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Conserved domains on  [gi|2267612541|ref|WP_253850890|]
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UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Actinosynnema pretiosum]

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
3-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


:

Pssm-ID: 236486  Cd Length: 417  Bit Score: 637.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGD-VATITTPAELN 81
Cdd:PRK09369    2 DKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNINN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  82 HRADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQG-LHGAQVWLD 160
Cdd:PRK09369   82 TEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGrLKGAHIVLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 161 FPSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWA 240
Cdd:PRK09369  162 FPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTFL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 241 FAAAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEGRPESVDFVTLPYPGFATDLQPFAIALSAVSAGT 320
Cdd:PRK09369  242 VAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEGT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 321 SMITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYP 400
Cdd:PRK09369  322 SVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGYE 401
                         410
                  ....*....|....*.
gi 2267612541 401 GFVENLRKLGATVERV 416
Cdd:PRK09369  402 RIEEKLRALGADIERV 417
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
3-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 637.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGD-VATITTPAELN 81
Cdd:PRK09369    2 DKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNINN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  82 HRADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQG-LHGAQVWLD 160
Cdd:PRK09369   82 TEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGrLKGAHIVLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 161 FPSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWA 240
Cdd:PRK09369  162 FPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTFL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 241 FAAAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEGRPESVDFVTLPYPGFATDLQPFAIALSAVSAGT 320
Cdd:PRK09369  242 VAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEGT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 321 SMITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYP 400
Cdd:PRK09369  322 SVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGYE 401
                         410
                  ....*....|....*.
gi 2267612541 401 GFVENLRKLGATVERV 416
Cdd:PRK09369  402 RIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
3-416 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: 612.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVT-IEGDVATITTPAELN 81
Cdd:COG0766     2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVErDDGGTLTIDASNINS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  82 HRADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQGLHGAQVWLDF 161
Cdd:COG0766    82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLDF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 162 PSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAF 241
Cdd:COG0766   162 PSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFLV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 242 AAAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEGRPESVDFVTLPYPGFATDLQPFAIALSAVSAGTS 321
Cdd:COG0766   242 AAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGTS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 322 MITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYPG 401
Cdd:COG0766   322 VITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYEN 401
                         410
                  ....*....|....*
gi 2267612541 402 FVENLRKLGATVERV 416
Cdd:COG0766   402 LEEKLRALGADIERV 416
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
3-415 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: 544.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATITTPAELNH 82
Cdd:TIGR01072   2 DKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  83 RADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQG-LHGAQVWLDF 161
Cdd:TIGR01072  82 EAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGrLVGAHIVLDK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 162 PSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAF 241
Cdd:TIGR01072 162 VSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFLV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 242 AAAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEG-RPESVDFVTLPYPGFATDLQPFAIALSAVSAGT 320
Cdd:TIGR01072 242 AAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQAEGT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 321 SMITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYP 400
Cdd:TIGR01072 322 SVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGYE 401
                         410
                  ....*....|....*
gi 2267612541 401 GFVENLRKLGATVER 415
Cdd:TIGR01072 402 DLEEKLRALGAKIER 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
13-409 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: 539.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  13 LVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEG-DVATITTPAELNHRADSEAMGK 91
Cdd:cd01555     1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  92 LRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAE-AQGLHGAQVWLDFPSVGATENI 170
Cdd:cd01555    81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKaAGRLKGARIYLDFPSVGATENI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 171 LMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAFAAAMTRGDI 250
Cdd:cd01555   161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 251 TVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEG-RPESVDFVTLPYPGFATDLQPFAIALSAVSAGTSMITENLFE 329
Cdd:cd01555   241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 330 ARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYPGFVENLRKL 409
Cdd:cd01555   321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-406 2.79e-110

