgpprdAFGGKHLKA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 305 IDMDYNHIPDAAMTIATTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELTHAAIDTYD 384
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYD 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 857999380 385 DHRMAMCFSLVALSDTPVTINDPGCTSKTFPDYFDKLKMLS 425
Cdd:PLN02338 401 DHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIA 441
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 12-424 0e+00

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: 553.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  12 VNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLsaDKTVCEVTGVGGAFSSDKAlDLF 91
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEE--EGGTVEIVGGGGLGLPPEA-VLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  92 LGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLkITGTGLKSGAVSIDGSISS 171
Cdd:cd01556   78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL-IGGGGLKGGEVEIPGAVSS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 172 QFLTAFLMAAPLAEGEVTIKIdGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPgDFLVEGDASSASYFL 251
Cdd:cd01556  157 QFKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 252 AAAAIKGGEIKVTGIGKNSiqGDIQFADALEKMGAEIEWGDDY--VISRCGELKGIDMDYNHIPDAAMTIATTALFAKGT 329
Cdd:cd01556  235 AAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNEDtvVVESGGKLKGIDIDGNDIPDEAPTLAVLAAFAEGP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 330 TAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPV-AELTHAAIDTYDDHRMAMCFSLVAL-SDTPVTINDP 407
Cdd:cd01556  313 TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGpLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDP 392

                        410
                 ....*....|....*..
gi 857999380 408 GCTSKTFPDYFDKLKML 424
Cdd:cd01556  393 ECVAKSFPNFFEDLESL 409
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-421 3.05e-174

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 493.35  E-value: 3.05e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380    7 QPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVD-YQLSADKTVCEVTGVGGAFSSD 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEiIKLDDEKSVVIVEGLGGSFEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   86 KALDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKITGtgLKSGAVSI 165
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRG--LRLGGIHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  166 DGSISSQFLTAFLMAAP-LAEGEVTIKidgELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPGDFLVEGDA 244
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAAlLAEGTTTIE---NLASEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPGQEYRVEGDR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  245 SSASYFLAAAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRCG-ELKGIDMDYNHIPDAAMTIATTA 323
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPpGLRGKAVDIRTAPDPAPTTAVLA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  324 LFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVA-ELTHAAIDTYDDHRMAMCFSLVAL-SDTP 401
Cdd:pfam00275 316 AFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYGDHRIAMALALAGLvAEGE 395

                         410       420
                  ....*....|....*....|
gi 857999380  402 VTINDPGCTSKTFPDYFDKL 421
Cdd:pfam00275 396 TIIDDIECTDRSFPDFEEKL 415
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 14-424 5.83e-167

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: 474.84  E-value: 5.83e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   14 GEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVceVTGVGGAFSSDKaldLFLG 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAV--IEGVGGKEPQAE---LDLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   94 NAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKITGtGLKSGAVSIDGSISSQF 173
Cdd:TIGR01356  76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISG-PLPGGIVYISGSASSQY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  174 LTAFLMAAPlAEGEVTIKIDGE-LVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYsAPGDFLVEGDASSASYFLA 252
Cdd:TIGR01356 155 KSALLLAAP-ALQAVGITIVGEpLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKY-GPQGYDVPGDYSSAAFFLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  253 AAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRCG-ELKGIDMDYNHIPDAAMTIATTALFAKGTTA 331
Cdd:TIGR01356 233 AAAITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTR 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  332 IRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELTHAAIDTYDDHRMAMCFSLVAL-SDTPVTINDPGCT 410
Cdd:TIGR01356 313 ITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECV 392

                         410
                  ....*....|....
gi 857999380  411 SKTFPDYFDKLKML 424
Cdd:TIGR01356 393 AKSFPSFFDVLERL 406
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 1-425 1.28e-165

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 481.13  E-value: 1.28e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVdyQLSADKTVCEVTGVGG 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGV--KLSRDGGTCVVGGTRG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSdKALDLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKITGTGLKS 160
Cdd:PRK11861 318 AFTA-KTADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISV 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 161 GA-VSIDGSISSQFLTAFLMAAPLA---EGEVTIKIDGELVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPG 236
Cdd:PRK11861 397 DApIRVRGDVSSQFLTALLMTLPLVkakDGASVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPG 476

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 237 DFLVEGDASSASYFLAAAAIKGGEIKVTGIGKNSIQGDIQFADALEKMGAEIEWGDDYVISRC-----GELKGIDMDYNH 311
Cdd:PRK11861 477 TIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVRGighdhGRLAPIDMDFNL 556

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 312 IPDAAMTIATTALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELT-HAAIDTYDDHRMAM 390
Cdd:PRK11861 557 IPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTpNASIDTYDDHRMAM 636

