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Conserved domains on  [gi|446333413|ref|WP_000411268|]
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MULTISPECIES: UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Bacillus]

Protein Classification

UDP-N-acetylglucosamine 1-carboxyvinyltransferase( domain architecture ID 10793226)

UDP-N-acetylglucosamine 1-carboxyvinyltransferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-417 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


:

Pssm-ID: 236486  Cd Length: 417  Bit Score: 708.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFE-NNQVTIDASKE 79
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  80 LNIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGELKGAKIY 159
Cdd:PRK09369  80 NNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 160 LDFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGT 239
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 240 FMVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDKLKAVDIKTMPHPGFPTDMQSQMMALLLQAD 319
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 320 GTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRG 399
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
                        410
                 ....*....|....*...
gi 446333413 400 YVDFHKKLAALGATIERV 417
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-417 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 708.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFE-NNQVTIDASKE 79
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  80 LNIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGELKGAKIY 159
Cdd:PRK09369  80 NNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 160 LDFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGT 239
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 240 FMVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDKLKAVDIKTMPHPGFPTDMQSQMMALLLQAD 319
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 320 GTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRG 399
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
                        410
                 ....*....|....*...
gi 446333413 400 YVDFHKKLAALGATIERV 417
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-417 0e+00

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: 700.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVF-ENNQVTIDASKE 79
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLT-DGPVTLRNVPDLSDVRTMLELLESLGVKVERdDGGTLTIDASNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  80 LNIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGeLKGAKIY 159
Cdd:COG0766   80 NSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGR-LKGARIY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 160 LDFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGT 239
Cdd:COG0766  159 LDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 240 FMVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDKLKAVDIKTMPHPGFPTDMQSQMMALLLQAD 319
Cdd:COG0766  239 FLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 320 GTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDlraaaalilaglVSEGYTRVTELKHLDRG 399
Cdd:COG0766  319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDlragaalvlaglAAEGETVIDNIYHIDRG 398
                        410
                 ....*....|....*...
gi 446333413 400 YVDFHKKLAALGATIERV 417
Cdd:COG0766  399 YENLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-410 0e+00

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: 627.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  12 LNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFEN-NQVTIDASKELNIEAPFEYVR 90
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  91 KMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGELKGAKIYLDFPSVGATEN 170
Cdd:cd01555   80 KMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 171 IMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGTFMVAAAITGGD 250
Cdd:cd01555  160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 251 ILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDK-LKAVDIKTMPHPGFPTDMQSQMMALLLQADGTSMITETVF 329
Cdd:cd01555  240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 330 ENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRGYVDFHKKLAA 409
Cdd:cd01555  320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399

                 .
gi 446333413 410 L 410
Cdd:cd01555  400 L 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 162190 [Multi-domain]  Cd Length: 416  Bit Score: 612.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413    1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFENNQVTIDASKEL 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLT-DEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNIN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   81 NIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGELKGAKIYL 160
Cdd:TIGR01072  80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  161 DFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGTF 240
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  241 MVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIG-PDKLKAVDIKTMPHPGFPTDMQSQMMALLLQAD 319
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMrQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  320 GTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRG 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
                         410
                  ....*....|....*..
gi 446333413  400 YVDFHKKLAALGATIER 416
Cdd:TIGR01072 400 YEDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-407 8.72e-132