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 330.41  E-value: 2.79e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   8 QGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVT-IEGDVATITTPAELNH-RAD 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIkLDDEKSVVIVEGLGGSfEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  86 SEAMGKLRASVCVLGPLVGRCKRAV--VALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVA----EAQGLHGAQVWL 159
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHIDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 160 DFPSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTST-LTVHGVPELHPTEHRVIGDRIVGAT 238
Cdd:pfam00275 161 DVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAAY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 239 WAFAAAMTRGDITVRGVDPKHI---NLVLEKLRTAGATVTTGENEFRVVQEG--RPESVDFVTLPYPGFATDLQPFAIAL 313
Cdd:pfam00275 241 FLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPglRGKAVDIRTAPDPAPTTAVLAAFAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 314 SAVSAGTSMITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVE-RLSSAPVWAS-DIRAGAGLVLAGLCADGATEVYE 391
Cdd:pfam00275 321 TTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYgDHRIAMALALAGLVAEGETIIDD 400
                         410
                  ....*....|....*
gi 2267612541 392 IFHIERGYPGFVENL 406
Cdd:pfam00275 401 IECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
3-416 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 637.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGD-VATITTPAELN 81
Cdd:PRK09369    2 DKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNINN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  82 HRADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQG-LHGAQVWLD 160
Cdd:PRK09369   82 TEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGrLKGAHIVLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 161 FPSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWA 240
Cdd:PRK09369  162 FPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTFL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 241 FAAAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEGRPESVDFVTLPYPGFATDLQPFAIALSAVSAGT 320
Cdd:PRK09369  242 VAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEGT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 321 SMITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYP 400
Cdd:PRK09369  322 SVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGYE 401
                         410
                  ....*....|....*.
gi 2267612541 401 GFVENLRKLGATVERV 416
Cdd:PRK09369  402 RIEEKLRALGADIERV 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
3-416 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: 612.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVT-IEGDVATITTPAELN 81
Cdd:COG0766     2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVErDDGGTLTIDASNINS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  82 HRADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQGLHGAQVWLDF 161
Cdd:COG0766    82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLDF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 162 PSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAF 241
Cdd:COG0766   162 PSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFLV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 242 AAAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEGRPESVDFVTLPYPGFATDLQPFAIALSAVSAGTS 321
Cdd:COG0766   242 AAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGTS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 322 MITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYPG 401
Cdd:COG0766   322 VITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYEN 401
                         410
                  ....*....|....*
gi 2267612541 402 FVENLRKLGATVERV 416
Cdd:COG0766   402 LEEKLRALGADIERV 416
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
3-415 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: 544.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATITTPAELNH 82
Cdd:TIGR01072   2 DKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  83 RADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQG-LHGAQVWLDF 161
Cdd:TIGR01072  82 EAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGrLVGAHIVLDK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 162 PSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAF 241
Cdd:TIGR01072 162 VSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFLV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 242 AAAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEG-RPESVDFVTLPYPGFATDLQPFAIALSAVSAGT 320
Cdd:TIGR01072 242 AAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQAEGT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 321 SMITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYP 400
Cdd:TIGR01072 322 SVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGYE 401
                         410
                  ....*....|....*
gi 2267612541 401 GFVENLRKLGATVER 415
Cdd:TIGR01072 402 DLEEKLRALGAKIER 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
13-409 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: 539.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  13 LVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEG-DVATITTPAELNHRADSEAMGK 91
Cdd:cd01555     1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  92 LRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAE-AQGLHGAQVWLDFPSVGATENI 170
Cdd:cd01555    81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKaAGRLKGARIYLDFPSVGATENI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 171 LMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAFAAAMTRGDI 250
Cdd:cd01555   161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 251 TVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEG-RPESVDFVTLPYPGFATDLQPFAIALSAVSAGTSMITENLFE 329
Cdd:cd01555   241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 330 ARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYPGFVENLRKL 409
Cdd:cd01555   321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
3-418 2.14e-147

