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Conserved domains on  [gi|1981674434|emb|CAD7837631|]
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UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) [Olavius algarvensis Delta 4 endosymbiont]

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
1-415 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


:

Pssm-ID: 236486  Cd Length: 417  Bit Score: 728.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRR-AGRVCIDAGGLD 79
Cdd:PRK09369    1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  80 SHEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEART-KQLRGAEIYF 158
Cdd:PRK09369   81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAdGRLKGAHIVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 159 DVATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTF 238
Cdd:PRK09369  161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 239 MVAAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKG 318
Cdd:PRK09369  241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 319 QSLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGY 398
Cdd:PRK09369  321 TSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGY 400
                         410
                  ....*....|....*..
gi 1981674434 399 EALEEKFFKLGAAIKRV 415
Cdd:PRK09369  401 ERIEEKLRALGADIERV 417
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-415 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 728.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRR-AGRVCIDAGGLD 79
Cdd:PRK09369    1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  80 SHEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEART-KQLRGAEIYF 158
Cdd:PRK09369   81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAdGRLKGAHIVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 159 DVATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTF 238
Cdd:PRK09369  161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 239 MVAAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKG 318
Cdd:PRK09369  241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 319 QSLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGY 398
Cdd:PRK09369  321 TSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGY 400
                         410
                  ....*....|....*..
gi 1981674434 399 EALEEKFFKLGAAIKRV 415
Cdd:PRK09369  401 ERIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-415 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: 725.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVC-IDAGGLD 79
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLtIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  80 SHEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEARTKQLRGAEIYFD 159
Cdd:COG0766    81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 160 VATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFM 239
Cdd:COG0766   161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 240 VAAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKGQ 319
Cdd:COG0766   241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 320 SLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGYE 399
Cdd:COG0766   321 SVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYE 400
                         410
                  ....*....|....*.
gi 1981674434 400 ALEEKFFKLGAAIKRV 415
Cdd:COG0766   401 NLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-408 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: 640.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  12 LQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGR-VCIDAGGLDSHEAPYDLVRK 90
Cdd:cd01555     1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENtLVIDASNINSTEAPYELVRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  91 MRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEART-KQLRGAEIYFDVATVGGTENL 169
Cdd:cd01555    81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAaGRLKGARIYLDFPSVGATENI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 170 MMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFMVAAALAGGDI 249
Cdd:cd01555   161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 250 RVENCEPEHLGASINKLRLTGAEVNVGSQSIQV-CSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKGQSLISETIFE 328
Cdd:cd01555   241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVdGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 329 NRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGYEALEEKFFKL 408
Cdd:cd01555   321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-414 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: 602.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVCIDAGGLDS 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  81 HEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEARTKQ-LRGAEIYFD 159
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGrLVGAHIVLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 160 VATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFM 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 240 VAAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQV-CSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKG 318
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVdMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 319 QSLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGY 398
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
                         410
                  ....*....|....*.
gi 1981674434 399 EALEEKFFKLGAAIKR 414
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-405 1.82e-124