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 385.88  E-value: 8.72e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413    7 RGGKRLNGTVRVEG-AKNAVLPIIAAALLAsdGKNVLSEVPVLSDVYTINEVLRHLNAEVVFE--NNQVTIDASKELNIE 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAA--GESTITNLLDSDDTLTMLEALRALGAEIIKLddEKSVVIVEGLGGSFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   84 APFEYVRKMRASVQVMGPLLARNGRAR--IALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVE---GELKGAKI 158
Cdd:pfam00275  79 APEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  159 YLDFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGT-IRIEGVDKLYGGNHSIIPDRIEA 237
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  238 GTFMVAAAITGGDILIENAVPEHLR---SITAKMEEMGVKIIEENEGVRVIGPDKL--KAVDIKTMPHPGFPTDMQSQMM 312
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLQgdeALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  313 ALLLQADGTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGP-NSLQGAEVGAT-DLRAAAALILAGLVSEGYTRV 390
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAvKELKGAEVDSYgDHRIAMALALAGLVAEGETII 398
                         410
                  ....*....|....*..
gi 446333413  391 TELKHLDRGYVDFHKKL 407
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-417 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 708.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFE-NNQVTIDASKE 79
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  80 LNIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGELKGAKIY 159
Cdd:PRK09369  80 NNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 160 LDFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGT 239
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 240 FMVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDKLKAVDIKTMPHPGFPTDMQSQMMALLLQAD 319
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 320 GTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRG 399
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
                        410
                 ....*....|....*...
gi 446333413 400 YVDFHKKLAALGATIERV 417
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-417 0e+00

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: 700.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVF-ENNQVTIDASKE 79
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLT-DGPVTLRNVPDLSDVRTMLELLESLGVKVERdDGGTLTIDASNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  80 LNIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGeLKGAKIY 159
Cdd:COG0766   80 NSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGR-LKGARIY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 160 LDFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGT 239
Cdd:COG0766  159 LDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 240 FMVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDKLKAVDIKTMPHPGFPTDMQSQMMALLLQAD 319
Cdd:COG0766  239 FLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 320 GTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDlraaaalilaglVSEGYTRVTELKHLDRG 399
Cdd:COG0766  319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDlragaalvlaglAAEGETVIDNIYHIDRG 398
                        410
                 ....*....|....*...
gi 446333413 400 YVDFHKKLAALGATIERV 417
Cdd:COG0766  399 YENLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-410 0e+00

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: 627.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  12 LNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFEN-NQVTIDASKELNIEAPFEYVR 90
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  91 KMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGELKGAKIYLDFPSVGATEN 170
Cdd:cd01555   80 KMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 171 IMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGTFMVAAAITGGD 250
Cdd:cd01555  160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 251 ILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDK-LKAVDIKTMPHPGFPTDMQSQMMALLLQADGTSMITETVF 329
Cdd:cd01555  240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 330 ENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRGYVDFHKKLAA 409
Cdd:cd01555  320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399

                 .
gi 446333413 410 L 410
Cdd:cd01555  400 L 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 162190 [Multi-domain]  Cd Length: 416  Bit Score: 612.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413    1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFENNQVTIDASKEL 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLT-DEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNIN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   81 NIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEGELKGAKIYL 160
Cdd:TIGR01072  80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  161 DFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGTF 240
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  241 MVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIG-PDKLKAVDIKTMPHPGFPTDMQSQMMALLLQAD 319
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMrQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  320 GTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRG 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
                         410
                  ....*....|....*..
gi 446333413  400 YVDFHKKLAALGATIER 416
Cdd:TIGR01072 400 YEDLEEKLRALGAKIER 416
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-417 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 551.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFENNQVTIDASKEL 80
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILA-DGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  81 NIEAPFEYVRKMRASVQVMGPLLARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVEgELKGAKIYL 160
Cdd:PRK12830  80 SMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKAD-ELKGAHIYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 161 DFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGTF 240
Cdd:PRK12830 159 DVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 241 MVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIGPDKLKAVDIKTMPHPGFPTDMQSQMMALLLQADG 320
Cdd:PRK12830 239 MILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 321 TSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGATDLRAAAALILAGLVSEGYTRVTELKHLDRGY 400
Cdd:PRK12830 319 RSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGY 398
                        410
                 ....*....|....*..
gi 446333413 401 VDFHKKLAALGATIERV 417
Cdd:PRK12830 399 SNIIEKLKALGADIWRE 415
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-407 8.72e-132

