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Conserved domains on  [gi|345100529|pdb|1Q3G|I]
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Chain I, UDP-N-acetylglucosamine 1-carboxyvinyltransferase

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
1-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


:

Pssm-ID: 236486  Cd Length: 417  Bit Score: 780.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER--*GSVWIDASNVN 78
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFdgNGTVTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVM 158
Cdd:PRK09369  81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
                        410
                 ....*....|....*...
1Q3G_I       399 YERIEDKLRALGANIERV 416
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 780.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER--*GSVWIDASNVN 78
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFdgNGTVTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVM 158
Cdd:PRK09369  81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
                        410
                 ....*....|....*...
1Q3G_I       399 YERIEDKLRALGANIERV 416
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-416 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: 742.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*--GSVWIDASNVN 78
Cdd:COG0766   1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdgGTLTIDASNIN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNgRLKGAHIVM 158
Cdd:COG0766  81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAG-RLKGARIYL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:COG0766 319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
                       410
                ....*....|....*...
1Q3G_I      399 YERIEDKLRALGANIERV 416
Cdd:COG0766 399 YENLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-409 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: 700.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G--SVWIDASNVNNFSAPYDLVKT 89
Cdd:cd01555   1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGenTLVIDASNINSTEAPYELVRK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       90 MRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDKVSVGATVTI 169
Cdd:cd01555  81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      170 MSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKI 249
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      250 VCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEGTGVITETIFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      330 NRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRAL 409
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-415 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: 674.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I          1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G-SVWIDASNVNN 79
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNnTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         80 FSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMD 159
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        160 KVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        240 VAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEG 319
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        320 TGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGY 399
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
                         410
                  ....*....|....*.
1Q3G_I        400 ERIEDKLRALGANIER 415
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-406 1.03e-163

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 466.39  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I          7 QGPTRLQGEVTISG-AKNAALPILFAALLAEEpVEIQNVPKLKDIDTTMKLLTQLG---TKVER*GSVWIDASNVNNFSA 82
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGE-STITNLLDSDDTLTMLEALRALGaeiIKLDDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         83 PYDLVKTMRASIWALGPLVARFGQ--GQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASV---NGRLKGAHIV 157
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALqsGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLkvrGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        158 MDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTD-RITIEGVERLGGGVYRVLPDRIETG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        237 TFLVAAAISGGKIVCRNAQPDTL---DAVLAKLREAGADIETGED-WISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTL 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        313 LNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEK-LSGAQVMAT-DLRASASLVLAGCIAEGTTVVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
1Q3G_I        391 RIYHIDRGYERIEDKL 406
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 780.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER--*GSVWIDASNVN 78
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFdgNGTVTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVM 158
Cdd:PRK09369  81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
                        410
                 ....*....|....*...
1Q3G_I       399 YERIEDKLRALGANIERV 416
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-416 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: 742.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*--GSVWIDASNVN 78
Cdd:COG0766   1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdgGTLTIDASNIN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNgRLKGAHIVM 158
Cdd:COG0766  81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAG-RLKGARIYL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:COG0766 319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
                       410
                ....*....|....*...
1Q3G_I      399 YERIEDKLRALGANIERV 416
Cdd:COG0766 399 YENLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-409 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: 700.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G--SVWIDASNVNNFSAPYDLVKT 89
Cdd:cd01555   1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGenTLVIDASNINSTEAPYELVRK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       90 MRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDKVSVGATVTI 169
Cdd:cd01555  81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      170 MSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKI 249
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      250 VCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEGTGVITETIFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      330 NRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRAL 409
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-415 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: 674.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I          1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G-SVWIDASNVNN 79
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNnTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         80 FSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMD 159
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        160 KVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        240 VAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEG 319
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        320 TGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGY 399
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
                         410
                  ....*....|....*.
1Q3G_I        400 ERIEDKLRALGANIER 415
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 416
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-409 3.09e-180