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 366.62  E-value: 1.82e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   7 EGGRPLQGSITVSGSK-NAALPILVSSLLTdGMSEYENVPQLRDIQSTIDLLMHLGARVSR--RAGRVCIDAGGLDSHEA 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKsNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKldDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  84 PYDLVRKMRASILVLGPLLARLKRAR--VSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEA----RTKQLRGAEIY 157
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 158 FDVATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSS-VITINGVETLKPAGATIIPDRIEAG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 237 TFMVAAALAGGDIRVENCEPEHL---GASINKLRLTGAEVNVGSQSIQVCSQGRLNG--VDIKTQPFPGFPTDMQAQFMV 311
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLRGkaVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 312 LMTIAKGQSLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTK-LSGAPVMAT-DLRASASLVLAGLVAEGTTEIS 389
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 1981674434 390 RIYHLDRGYEALEEKF 405
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-415 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 728.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRR-AGRVCIDAGGLD 79
Cdd:PRK09369    1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  80 SHEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEART-KQLRGAEIYF 158
Cdd:PRK09369   81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAdGRLKGAHIVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 159 DVATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTF 238
Cdd:PRK09369  161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 239 MVAAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKG 318
Cdd:PRK09369  241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 319 QSLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGY 398
Cdd:PRK09369  321 TSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGY 400
                         410
                  ....*....|....*..
gi 1981674434 399 EALEEKFFKLGAAIKRV 415
Cdd:PRK09369  401 ERIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-415 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: 725.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVC-IDAGGLD 79
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLtIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  80 SHEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEARTKQLRGAEIYFD 159
Cdd:COG0766    81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 160 VATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFM 239
Cdd:COG0766   161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 240 VAAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKGQ 319
Cdd:COG0766   241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 320 SLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGYE 399
Cdd:COG0766   321 SVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYE 400
                         410
                  ....*....|....*.
gi 1981674434 400 ALEEKFFKLGAAIKRV 415
Cdd:COG0766   401 NLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-408 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: 640.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  12 LQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGR-VCIDAGGLDSHEAPYDLVRK 90
Cdd:cd01555     1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENtLVIDASNINSTEAPYELVRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  91 MRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEART-KQLRGAEIYFDVATVGGTENL 169
Cdd:cd01555    81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAaGRLKGARIYLDFPSVGATENI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 170 MMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFMVAAALAGGDI 249
Cdd:cd01555   161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 250 RVENCEPEHLGASINKLRLTGAEVNVGSQSIQV-CSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKGQSLISETIFE 328
Cdd:cd01555   241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVdGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 329 NRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGYEALEEKFFKL 408
Cdd:cd01555   321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-414 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: 602.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVCIDAGGLDS 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  81 HEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEARTKQ-LRGAEIYFD 159
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGrLVGAHIVLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 160 VATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFM 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 240 VAAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQV-CSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKG 318
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVdMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 319 QSLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGY 398
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
                         410
                  ....*....|....*.
gi 1981674434 399 EALEEKFFKLGAAIKR 414
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 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: 524.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVCIDAGGLDS 80
Cdd:PRK12830    1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  81 HEAPYDLVRKMRASILVLGPLLARLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEARTKQLRGAEIYFDV 160
Cdd:PRK12830   81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGAHIYLDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 161 ATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFMV 240
Cdd:PRK12830  161 VSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYMI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 241 AAALAGGDIRVENCEPEHLGASINKLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTQPFPGFPTDMQAQFMVLMTIAKGQS 320
Cdd:PRK12830  241 LAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGRS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 321 LISETIFENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMATDLRASASLVLAGLVAEGTTEISRIYHLDRGYEA 400
Cdd:PRK12830  321 VVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYSN 400
                         410
                  ....*....|....*..
gi 1981674434 401 LEEKFFKLGAAIKRVKE 417
Cdd:PRK12830  401 IIEKLKALGADIWREED 417
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-405 1.82e-124

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 366.62  E-value: 1.82e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   7 EGGRPLQGSITVSGSK-NAALPILVSSLLTdGMSEYENVPQLRDIQSTIDLLMHLGARVSR--RAGRVCIDAGGLDSHEA 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKsNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKldDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  84 PYDLVRKMRASILVLGPLLARLKRAR--VSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEA----RTKQLRGAEIY 157
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 158 FDVATVGGTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSS-VITINGVETLKPAGATIIPDRIEAG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 237 TFMVAAALAGGDIRVENCEPEHL---GASINKLRLTGAEVNVGSQSIQVCSQGRLNG--VDIKTQPFPGFPTDMQAQFMV 311
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLRGkaVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 312 LMTIAKGQSLISETIFENRFIHVSELKRMGADITINGNAAMVRGVTK-LSGAPVMAT-DLRASASLVLAGLVAEGTTEIS 389
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 1981674434 390 RIYHLDRGYEALEEKF 405
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-408 3.26e-103