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 385.88  E-value: 8.72e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413    7 RGGKRLNGTVRVEG-AKNAVLPIIAAALLAsdGKNVLSEVPVLSDVYTINEVLRHLNAEVVFE--NNQVTIDASKELNIE 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAA--GESTITNLLDSDDTLTMLEALRALGAEIIKLddEKSVVIVEGLGGSFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   84 APFEYVRKMRASVQVMGPLLARNGRAR--IALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEAYVE---GELKGAKI 158
Cdd:pfam00275  79 APEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  159 YLDFPSVGATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGT-IRIEGVDKLYGGNHSIIPDRIEA 237
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  238 GTFMVAAAITGGDILIENAVPEHLR---SITAKMEEMGVKIIEENEGVRVIGPDKL--KAVDIKTMPHPGFPTDMQSQMM 312
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLQgdeALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  313 ALLLQADGTSMITETVFENRFMHVEEFRRMNADIKIEGRSVIMNGP-NSLQGAEVGAT-DLRAAAALILAGLVSEGYTRV 390
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAvKELKGAEVDSYgDHRIAMALALAGLVAEGETII 398
                         410
                  ....*....|....*..
gi 446333413  391 TELKHLDRGYVDFHKKL 407
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-410 2.11e-86

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: 269.47  E-value: 2.11e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  12 LNGTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFENNQVTIDASKELNIEAP---FEY 88
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLA-EGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPqnaLNL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  89 VRKMRASVQVMGPLLARNGRarIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNGFVEA--YVEGELKGAKIYLD-FPSV 165
Cdd:cd01554   80 GNSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPplLKGGKNLGPIHYEDpIASA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 166 GATENIMSAATLAKGTTILENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGTFMVAAA 245
Cdd:cd01554  158 QVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 246 ITGGDILIENAVP-EHLRSITAKMEEMGVKiIEENEGVRVIGPDKLKAVDIKTMPHPgFPTDMQSQMMALLLQADGTSMI 324
Cdd:cd01554  238 IAPGRLVLQNVGInETRTGIIDVLRAMGAK-IEIGEDTISVESSDLKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 325 TETVF------ENRFMHVEEFRRMNADIKIEGRSVIMNGPNSLQGAEVGAT-DLRAAAALILAGLVSEGYTRVTELKHLD 397
Cdd:cd01554  316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAIN 395
                        410
                 ....*....|...
gi 446333413 398 RGYVDFHKKLAAL 410
Cdd:cd01554  396 TSYPSFFDDLESL 408
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-366 7.78e-22

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: 97.08  E-value: 7.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAK---NAVLpiIAAALlaSDGKNVLSEVPVLSDV-YTINeVLRHLNAEV-VFENNQVTID 75
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL--LLAAL--AEGESTIRNLLESDDTlATLE-ALRALGAEIeELDGGTLRVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  76 aSKELNIEAPFEYVR------KMRasvqVMGPLLA-RNGRARIAlpGGCAIGSRPIDQHLKGFEAMGAKVQ-VGNGFVEA 147
Cdd:COG0128   76 -GVGGGLKEPDAVLDcgnsgtTMR----LLTGLLAlQPGEVVLT--GDESLRKRPMGRLLDPLRQLGARIEsRGGGYLPL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 148 YVEG-ELKGAKIYLDfpsvgatENI---------MSAATLAKGTTILENAAKEPEI-VDLA-NFLNAMGAKVRGAGTGTI 215
Cdd:COG0128  149 TIRGgPLKGGEYEIP-------GSAssqfksallLAGPLAEGGLEITVTGELESKPyRDHTeRMLRAFGVEVEVEGYRRF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 216 RIEGVDKLYGGNHSIIPDRIEAGTFMVAAAITGGDILIENAVPEHLRSITA---KMEEMGVKIIEENEGVRVIGpDKLKA 292
Cdd:COG0128  222 TVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGildILKEMGADIEIENDGITVRG-SPLKG 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 293 VDIktmphPG------FPTdmqsqMMALLLQADGTSMIT--------ETvfeNRF--MhVEEFRRMNADIKIEGRSVIMN 356
Cdd:COG0128  301 IDI-----DLsdipdeAPT-----LAVLAAFAEGTTRIRgaaelrvkES---DRIaaM-ATELRKLGADVEETEDGLIIE 366
                        410
                 ....*....|
gi 446333413 357 GPNSLQGAEV 366
Cdd:COG0128  367 GGPKLKGAEV 376
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
232-410 2.25e-18