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: 508.30  E-value: 3.09e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER-*GSVWIDASNVNNFSAP---YDLV 87
Cdd:cd01554   1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDkDGVITIQGVGMAGLKAPqnaLNLG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       88 KTMRASIWALGPLVARfgQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKAS--VNGRLKGAHIVMDKV-SVG 164
Cdd:cd01554  81 NSGTAIRLISGVLAGA--DFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPllKGGKNLGPIHYEDPIaSAQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      165 ATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAI 244
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      245 SGGKIVCRNAQPDT-LDAVLAKLREAGADIETGEDWISLDMHgkRPKAVTVRTAPHPaFPTAMQAQFTLLNLVAEGTGVI 323
Cdd:cd01554 239 APGRLVLQNVGINEtRTGIIDVLRAMGAKIEIGEDTISVESS--DLKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      324 TETIF------ENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMAT-DLRASASLVLAGCIAEGTTVVDRIYHID 396
Cdd:cd01554 316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAIN 395
                       410
                ....*....|...
1Q3G_I      397 RGYERIEDKLRAL 409
Cdd:cd01554 396 TSYPSFFDDLESL 408
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-417 3.94e-180

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 508.24  E-value: 3.94e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G-SVWIDASNVNN 79
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGdTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        80 FSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNgRLKGAHIVMD 159
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKAD-ELKGAHIYLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       160 KVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       240 VAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDwiSLDMHGKRP-KAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNED--SIFVEKQGNlKAVDIKTLPYPGFATDLQQPLTPLLLKAN 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK12830 318 GRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
                        410
                 ....*....|....*....
1Q3G_I       399 YERIEDKLRALGANIERVK 417
Cdd:PRK12830 398 YSNIIEKLKALGADIWREE 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-406 1.03e-163

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 466.39  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I          7 QGPTRLQGEVTISG-AKNAALPILFAALLAEEpVEIQNVPKLKDIDTTMKLLTQLG---TKVER*GSVWIDASNVNNFSA 82
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGE-STITNLLDSDDTLTMLEALRALGaeiIKLDDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         83 PYDLVKTMRASIWALGPLVARFGQ--GQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASV---NGRLKGAHIV 157
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALqsGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLkvrGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        158 MDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTD-RITIEGVERLGGGVYRVLPDRIETG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        237 TFLVAAAISGGKIVCRNAQPDTL---DAVLAKLREAGADIETGED-WISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTL 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        313 LNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEK-LSGAQVMAT-DLRASASLVLAGCIAEGTTVVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
1Q3G_I        391 RIYHIDRGYERIEDKL 406
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
230-409 4.78e-49

This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.


Pssm-ID: 238794  Cd Length: 211  Bit Score: 165.92  E-value: 4.78e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      230 PDRIETGTFLVAAAISGGKIVCRNAQPDT--------LDAVLAKLREA-GADIETGE---DWISLDMHGkrPKAVTVRTA 297
Cdd:cd01553   8 GGGQILRSFLVLAAISGGPITVTGIRPDRakpgllrqHLTFLKALEKIcGATVEGGElgsDRISFRPGT--VRGGDVRFA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      298 PHPA-FPTAMQAQFTLLNLVAEGTGVITETIF----------ENRFMHVPELIRMGAHAEIESN------------TVIC 354
Cdd:cd01553  86 IGSAgSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEV 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
1Q3G_I      355 HGVEKLSGAQVmatdlRASASLVLAGciaeGTTVVDRIYHIDRGYERIEDKLRAL 409
Cdd:cd01553 166 SPVEKLNTAQL-----RQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-396 1.14e-33