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: 311.85  E-value: 3.26e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  12 LQGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVCIDAGGLDSHEAP---YDLV 88
Cdd:cd01554     1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPqnaLNLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  89 RKMRASILVLGPLLARlkRARVSLPGGCAIGARPINLHLKGMERLGATIELKHGYVEARTK---QLRGAEIYFD-VATVG 164
Cdd:cd01554    81 NSGTAIRLISGVLAGA--DFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLkggKNLGPIHYEDpIASAQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 165 GTENLMMAACLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGTFMVAAAL 244
Cdd:cd01554   159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 245 AGGDIRVENCEP-EHLGASINKLRLTGAEVNVGSQSIqVCSQGRLNGVDIKTQPFPgFPTDMQAQFMVLMTIAKGQSLIS 323
Cdd:cd01554   239 APGRLVLQNVGInETRTGIIDVLRAMGAKIEIGEDTI-SVESSDLKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 324 ETIF------ENRFIHVSELKRMGADITINGNAAMVRGVTKLSGAPVMAT-DLRASASLVLAGLVAEGTTEISRIYHLDR 396
Cdd:cd01554   317 DAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAINT 396
                         410
                  ....*....|..
gi 1981674434 397 GYEALEEKFFKL 408
Cdd:cd01554   397 SYPSFFDDLESL 408
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-389 4.78e-32

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: 125.59  E-value: 4.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSK---NAALpILvsSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVCI---D 74
Cdd:COG0128     1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL-LL--AALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRvtgV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  75 AGGLDSHEAPYDL-----VrkMRasilVLGPLLArLKRARVSLPGGCAIGARPINLHLKGMERLGATIE-LKHGY--VEA 146
Cdd:COG0128    78 GGGLKEPDAVLDCgnsgtT--MR----LLTGLLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIEsRGGGYlpLTI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 147 RTKQLRGAEIyfdvaTVGGTEN------LMMAACLAE-GQTILRNAAREP----EITAlaEILNAMGADVQGAGSSVITI 215
Cdd:COG0128   151 RGGPLKGGEY-----EIPGSASsqfksaLLLAGPLAEgGLEITVTGELESkpyrDHTE--RMLRAFGVEVEVEGYRRFTV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 216 NGVETLKPAGATIIPDRIEAGTFMVAAALAGGDIRVENCEPEHLGAS---INKLRLTGAEVNVGSQSIQVCSqGRLNGVD 292
Cdd:COG0128   224 PGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDtgiLDILKEMGADIEIENDGITVRG-SPLKGID 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 293 IKTQPFPG-FPTdmqaqFMVLMTIAKGQSLIS--------ETifeNRfIH--VSELKRMGADITINGNAAMVRGVTKLSG 361
Cdd:COG0128   303 IDLSDIPDeAPT-----LAVLAAFAEGTTRIRgaaelrvkES---DR-IAamATELRKLGADVEETEDGLIIEGGPKLKG 373
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1981674434 362 APV-------MATdlrasaSLVLAGLVAEGTTEIS 389
Cdd:COG0128   374 AEVdsygdhrIAM------AFAVAGLRAEGPVTID 402
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-393 4.46e-29

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: 117.27  E-value: 4.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  12 LQGSITVSGSK---NAALpILvsSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVCIDAGGLDSHEAPYDLV 88
Cdd:cd01556     1 LSGEITVPGSKsisHRAL-LL--AALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGLPPEAVLD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  89 RK-----MRASIlvlgPLLArLKRARVSLPGGCAIGARPINLHLKGMERLGATIELKHG---YVEARTKQLRGAEIYFDV 160
Cdd:cd01556    78 CGnsgttMRLLT----GLLA-LQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGggyPPLIGGGGLKGGEVEIPG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 161 AT----VGGtenLMMAACLAEGQTILRNAAREP----EITalAEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDR 232
Cdd:cd01556   153 AVssqfKSA---LLLAAPLAEGPTTIIIGELESkpyiDHT--ERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 233 IEAGTFMVAAALAGGDIRVENCEPEHLGASI-NKLRLTGAEVNVGSQSIQVC-SQGRLNGVDIKTQPFPG-FPTdmqaqF 309
Cdd:cd01556   228 SSAAFFLAAAAITGSEIVIKNVGLNSGDTGIiDVLKEMGADIEIGNEDTVVVeSGGKLKGIDIDGNDIPDeAPT-----L 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 310 MVLMTIAKGQSLIS--------ETifeNRfIH--VSELKRMGADITINGNAAMVRGVTKLSGAPVMAT--DLRASASLVL 377
Cdd:cd01556   303 AVLAAFAEGPTRIRnaaelrvkES---DR-IAamATELRKLGADVEETEDGLIIEGGPLKGAGVEVYTygDHRIAMSFAI 378
                         410
                  ....*....|....*.
gi 1981674434 378 AGLVAEGTTEISRIYH 393
Cdd:cd01556   379 AGLVAEGGVTIEDPEC 394
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-388 8.58e-25