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 857999380 391 CFSLVALSDTPVTINDPGCTSKTFPDYFDKLKMLS 425
Cdd:PRK11861 637 CFSLVSLGGVPVRINDPKCVGKTFPDYFDRFLALA 671
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
 12-424 2.44e-164

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: 468.24  E-value: 2.44e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  12 VNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSAdkTVCEVTGVGGAFSSDKALDLF 91
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  92 LGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLENENYPPLKItGTGLKSGAVSIDGSISS 171
Cdd:cd01554   79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLK-GGKNLGPIHYEDPIASA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 172 QFLTAFLMAAPLAEGEVTIKIDgelVSKPYIDITLHIMKQFGVDVINNDYQEFVIPTGQSYSAPgDFLVEGDASSASYFL 251
Cdd:cd01554  158 QVKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 252 AAAAIKGGEIKVTGIGKNSiqGDIQFADALEKMGAEIEWGDDYVISRCGELKGIDMDYNHIP---DAAMTIATTALFAKG 328
Cdd:cd01554  234 VAAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQG 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 329 TTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPVAELTHAAIDTYDDHRMAMCFSLVAL-SDTPVTINDP 407
Cdd:cd01554  312 TTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRA 391

                        410
                 ....*....|....*..
gi 857999380 408 GCTSKTFPDYFDKLKML 424
Cdd:cd01554  392 EAINTSYPSFFDDLESL 408
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
 241-424 2.00e-49

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: 167.07  E-value: 2.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 241 EGDASSASYFLAAAAIKGGEIKVTGIGKNS-----IQGDIQFADALEKM-GAEIEWG---DDYVISRCGELKGIDMDYNH 311
Cdd:cd01553    7 KGGGQILRSFLVLAAISGGPITVTGIRPDRakpglLRQHLTFLKALEKIcGATVEGGelgSDRISFRPGTVRGGDVRFAI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 312 -----IPDAAMTIATTALFAKGTTAIRNVYNWRV----KETDRLAAMATELRKVGAEVEEGED------------YIIVN 370
Cdd:cd01553   87 gsagsCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEVS 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 857999380 371 PVAELTHAAIdtyddhRMAMCFSLVAlsdTPVTINDPGCTSKTFPDYFDKLKML 424
Cdd:cd01553  167 PVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 3-417 8.44e-49

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 177.11  E-value: 8.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   3 SLTLQPIQKVNGEVNLPGSKSVSNRALLLAALSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVcEVTGVG--G 80
Cdd:PRK14806 303 SYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEGPHNGRV-TIHGVGlhG 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKAldLFLGNAGTAMRPLAAALCLGRGEYVLTGEPRMKERPIGHLVTALREAGADVEYLEnENYPPLKITGtGLKS 160
Cdd:PRK14806 382 LKAPPGP--LYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIETGE-EGRPPLSIRG-GQRL 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 161 GAVSIDGSI-SSQFLTAFLMAAPLAEGEVTIKidgELvsKPYIDITLHIMKQFGVDViNNDYQEFVIPTGQSYSApGDFL 239
Cdd:PRK14806 458 KGIHYDLPMaSAQVKSCLLLAGLYAEGETSVT---EP--APTRDHTERMLRGFGYPV-KVEGNTISVEGGGKLTA-TDIE 530

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 240 VEGDASSASYFLAAAAI-KGGEIKVTGIGKNSIQgdIQFADALEKMGAEIEWGDDYVIS---------RCGELKGIDMDY 309
Cdd:PRK14806 531 VPADISSAAFFLVAASIaEGSELTLEHVGINPTR--TGVIDILKLMGADITLENEREVGgepvadirvRGARLKGIDIPE 608

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 310 NHIPDA-----AMTIAttALFAKGTTAIRNVYNWRVKETDRLAAMATELRKVGAEVEEGEDYIIVNPvAELTHAAIDTYD 384
Cdd:PRK14806 609 DQVPLAidefpVLFVA--AACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEG-GIFGGGEVESHG 685

                        410       420       430
                 ....*....|....*....|....*....|....
gi 857999380 385 DHRMAMCFSLVAL-SDTPVTINDPGCTSKTFPDY 417
Cdd:PRK14806 686 DHRIAMSFSVASLrASGPITIHDCANVATSFPNF 719
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 1-376 3.71e-19