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: 130.21  E-value: 1.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        1 MDKFRVQGPTRLQGEVTISGAK---NAALpilFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*-GSVWIDASN 76
Cdd:COG0128   1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL---LLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       77 VNNFSAPYDLVK------TMR--ASIWALGPLVARF-GQGQvslpggcaIGARPVDlHIFG-LEKLGAEIK-LEEGYVKA 145
Cdd:COG0128  78 GGGLKEPDAVLDcgnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMG-RLLDpLRQLGARIEsRGGGYLPL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      146 SVNG-RLKGAHIVMDkVSVGATVT---IMSAATLAEGTTIIENAAREPEI-VD-TANFLVALGAKISGQGTDRITIEGVE 219
Cdd:COG0128 149 TIRGgPLKGGEYEIP-GSASSQFKsalLLAGPLAEGGLEITVTGELESKPyRDhTERMLRAFGVEVEVEGYRRFTVPGGQ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      220 RLGGGVYRVLPDRIETGTFLVAAAISGGKIVCRNAQPDTL---DAVLAKLREAGADIETGEDWISLdmHGKRPKAVTV-- 294
Cdd:COG0128 228 RYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITV--RGSPLKGIDIdl 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      295 RTAPHpAFPTamqaqFTLLNLVAEGTGVIT--------ETifeNRF--MhVPELIRMGAHAEIESNTVICHGVEKLSGAQ 364
Cdd:COG0128 306 SDIPD-EAPT-----LAVLAAFAEGTTRIRgaaelrvkES---DRIaaM-ATELRKLGADVEETEDGLIIEGGPKLKGAE 375
                       410       420       430
                ....*....|....*....|....*....|....*....
1Q3G_I      365 V-------MATdlrasaSLVLAGCIAEGTTVVDRIYHID 396
Cdd:COG0128 376 VdsygdhrIAM------AFAVAGLRAEGPVTIDDAECVA 408
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-396 7.52e-31

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: 122.28  E-value: 7.52e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIDASNVNNFSAPYDLVK--- 88
Cdd:cd01556   1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGLPPEAVLDcgn 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       89 ---TMRASIwalgPLVArFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKL--EEGYVKASVNGRLKGAHIVMDkVSV 163
Cdd:cd01556  81 sgtTMRLLT----GLLA-LQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGreGGGYPPLIGGGGLKGGEVEIP-GAV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      164 GATVT--IMSAATLAEGTTIIENAAREPEI-VD-TANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:cd01556 155 SSQFKsaLLLAAPLAEGPTTIIIGELESKPyIDhTERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDASSAAFFL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      240 VAAAISGGKIVCRNAQPDTLDAVLAK-LREAGADIETGEDWIsLDMHGKRP-KAVTVRTAPHP-AFPTAmqaqfTLLNLV 316
Cdd:cd01556 235 AAAAITGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIGNEDT-VVVESGGKlKGIDIDGNDIPdEAPTL-----AVLAAF 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      317 AEGTGVIT--------ETifeNRF--MHVpELIRMGAHAEIESNTVICHGVEKLSGAQVMAT--DLRASASLVLAGCIAE 384
Cdd:cd01556 309 AEGPTRIRnaaelrvkES---DRIaaMAT-ELRKLGADVEETEDGLIIEGGPLKGAGVEVYTygDHRIAMSFAIAGLVAE 384
                       410
                ....*....|..
1Q3G_I      385 GTTVVDRIYHID 396
Cdd:cd01556 385 GGVTIEDPECVA 396
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-412 5.80e-30