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: 105.05  E-value: 8.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  14 GSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRAGRVCIDAGGLDSHEAPYDlvrkMRA 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGKEPQAELD----LGN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  94 SILVLGPLLARLKRAR--VSLPGGCAIGARPINLHLKGMERLGATIE--LKHGYVEARTK-QLRGAEIYFD------VAT 162
Cdd:TIGR01356  77 SGTTARLLTGVLALADgeVVLTGDESLRKRPMGRLVDALRQLGAEISslEGGGSLPLTISgPLPGGIVYISgsassqYKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 163 VggtenLMMAACLAEGQTILRNAAREP-----EITAlaEILNAMGADVQGAGSSVITINGVETLKPAGATIIPDRIEAGT 237
Cdd:TIGR01356 157 A-----LLLAAPALQAVGITIVGEPLKsrpyiEITL--DLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAF 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 238 FMVAAALAGGDIRVENCEPEHL---GASINKLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTQPFPG-FPTdmqaqFMVLM 313
Cdd:TIGR01356 230 FLAAAAITGGRVTLENLGINPTqgdKAIIIVLEEMGADIEVEEDDLIVEGASGLKGIKIDMDDMIDeLPT-----LAVLA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 314 TIAKGQSLIS--------ETifeNRfIH--VSELKRMGADITINGNAAMVRGVTKLSGAPVMA-TDLRASASLVLAGLVA 382
Cdd:TIGR01356 305 AFAEGVTRITgaeelrvkES---DR-IAaiAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTfGDHRIAMAFAVAGLVA 380

                  ....*.
gi 1981674434 383 EGTTEI 388
Cdd:TIGR01356 381 EGEVLI 386
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
230-404 3.64e-20

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: 88.11  E-value: 3.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 230 PDRIEAGTFMVAAALAGGDIRVENCEP--------EHLGASINKLR-LTGAEVNVGSQSIQ--VCSQGRLNGVDIKTQPF 298
Cdd:cd01553     8 GGGQILRSFLVLAAISGGPITVTGIRPdrakpgllRQHLTFLKALEkICGATVEGGELGSDriSFRPGTVRGGDVRFAIG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 299 P-GFPTDMQAQFMVLMTIAKGQSLISETIF----------ENRFIHVSELKRMGADITINGNAAMVRGV------TKLSG 361
Cdd:cd01553    88 SaGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETLLRHGFYPAgggvvaTEVSP 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1981674434 362 APVMAT-DLRASASLVLAGlvaeGTTEISRIYHLDRGYEALEEK 404
Cdd:cd01553   168 VEKLNTaQLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAV 207
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-391 5.56e-19

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 88.28  E-value: 5.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434   1 MDKIIIEGGRPLQGSITVSGSK---NAALpILvsSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRraGRVCIDAGG 77
Cdd:PRK02427    2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL-LL--AALAEGETTITNLLRSEDTLATLNALRALGVEIED--DEVVVEGVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  78 LDSHEAPYDLV------RKMRasiLVLGpLLArLKRARVSLPGGCAIGARPINLHLKGMERLGATIELK---------HG 142
Cdd:PRK02427   77 GGGLKEPEDVLdcgnsgTTMR---LLTG-LLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRdegylpltiRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 143 yvearTKQLRGAEIYFDVAT--VGGtenLMMAACL-AEGQTILRNAAREP-----EITalAEILNAMGADVQ---GAGSS 211
Cdd:PRK02427  152 -----GKKGGPIEYDGPVSSqfVKS---LLLLAPLfAEGDTETTVIEPLPsrphtEIT--LRMLRAFGVEVEnveGWGYR 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 212 VITINGVETLKPAGATIIPDRIEAGTFMVAAALAGG-DIRVENCEPEHL--GASI-NKLRLTGAEVNVGSQSIQ------ 281
Cdd:PRK02427  222 RIVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTqgGKAIiDVLEKMGADIEIENEREGgepvgd 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 282 -VCSQGRLNGVDIktqPFPGFPtDmqaQFM---VLMTIAKGQSLIS--------ETifeNRfIH--VSELKRMGADITIN 347
Cdd:PRK02427  302 iRVRSSELKGIDI---DIPDII-D---EAPtlaVLAAFAEGTTVIRnaeelrvkET---DR-IAamATELRKLGAEVEET 370
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1981674434 348 GNAAMVRGVTKlsgAPVMAT--DLRASASLVLAGLVAEGTTEISRI 391
Cdd:PRK02427  371 EDGLIITGGPL---AGVVDSygDHRIAMAFAIAGLAAEGPVTIDDP 413
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
169-413 1.67e-09