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: 83.10  E-value: 2.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 232 PDRIEAGTFMVAAAITGGDILIENAVPEHLRSITAKMEEMGVKIIEENEGVRVIG-----------PDKLKAVDIKTMPH 300
Cdd:cd01553    8 GGGQILRSFLVLAAISGGPITVTGIRPDRAKPGLLRQHLTFLKALEKICGATVEGgelgsdrisfrPGTVRGGDVRFAIG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 301 P-GFPTDMQSQMMALLLQADGTSMITETVF----------ENRFMHVEEFRRMNADIKIE------------GRSVIMNG 357
Cdd:cd01553   88 SaGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETllrhgfypagggVVATEVSP 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446333413 358 PNSLQGAEVGATdlraaaaliLAGLVSEGYTRVTELKHLDRGYVDFHKKLAAL 410
Cdd:cd01553  168 VEKLNTAQLRQL---------VLPMLLASGAVEFTVAHPSCHLLTNFAVLEAL 211
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-412 4.54e-18

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: 85.79  E-value: 4.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   14 GTVRVEGAKNAVLPIIAAALLAsDGKNVLSEVPVLSDVYTINEVLRHLNAEVVFENNQVTIDASKELNIEAPFeyvrKMR 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALA-EGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGKEPQAEL----DLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   94 ASVQVMGPLLARNGRAR--IALPGGCAIGSRPIDQHLKGFEAMGAKV--QVGNGFVEAYVEGELKGAKIYLDfPSVGA-- 167
Cdd:TIGR01356  76 NSGTTARLLTGVLALADgeVVLTGDESLRKRPMGRLVDALRQLGAEIssLEGGGSLPLTISGPLPGGIVYIS-GSASSqy 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  168 -TENIMSAATL-AKGTTIL-ENAAKEPEIVDLANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRIEAGTFMVAA 244
Cdd:TIGR01356 155 kSALLLAAPALqAVGITIVgEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  245 AITGGDILIENAVPEHLR---SITAKMEEMGVKIIEENEGVRVIGPDKLKAV--DIKTMPHPgFPTdmqsqMMALLLQAD 319
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQgdkAIIIVLEEMGADIEVEEDDLIVEGASGLKGIkiDMDDMIDE-LPT-----LAVLAAFAE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  320 GTSMIT--------ETvfeNRFMHV-EEFRRMNADIKIEGRSVIMNGPNSLQGAEVGA-TDLRAAAALILAGLVSEGYTR 389
Cdd:TIGR01356 309 GVTRITgaeelrvkES---DRIAAIaEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTfGDHRIAMAFAVAGLVAEGEVL 385
                         410       420
                  ....*....|....*....|...
gi 446333413  390 VTELKHLDRGYVDFHKKLAALGA 412
Cdd:TIGR01356 386 IDDPECVAKSFPSFFDVLERLGA 408
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-410 5.71e-15