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: 88.89  E-value: 3.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKsvsNRAL-LLAA--LSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVcEVTG 77
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAK---NAALpILAAalLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTL-TIDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  78 vgGAFSSDKA-LDLflgnaGTAMRplAAALCLGrgeyVLTGepRMKE-------------RPIG-HLvTALREAGADVEY 142
Cdd:COG0766   77 --SNINSTEApYEL-----VRKMR--ASILVLG----PLLA--RFGEarvslpggcaigaRPIDlHL-KGLEALGAEIEI 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 143 lENENYpplKITGTGLKSGAVSIDgsISSqfLTA---FLMAAPLAEGEVTI---------------------KIDGELVS 198
Cdd:COG0766  141 -EHGYI---EARAGRLKGARIYLD--FPS--VGAtenIMMAAVLAEGTTVIenaarepeivdlanflnamgaKIEGAGTD 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 199 kpyidiTLHImkqFGVDVINndyqefviptGQSYSAPGDFLVegdassASYFLAAAAIKGGEIKVTGIgknsIQGDIQ-F 277
Cdd:COG0766  213 ------TITI---EGVEKLH----------GAEHTVIPDRIE------AGTFLVAAAITGGDVTVKNV----IPEHLEaV 263

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 278 ADALEKMGAEIEWGDDYV-ISRCGELKGID---MDYNHIP-D---AAMTIATTalfAKGTTAIR-NVYNWRVKETDrlaa 348
Cdd:COG0766  264 LAKLREAGVEIEEGDDGIrVRGPGRLKAVDiktAPYPGFPtDlqaQFMALLTQ---AEGTSVITeTVFENRFMHVD---- 336

                        410       420
                 ....*....|....*....|....*....
gi 857999380 349 matELRKVGAEVE-EGeDYIIVNPVAELT 376
Cdd:COG0766  337 ---ELNRMGADIKlDG-HTAIVRGVTKLS 361
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
 13-397 1.38e-14

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: 74.82  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  13 NGEVNLPGSKsvsNRAL-LLAA--LSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTV---------CEVTGvgG 80
Cdd:cd01555    2 SGEVRISGAK---NAALpILAAalLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLvidasninsTEAPY--E 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  81 AFSSDKALDLFLGnagtamrPLAAALclGRGEYVLTGEPRMKERPIG-HLVtALREAGADVEyLENENYppLKITGTGLK 159
Cdd:cd01555   77 LVRKMRASILVLG-------PLLARF--GEARVSLPGGCAIGARPVDlHLK-GLEALGAKIE-IEDGYV--EAKAAGRLK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 160 sGA------VSIDGSISSqfltafLMAAPLAEGEVTI---------------------KIDGelVSKPYIDITlhimkqf 212
Cdd:cd01555  144 -GAriyldfPSVGATENI------MMAAVLAEGTTVIenaarepeivdlanflnkmgaKIEG--AGTDTIRIE------- 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 213 GVDVInndyqefvipTGQSYSAPGDFLVEGDassasyFLAAAAIKGGEIKVTGIGKNSIqgdIQFADALEKMGAEIEWGD 292
Cdd:cd01555  208 GVERL----------HGAEHTVIPDRIEAGT------FLVAAAITGGDITVENVIPEHL---EAVLAKLREMGAKIEIGE 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 293 D--YVISRCGELKGIDMDYNHIP----DAAMTIATTALFAKGTTAIR-NVYNWRVKETDrlaamatELRKVGAEVEEGED 365
Cdd:cd01555  269 DgiRVDGDGGRLKAVDIETAPYPgfptDLQAQFMALLTQAEGTSVITeTIFENRFMHVD-------ELNRMGADIKVEGN 341

                        410       420       430
                 ....*....|....*....|....*....|..
gi 857999380 366 YIIVNPVAELTHAAIDTyDDHRMAMCFSLVAL 397
Cdd:cd01555  342 TAIIRGVTKLSGAPVMA-TDLRAGAALVLAGL 372
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 178-380 1.28e-10

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: 62.70  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 178 LMAAPLAEGEVTIK-----IDgelvskpyIDITLHIMKQFGVDVINNDYQEFVIPTGQ--SYSAPGDFlvegdASS--AS 248
Cdd:COG0766   29 LAAALLTDGPVTLRnvpdlSD--------VRTMLELLESLGVKVERDDGGTLTIDASNinSTEAPYEL-----VRKmrAS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 249 YFLAAAAI-KGGEIKVT---G--IGKNSIqgDIQFaDALEKMGAEIEWGDDYVISRCGELKG--IDMDY-------Nhip 313
Cdd:COG0766   96 ILVLGPLLaRFGEARVSlpgGcaIGARPI--DLHL-KGLEALGAEIEIEHGYIEARAGRLKGarIYLDFpsvgateN--- 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 857999380 314 daAMTIATtalFAKGTTAIRNVYnwrvKE---TDrLAAMateLRKVGAEVE-EGEDYIIVNPVAEL---THAAI 380
Cdd:COG0766  170 --IMMAAV---LAEGTTVIENAA----REpeiVD-LANF---LNAMGAKIEgAGTDTITIEGVEKLhgaEHTVI 230
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
 1-306 1.50e-10