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: 59.33  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 169 LMMAAcLAEGQTILRNAAREPEITALAEILNAMGADVQGAGSSVITINGV-ETLKPAGATIipDRIEAGT----FMVAAA 243
Cdd:COG0128    29 LLLAA-LAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGVgGGLKEPDAVL--DCGNSGTtmrlLTGLLA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 244 LAGGDI-------------------------RVENCEPEHLGASINKLRLTGAEVNV-GSQSIQVCS------------- 284
Cdd:COG0128   106 LQPGEVvltgdeslrkrpmgrlldplrqlgaRIESRGGGYLPLTIRGGPLKGGEYEIpGSASSQFKSalllagplaeggl 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 285 ----QGRLN---------------GVDIKTQPFPGF---------PTDMQ--------AQFMVLMTIAKGQSLI-----S 323
Cdd:COG0128   186 eitvTGELEskpyrdhtermlrafGVEVEVEGYRRFtvpggqryrPGDYTvpgdissaAFFLAAAAITGSEVTVegvglN 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 324 ETIFENRFIHVseLKRMGADITINGNAAMVRGvTKLSG-----------APVMAtdlrasaslVLAgLVAEGTTEISRIY 392
Cdd:COG0128   266 STQGDTGILDI--LKEMGADIEIENDGITVRG-SPLKGididlsdipdeAPTLA---------VLA-AFAEGTTRIRGAA 332
                         330       340
                  ....*....|....*....|....*.
gi 1981674434 393 HLdRGYE-----ALEEKFFKLGAAIK 413
Cdd:COG0128   333 EL-RVKEsdriaAMATELRKLGADVE 357
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
130-255 6.18e-08

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 54.38  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 130 MERLGATIELKH--------GYVEARTKQLRGAEIyfDVATVGgtENLMM---AACLAEGQTILRNAA--REPE---ITA 193
Cdd:PRK02427  280 LEKMGADIEIENereggepvGDIRVRSSELKGIDI--DIPDII--DEAPTlavLAAFAEGTTVIRNAEelRVKEtdrIAA 355
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1981674434 194 LAEILNAMGADVQgAGSSVITINGvetlKPAGATIIP--D-RIeAGTFMVAAALAGGDIRVENCE 255
Cdd:PRK02427  356 MATELRKLGAEVE-ETEDGLIITG----GPLAGVVDSygDhRI-AMAFAIAGLAAEGPVTIDDPE 414
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
13-344 5.62e-06

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 48.55  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  13 QGSITVSGSKNAALPILVSSLLTDGMSEYENVPQLRDIQSTIDLLMHLGARVSRRaGRVCIDAGGLDSHEAPY-DL---- 87
Cdd:PRK11861  252 QGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRD-GGTCVVGGTRGAFTAKTaDLflgn 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434  88 ----VRKMRASILVLGpllarlkrARVSLPGGCAIGARPINLHLKGMERLGATIELK--HGYVEARtkqLRGAEIYFD-- 159
Cdd:PRK11861  331 agtaVRPLTAALAVNG--------GEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEgnEGFPPLR---IRPATISVDap 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 160 VATVGGTENLMMAACL--------AEGQTILR---NAAREPEITALAEILNAMGADVQGAGSSVITI-NGVETLKPAGAT 227
Cdd:PRK11861  400 IRVRGDVSSQFLTALLmtlplvkaKDGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVpAGVRYRSPGTIM 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 228 IIPDRIEAGTFMVAAALAGGDIRVENCEPEHLGASI---NKLRLTGAEVNVGSQSIQV----CSQGRLNGVDIKTQPFPg 300
Cdd:PRK11861  480 VEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVgfaNALMQMGANVTMGDDWIEVrgigHDHGRLAPIDMDFNLIP- 558
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1981674434 301 fptDMQAQFMVLMTIAKGQSLI----SETIFENRFI--HVSELKRMGADI 344
Cdd:PRK11861  559 ---DAAMTIAVAALFADGPSTLrnigSWRVKETDRIaaMATELRKVGATV 605
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
169-413 2.22e-04