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: 76.06  E-value: 5.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  12 LNGTVRVEGAKN----AvlpIIAAALlaSDGKNVLsEVPVLSD--VYTINeVLRHLNAEVVFENNQVTIDASKELNieAP 85
Cdd:cd01556    1 LSGEITVPGSKSishrA---LLLAAL--AEGESRI-ENLLDSDdtLATLE-ALRALGAKIEEEGGTVEIVGGGGLG--LP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  86 FEYVRKMRASVQVMGPL--LARNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKV--QVGNGFVEAYVEGELKGAKIYLD 161
Cdd:cd01556   72 PEAVLDCGNSGTTMRLLtgLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIegREGGGYPPLIGGGGLKGGEVEIP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 162 FPS----VGAtenIMSAATLAKGTTILENAAKEPEI-VDL-ANFLNAMGAKVRGAGTGTIRIEGVDKLYGGNHSIIPDRI 235
Cdd:cd01556  152 GAVssqfKSA---LLLAAPLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDAS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 236 EAGTFMVAAAITGGDILIENaVPEHL--RSITAKMEEMGVKIIEENEG-VRVIGPDKLKAVDIKTMPHPG-FPTdmqsqm 311
Cdd:cd01556  229 SAAFFLAAAAITGSEIVIKN-VGLNSgdTGIIDVLKEMGADIEIGNEDtVVVESGGKLKGIDIDGNDIPDeAPT------ 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 312 MALL-LQADGTSMIT--------ETvfeNRF--MhVEEFRRMNADIKIEGRSVIMNGPNS-LQGAEV-GATDLRAAAALI 378
Cdd:cd01556  302 LAVLaAFAEGPTRIRnaaelrvkES---DRIaaM-ATELRKLGADVEETEDGLIIEGGPLkGAGVEVyTYGDHRIAMSFA 377
                        410       420       430
                 ....*....|....*....|....*....|..
gi 446333413 379 LAGLVSEGYTRVTELKHLDRGYVDFHKKLAAL 410
Cdd:cd01556  378 IAGLVAEGGVTIEDPECVAKSFPNFFEDLESL 409
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-351 2.47e-11

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 65.16  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAKN----AvlpIIAAALlaSDGKNVLSEVPVLSDV-YTINeVLRHLNAEVvfENNQVTID 75
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSishrA---LLLAAL--AEGETTITNLLRSEDTlATLN-ALRALGVEI--EDDEVVVE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  76 ASKELNIEAPFEYV---------RKMrasvqvMGPLLARNGRARIAlpGGCAIGSRPIDQHLKGFEAMGAKVQVG-NGFV 145
Cdd:PRK02427  74 GVGGGGLKEPEDVLdcgnsgttmRLL------TGLLALQPGEVVLT--GDESLRKRPMGRLLDPLRQMGAKIEGRdEGYL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 146 EAYVEGELKGAKIYLDFPS----V-GAtenIMSAATLAKG---TTILENAAKEPEIVDLANFLNAMGAKVR---GAGTGT 214
Cdd:PRK02427 146 PLTIRGGKKGGPIEYDGPVssqfVkSL---LLLAPLFAEGdteTTVIEPLPSRPHTEITLRMLRAFGVEVEnveGWGYRR 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 215 IRIEGVDKLYGGNHSIIPDRIEAGTFMVAAAITGG-DILIENaVPE-------HLRSItakMEEMGVKIIEENEGVR--- 283
Cdd:PRK02427 223 IVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITN-VGLnstqggkAIIDV---LEKMGADIEIENEREGgep 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 284 ----VIGPDKLKAVDIkTMPHPG--FPTdmqsqMMALLLQADGTSMIT--------ETvfeNRF--MhVEEFRRMNADIK 347
Cdd:PRK02427 299 vgdiRVRSSELKGIDI-DIPDIIdeAPT-----LAVLAAFAEGTTVIRnaeelrvkET---DRIaaM-ATELRKLGAEVE 368
                        410
                 ....*....|.
gi 446333413 348 -------IEGR 351
Cdd:PRK02427 369 etedgliITGG 379
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
1-344 5.16e-07

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 51.67  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413   1 MEKIIVRGGKRLNGTVRVEGAK---NAVLpiIAAALlaSDGKNVLSEVPVLSDVYTINEVLRHLNAEVV--FENNQVTID 75
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKslsNRIL--LLAAL--SEGTTVVDNLLDSDDIRYMLGALKTLGLNVEedSENNRAVVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  76 ASKelnieAPFEYVRKMRASVQV--------MGPLLA----RNGRARIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGNG 143
Cdd:PLN02338  77 GCG-----GKFPVSGDSKEDVELflgnagtaMRPLTAavtaAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 144 F----VEAYVEGELKGAKIYLD--FPSVGATENIMsAATLAKGT---TILENAAKEPEIVDLANFLNAMGAKV-RGAGTG 213
Cdd:PLN02338 152 TncppVRVNAAGGLPGGKVKLSgsISSQYLTALLM-AAPLALGDveiEIVDKLISVPYVEMTLKLMERFGVSVeHSDSWD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 214 TIRIEGVDKLYG-GNHSIIPDRIEAGTFMVAAAITGGDILIENAVPEHLRSITA---KMEEMGVKIIEENEGVRVIGPD- 288
Cdd:PLN02338 231 RFFIKGGQKYKSpGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKfaeVLEKMGAKVEWTENSVTVTGPPr 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446333413 289 ------KLKAVDI--KTMPhpgfptDMQSQMMALLLQADGTSMITEtVFENRfmhVEEFRRMNA 344
Cdd:PLN02338 311 dafggkHLKAIDVnmNKMP------DVAMTLAVVALFADGPTAIRD-VASWR---VKETERMIA 364
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
171-366 2.00e-06