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: 119.69  E-value: 5.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         14 GEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIdaSNVNNFSAPYDLVKtMRAS 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAV--IEGVGGKEPQAELD-LGNS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         94 IWALGPL--VARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEI--KLEEGYVKASVNGRLKGAHIVMDKV--SVGATV 167
Cdd:TIGR01356  78 GTTARLLtgVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEIssLEGGGSLPLTISGPLPGGIVYISGSasSQYKSA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        168 TIMSAATLAEG--TTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAIS 245
Cdd:TIGR01356 158 LLLAAPALQAVgiTIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAAIT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        246 GGKIVCRNAQPDTL---DAVLAKLREAGADIETGEDWISLDMHGKRpKAVTVRTAPHP-AFPTAmqaqfTLLNLVAEGTG 321
Cdd:TIGR01356 238 GGRVTLENLGINPTqgdKAIIIVLEEMGADIEVEEDDLIVEGASGL-KGIKIDMDDMIdELPTL-----AVLAAFAEGVT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        322 VIT--------ETifeNRF--MHVpELIRMGAHAEIESNTVICHGVEKLSGAqVMAT--DLRASASLVLAGCIAEGTTVV 389
Cdd:TIGR01356 312 RITgaeelrvkES---DRIaaIAE-ELRKLGVDVEEFEDGLYIRGKKELKGA-VVDTfgDHRIAMAFAVAGLVAEGEVLI 386
                         410       420
                  ....*....|....*....|...
1Q3G_I        390 DRIYHIDRGYERIEDKLRALGAN 412
Cdd:TIGR01356 387 DDPECVAKSFPSFFDVLERLGAN 409
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-414 7.48e-24

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 102.91  E-value: 7.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         1 MDKFRVQGPTRLQGEVTISGAK---NAALpiLFAALlAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIDASNV 77
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL--LLAAL-AEGETTITNLLRSEDTLATLNALRALGVEIED-DEVVVEGVGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        78 NNFSAPYDLVK------TMR--ASIWALGPLVARFgQGQVSLpggcaiGARPVDlHIF-GLEKLGAEIKL-EEGYVKASV 147
Cdd:PRK02427  78 GGLKEPEDVLDcgnsgtTMRllTGLLALQPGEVVL-TGDESL------RKRPMG-RLLdPLRQMGAKIEGrDEGYLPLTI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       148 NGRLKGAHIVMD-KVSvGATVT--IMSAATLAEG---TTIIENAAREPEIVDTANFLVALGAKISGQGTD---RITIEGV 218
Cdd:PRK02427 150 RGGKKGGPIEYDgPVS-SQFVKslLLLAPLFAEGdteTTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWgyrRIVIKGG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       219 ERLGGGVYRVLPDRIETGTFLVAAAISGG-KIVCRN-----AQPDtlDAVLAKLREAGADIETGEDWISL----DMHGKR 288
Cdd:PRK02427 229 QRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNvglnsTQGG--KAIIDVLEKMGADIEIENEREGGepvgDIRVRS 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       289 P--KAVTVrTAPH-P-AFPTAmqaqfTLLNLVAEGTGVIT--------ETifeNRF--MHVpELIRMGAHAEIESNTVIC 354
Cdd:PRK02427 307 SelKGIDI-DIPDiIdEAPTL-----AVLAAFAEGTTVIRnaeelrvkET---DRIaaMAT-ELRKLGAEVEETEDGLII 376
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1Q3G_I       355 HGVEKlsGAQV-------MATdlrasaSLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIE 414
Cdd:PRK02427 377 TGGPL--AGVVdsygdhrIAM------AFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANIE 435
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
8-323 3.07e-09

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 58.95  E-value: 3.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         8 GP-TRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIDASNVNNFSAPYDL 86
Cdd:PRK11861 246 GPfSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAFTAKTAD 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        87 VKTMRASIwALGPLVARFG--QGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLE--EGYVKAsvngRLKGAHIVMD--- 159
Cdd:PRK11861 326 LFLGNAGT-AVRPLTAALAvnGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEgnEGFPPL----RIRPATISVDapi 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       160 KVSVGATVTIMSAATLA-------EGTTIIE---NAAREPEIVDTANFLVALGAKISGQGTDRITI-EGVERLGGGVYRV 228
Cdd:PRK11861 401 RVRGDVSSQFLTALLMTlplvkakDGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVpAGVRYRSPGTIMV 480
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       229 LPDRIETGTFLVAAAISGGKIVCRNAQPDTLDAVLA---KLREAGADIETGEDWISL----DMHGK-RPKAVTVRTAPHP 300
Cdd:PRK11861 481 EGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGfanALMQMGANVTMGDDWIEVrgigHDHGRlAPIDMDFNLIPDA 560
                        330       340
                 ....*....|....*....|...
1Q3G_I       301 AFPTAMQAQFtllnlvAEGTGVI 323
Cdd:PRK11861 561 AMTIAVAALF------ADGPSTL 577
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
172-415 4.03e-07