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 43.21  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 169 LMMAAcLAEGQTILRNAAREPEITALAEILNAMGADVQGaGSSVITINGVETLKPAGATIipDRIEAGTFM--VAAALAG 246
Cdd:PRK02427   30 LLLAA-LAEGETTITNLLRSEDTLATLNALRALGVEIED-DEVVVEGVGGGGLKEPEDVL--DCGNSGTTMrlLTGLLAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 247 GDIRVENCEPEHL---------------GASINK-------LRLTGA--------EVNVGSQsiQVCS---------QGR 287
Cdd:PRK02427  106 QPGEVVLTGDESLrkrpmgrlldplrqmGAKIEGrdegylpLTIRGGkkggpieyDGPVSSQ--FVKSllllaplfaEGD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 288 LN-----------------------GVDIKTQPFPGF-------PTDMQAQ-------------FMVLMTIAKGQSLISE 324
Cdd:PRK02427  184 TEttvieplpsrphteitlrmlrafGVEVENVEGWGYrrivikgGQRLRGQditvpgdpssaafFLAAAAITGGSEVTIT 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 325 TIFEN------RFIHVseLKRMGADITINGNAAMVRGVTKL--SGAPVMATDLRASA------SLVLAGLVAEGTTEISR 390
Cdd:PRK02427  264 NVGLNstqggkAIIDV--LEKMGADIEIENEREGGEPVGDIrvRSSELKGIDIDIPDiideapTLAVLAAFAEGTTVIRN 341
                         330       340
                  ....*....|....*....|....*...
gi 1981674434 391 IYHL-----DRgYEALEEKFFKLGAAIK 413
Cdd:PRK02427  342 AEELrvketDR-IAAMATELRKLGAEVE 368
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
169-255 8.83e-04

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 41.52  E-value: 8.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 169 LMMAACLAEGQTILRNAAR-----EPEITALAEILNAMGADVQGAGSSVITINGVetlkPAGATIIP---DRIeAGTFMV 240
Cdd:PRK14806  621 LFVAAACAEGRTVLTGAEElrvkeSDRIQVMADGLKTLGIDCEPTPDGIIIEGGI----FGGGEVEShgdHRI-AMSFSV 695
                          90
                  ....*....|....*
gi 1981674434 241 AAALAGGDIRVENCE 255
Cdd:PRK14806  696 ASLRASGPITIHDCA 710
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
194-346 8.75e-03

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 38.44  E-value: 8.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 194 LAEILNAMGADVQGA--GSSVITINGVETLK------PAGATiipdRIEAGTFMvAAALAGGDIRVENCEP-----EHLg 260
Cdd:PRK14806  428 VAKPLREMGAVIETGeeGRPPLSIRGGQRLKgihydlPMASA----QVKSCLLL-AGLYAEGETSVTEPAPtrdhtERM- 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981674434 261 asinkLRLTGAEVNVGSQSIQVCSQGRLNGVDIKTqpfpgfPTDMQ--AQFMVLMTIAKGQSLISETIFEN--RFIHVSE 336
Cdd:PRK14806  502 -----LRGFGYPVKVEGNTISVEGGGKLTATDIEV------PADISsaAFFLVAASIAEGSELTLEHVGINptRTGVIDI 570
                         170
                  ....*....|
gi 1981674434 337 LKRMGADITI 346
Cdd:PRK14806  571 LKLMGADITL 580
 
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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