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 62.74  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKsvsNRAL-LLAA--LSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVcevtg 77
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAK---NAALpILAAslLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTV----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  78 vggAFSSDKALD---------------LFLGnagtamrPLAAALclGRGEYVLTGEPRMKERPIG-HLvTALREAGADVE 141
Cdd:PRK09369  73 ---TIDASNINNteapyelvkkmrasiLVLG-------PLLARF--GEAKVSLPGGCAIGARPVDlHL-KGLEALGAEIE 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 142 ylENENYPPLKITGtGLKsGA------VSIDGSISsqfltaFLMAAPLAEGEVTI---------------------KIDG 194
Cdd:PRK09369 140 --IEHGYVEAKADG-RLK-GAhivldfPSVGATEN------ILMAAVLAEGTTVIenaarepeivdlanflnkmgaKISG 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 195 ELVSkpyidiTLHImkqFGVDVINndyqefviptGQSYSAPGDFLVEGDassasyFLAAAAIKGGEIKVTGIgknsIQGD 274
Cdd:PRK09369 210 AGTD------TITI---EGVERLH----------GAEHTVIPDRIEAGT------FLVAAAITGGDVTIRGA----RPEH 260

                        330       340       350
                 ....*....|....*....|....*....|....
gi 857999380 275 IQ-FADALEKMGAEIEWGDDYV-ISRCGELKGID 306
Cdd:PRK09369 261 LEaVLAKLREAGAEIEEGEDGIrVDMPGRLKAVD 294
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
 1-378 7.90e-09

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 57.17  E-value: 7.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380   1 MESLTLQPIQKVNGEVNLPGSKSvSNRALLLAA-LSTGTTRLTNLLDSDDIRHMLNALTQLGVDYQLSADKTVCEVTGV- 78
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKN-SAVALIPAAiLADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIq 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380  79 -----GGAFSSDKALDLFLGnagtAMrplaaalcLGR-GEYV--LTGEPRMKERPIGHLVTALREAGADVEYlENENypp 150
Cdd:PRK12830  80 smplpNGKVKSLRASYYFMG----AL--------LGRfKKAVvgLPGGCDLGPRPIDQHIKGFEALGAEVTN-EGGA--- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 151 LKITGTGLKsGA------VSIDGSISsqfltaFLMAAPLAEGEVTIkidgELVSK-PYI-DI-TL------HImKQFGVD 215
Cdd:PRK12830 144 IYLKADELK-GAhiyldvVSVGATIN------IMLAAVKAKGRTVI----ENAAKePEIiDVaTLlnnmgaNI-KGAGTD 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 216 VIN---------NDYQefVIPtgqsysapgdflvegDASSASYFLAAAAIKGGEIKVTGIGKNSIQGdiqFADALEKMGA 286
Cdd:PRK12830 212 VIRiegvdelhgCRHT--VIP---------------DRIEAGTYMILAAACGGGVTINNVIPEHLES---FIAKLEEMGV 271

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 287 EIEWGDDYV-ISRCGELKGID---MDYNHIP-DAAMTIATTALFAKGTTAIR-NVYNWRVKETDrlaamatELRKVGAEV 360
Cdd:PRK12830 272 RVEVNEDSIfVEKQGNLKAVDiktLPYPGFAtDLQQPLTPLLLKANGRSVVTdTIYEKRFKHVD-------ELKRMGANI 344

                        410
                 ....*....|....*...
gi 857999380 361 EEGEDYIIVNPVAELTHA 378
Cdd:PRK12830 345 KVEGRSAIITGPSKLTGA 362
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
 178-380 7.46e-08

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 54.27  E-value: 7.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 178 LMAAPLAEGEVTIK-----IDgelvskpyIDITLHIMKQFGVDVINNDYQEFVIPTGQ--SYSAPGDfLVegDASSASYF 250
Cdd:PRK09369  29 LAASLLAEEPVTLTnvpdlSD--------VRTMIELLRSLGAKVEFDGNGTVTIDASNinNTEAPYE-LV--KKMRASIL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857999380 251 LAAAAI-KGGEIKVT---G--IGKNSIqgDIQFaDALEKMGAEIEWGDDYVISRC-GELKG--IDMDYnhiPD--AAMTI 319
Cdd:PRK09369  98 VLGPLLaRFGEAKVSlpgGcaIGARPV--DLHL-KGLEALGAEIEIEHGYVEAKAdGRLKGahIVLDF---PSvgATENI 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 857999380 320 ATTALFAKGTTAIRNVynwrVKE---TDrLAAMateLRKVGAEVE-EGEDYIIVNPVAEL---THAAI 380
Cdd:PRK09369 172 LMAAVLAEGTTVIENA----AREpeiVD-LANF---LNKMGAKISgAGTDTITIEGVERLhgaEHTVI 231
 
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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