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: 52.01  E-value: 4.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      172 AATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVerlgGGVYRVLPDRIE-----TGTFLVAAAISG 246
Cdd:COG0128  31 LAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGV----GGGLKEPDAVLDcgnsgTTMRLLTGLLAL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      247 GKIVCR-------NAQPdtLDAVLAKLREAGADIE-TGEDWISLDMHGKRPKAVTVRTaphpafPTAMQAQFT----LLN 314
Cdd:COG0128 107 QPGEVVltgdeslRKRP--MGRLLDPLRQLGARIEsRGGGYLPLTIRGGPLKGGEYEI------PGSASSQFKsallLAG 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I      315 LVAEGTGVITetifenrfmHVPEL---------IRM----GAHAEIE-SNTVICHGVEKLSGAQVM-ATDLRASASLVLA 379
Cdd:COG0128 179 PLAEGGLEIT---------VTGELeskpyrdhtERMlrafGVEVEVEgYRRFTVPGGQRYRPGDYTvPGDISSAAFFLAA 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
1Q3G_I      380 GCIAEGTTVVDRI----YHIDRGyerIEDKLRALGANIER 415
Cdd:COG0128 250 AAITGSEVTVEGVglnsTQGDTG---ILDILKEMGADIEI 286
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
1-390 4.22e-06

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 48.59  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVE--R*GSVWIDASNVN 78
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEedSENNRAVVEGCGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        79 NFSAPYDLVKTMRASI----WALGPL----VARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGY----VKAS 146
Cdd:PLN02338  81 KFPVSGDSKEDVELFLgnagTAMRPLtaavTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTncppVRVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       147 VNGRLKGAHIVMD-KVSVGATVTIMSAATLAEGT---TIIENAAREPEIVDTANFLVALGAKISGQGT-DRITIEGVERL 221
Cdd:PLN02338 161 AAGGLPGGKVKLSgSISSQYLTALLMAAPLALGDveiEIVDKLISVPYVEMTLKLMERFGVSVEHSDSwDRFFIKGGQKY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       222 G--GGVYrVLPDRIETGTFLVAAAISGGKIVCRNAQPDTL--DAVLAKLREA-GADIETGEDWISL------DMHGKRPK 290
Cdd:PLN02338 241 KspGNAY-VEGDASSASYFLAGAAITGGTVTVEGCGTTSLqgDVKFAEVLEKmGAKVEWTENSVTVtgpprdAFGGKHLK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       291 AVTVRTAPHPafPTAMqaQFTLLNLVAEGTGVI--------TETifENRFMHVPELIRMGAHAEIESNTVICHGVEKLSG 362
Cdd:PLN02338 320 AIDVNMNKMP--DVAM--TLAVVALFADGPTAIrdvaswrvKET--ERMIAICTELRKLGATVEEGPDYCIITPPKKLKP 393
                        410       420
                 ....*....|....*....|....*....
1Q3G_I       363 AQV-MATDLRASASLVLAGCIAEGTTVVD 390
Cdd:PLN02338 394 AEIdTYDDHRMAMAFSLAACGDVPVTIND 422
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
169-415 6.11e-06