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 49.76  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 171 IMSAAtLAKGTTILENAAKEPEIVDLANFLNAMGAKVRgagTGTIRIEGVdklyGGNHSIIPDRI----EAGT----FMV 242
Cdd:PRK02427  30 LLLAA-LAEGETTITNLLRSEDTLATLNALRALGVEIE---DDEVVVEGV----GGGGLKEPEDVldcgNSGTtmrlLTG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 243 AAAITGGDILIENavPEHLRS-----ITAKMEEMGVKIIEENEG---VRVIGPDKLKAVDIKtmphpgfpTDMQSQ---- 310
Cdd:PRK02427 102 LLALQPGEVVLTG--DESLRKrpmgrLLDPLRQMGAKIEGRDEGylpLTIRGGKKGGPIEYD--------GPVSSQfvks 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446333413 311 -MMALLLQADG--TSMITETV-----FEnrfMHVEEFRRMNADIKIEG----RSVIMNGPNSLQGAEV 366
Cdd:PRK02427 172 lLLLAPLFAEGdtETTVIEPLpsrphTE---ITLRMLRAFGVEVENVEgwgyRRIVIKGGQRLRGQDI 236
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
132-269 2.26e-06

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 49.76  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 132 EAMGAKVQVGNGFVEAYVEG-------ELKGakIYLDFPSVG-ATENIMSAATLAKGTTILENAA----KEPE-IVDLAN 198
Cdd:PRK02427 281 EKMGADIEIENEREGGEPVGdirvrssELKG--IDIDIPDIIdEAPTLAVLAAFAEGTTVIRNAEelrvKETDrIAAMAT 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 199 FLNAMGAKVRgAGTGTIRIEGVDKLYG----GNHsiipdRIeAGTFMVAAAITGGDILIENA--V-------PEHLRSIT 265
Cdd:PRK02427 359 ELRKLGAEVE-ETEDGLIITGGPLAGVvdsyGDH-----RI-AMAFAIAGLAAEGPVTIDDPecVaksfpdfFEDLASLG 431

                 ....
gi 446333413 266 AKME 269
Cdd:PRK02427 432 ANIE 435
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
88-295 4.47e-04

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 42.67  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413  88 YVRKMRASVQVMGPLLArnGRA-RIALPGGCAIGSRPIDQHLKGFEAMGAKVQVGN-GFVEAYVEGELKGAKIYLDFPSv 165
Cdd:PRK14806 390 YMGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIETGEeGRPPLSIRGGQRLKGIHYDLPM- 466
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446333413 166 gATENIMSAATLA----KGTTilenAAKEPEIV--DLANFLNAMGAKVRGAGTgTIRIEGVDKLYGGNHSIIPDRIEAGT 239
Cdd:PRK14806 467 -ASAQVKSCLLLAglyaEGET----SVTEPAPTrdHTERMLRGFGYPVKVEGN-TISVEGGGKLTATDIEVPADISSAAF 540
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446333413 240 FMVAAAITGG-DILIEN--------AVPEHLRSitakmeeMGVKIIEENEGVR--------VIGPDKLKAVDI 295
Cdd:PRK14806 541 FLVAASIAEGsELTLEHvginptrtGVIDILKL-------MGADITLENEREVggepvadiRVRGARLKGIDI 606
 
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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