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 48.22  E-value: 6.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       169 IMSAAtLAEGTTIIENAAREPEIVDTANFLVALGAKIsgqGTDRITIEGVerlGGGVYRVLPDRIET---GT---FLVA- 241
Cdd:PRK02427  30 LLLAA-LAEGETTITNLLRSEDTLATLNALRALGVEI---EDDEVVVEGV---GGGGLKEPEDVLDCgnsGTtmrLLTGl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       242 AAISGGKIV--------CRnaqPdtLDAVLAKLREAGADIETGED-WISLDMHG-KRPKAVTVRtAPHP-AFPTAMqaqF 310
Cdd:PRK02427 103 LALQPGEVVltgdeslrKR---P--MGRLLDPLRQMGAKIEGRDEgYLPLTIRGgKKGGPIEYD-GPVSsQFVKSL---L 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       311 TLLNLVAEGTGVITetifenrfmHVPEL---------IRM--GAHAEIESNTVICHGVEKLSGAQVM-ATDLR-----AS 373
Cdd:PRK02427 174 LLAPLFAEGDTETT---------VIEPLpsrphteitLRMlrAFGVEVENVEGWGYRRIVIKGGQRLrGQDITvpgdpSS 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
1Q3G_I       374 AS-LVLAGCIAEGTTVvdRIYHID----RGYERIEDKLRALGANIER 415
Cdd:PRK02427 245 AAfFLAAAAITGGSEV--TITNVGlnstQGGKAIIDVLEKMGADIEI 289
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
4-274 6.73e-06

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 48.45  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I         4 FRVQGPTRLQGEVTISGAKNAA-LPILFAALlAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVE--R*GSVWIDASNVNNF 80
Cdd:PRK14806 304 YSVLPGGAVKGTIRVPGDKSIShRSIMLGSL-AEGVTEVEGFLEGEDALATLQAFRDMGVVIEgpHNGRVTIHGVGLHGL 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I        81 SAP----YdlVKTMRASIWALGPLVArfGQG-QVSLPGGCAIGARPVDLHIFGLEKLGAEIKL-EEGYVKASVNG--RLK 152
Cdd:PRK14806 383 KAPpgplY--MGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIETgEEGRPPLSIRGgqRLK 458
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       153 GAHIVMDKVSVGATVTIMSAATLAEGTTIIenaaREPEIV--DTANFLVALGAKISGQGtDRITIEGVERLGGGVYRVLP 230
Cdd:PRK14806 459 GIHYDLPMASAQVKSCLLLAGLYAEGETSV----TEPAPTrdHTERMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPA 533
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
1Q3G_I       231 DRIETGTFLVAAAISGG-KIVCRNAQPD-TLDAVLAKLREAGADIE 274
Cdd:PRK14806 534 DISSAAFFLVAASIAEGsELTLEHVGINpTRTGVIDILKLMGADIT 579
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
169-414 5.29e-03

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 39.21  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       169 IMSAAtLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLG-----GGVYRVlpdriETGT--FLVA 241
Cdd:PRK14806 329 IMLGS-LAEGVTEVEGFLEGEDALATLQAFRDMGVVIEGPHNGRVTIHGVGLHGlkappGPLYMG-----NSGTsmRLLS 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       242 AAISGGKIvcrnaqPDTL--DAVLAK---------LREAGADIETGEDwisldmhGKRPKAVT---VRTAPHPAFPTAmQ 307
Cdd:PRK14806 403 GLLAAQSF------DSVLtgDASLSKrpmervakpLREMGAVIETGEE-------GRPPLSIRggqRLKGIHYDLPMA-S 468
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_I       308 AQFT----LLNLVAEGTGVITETifENRFMHVPELIR-MGAHAEIESNTVICHGVEKLSGAQ-VMATDLRASASLVLAGC 381
Cdd:PRK14806 469 AQVKscllLAGLYAEGETSVTEP--APTRDHTERMLRgFGYPVKVEGNTISVEGGGKLTATDiEVPADISSAAFFLVAAS 546
                        250       260       270
                 ....*....|....*....|....*....|...
1Q3G_I       382 IAEGTTVVDRIYHIDRGYERIEDKLRALGANIE 414
Cdd:PRK14806 547 IAEGSELTLEHVGINPTRTGVIDILKLMGADIT 579
 
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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