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 425.04  E-value: 2.14e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   3 EHFRVQGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATITTPAELNH 82
Cdd:PRK12830    2 EKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQSM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  83 RADSEAMGKLRASVCVLGPLVGRCKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQGLHGAQVWLDFP 162
Cdd:PRK12830   82 PLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGAHIYLDVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 163 SVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAFA 242
Cdd:PRK12830  162 SVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYMIL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 243 AAMTRGDITVRGVDPKHINLVLEKLRTAGATVTTGENEFRVVQEGRPESVDFVTLPYPGFATDL-QPFAiALSAVSAGTS 321
Cdd:PRK12830  242 AAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLqQPLT-PLLLKANGRS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 322 MITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWASDIRAGAGLVLAGLCADGATEVYEIFHIERGYPG 401
Cdd:PRK12830  321 VVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYSN 400
                         410
                  ....*....|....*..
gi 2267612541 402 FVENLRKLGATVERVSV 418
Cdd:PRK12830  401 IIEKLKALGADIWREED 417
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-406 2.79e-110

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 330.41  E-value: 2.79e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541   8 QGGARLVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVT-IEGDVATITTPAELNH-RAD 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIkLDDEKSVVIVEGLGGSfEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  86 SEAMGKLRASVCVLGPLVGRCKRAV--VALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVA----EAQGLHGAQVWL 159
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHIDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 160 DFPSVGATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTST-LTVHGVPELHPTEHRVIGDRIVGAT 238
Cdd:pfam00275 161 DVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAAY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 239 WAFAAAMTRGDITVRGVDPKHI---NLVLEKLRTAGATVTTGENEFRVVQEG--RPESVDFVTLPYPGFATDLQPFAIAL 313
Cdd:pfam00275 241 FLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPglRGKAVDIRTAPDPAPTTAVLAAFAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 314 SAVSAGTSMITENLFEARFRFIEEMVRLGADARTDGHHAVVRGVE-RLSSAPVWAS-DIRAGAGLVLAGLCADGATEVYE 391
Cdd:pfam00275 321 TTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYgDHRIAMALALAGLVAEGETIIDD 400
                         410
                  ....*....|....*
gi 2267612541 392 IFHIERGYPGFVENL 406
Cdd:pfam00275 401 IECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
13-409 2.39e-68

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: 222.09  E-value: 2.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  13 LVGEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATITTPAELNHRADSEA--MG 90
Cdd:cd01554     1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQNAlnLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  91 K-LRASVCVLGPLVGRCKRavVALPGGDAIGSRPLDMHQSGLRKLGAHSEIEHGCVVAEAQ---GLHGAQVWLD-FPSVG 165
Cdd:cd01554    81 NsGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLkggKNLGPIHYEDpIASAQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 166 ATENILMAAVLADGTTVIDNAAREPEIVDICVMLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAFAAAM 245
Cdd:cd01554   159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 246 TRGDITVRGVDPKHINL-VLEKLRTAGATVTTGEnEFRVVQEGRPESVDFVTLPYPgFATDLQPFAIALSAVSAGTSMIT 324
Cdd:cd01554   239 APGRLVLQNVGINETRTgIIDVLRAMGAKIEIGE-DTISVESSDLKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 325 ENLF------EARFRFIEEMVRLGADARTDGHHAVVRGVERLSSAPVWA-SDIRAGAGLVLAGLCADGATEVYEIFHIER 397
Cdd:cd01554   317 DAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTfGDHRIGMMTALAALVADGEVELDRAEAINT 396
                         410
                  ....*....|..
gi 2267612541 398 GYPGFVENLRKL 409
Cdd:cd01554   397 SYPSFFDDLESL 408
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
37-409 2.54e-21

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: 95.16  E-value: 2.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  37 EGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATITTPAElnhradseamGKLRASVCVL-----G----PLVGrck 107
Cdd:COG0128    36 EGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGVG----------GGLKEPDAVLdcgnsGttmrLLTG--- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 108 rAVVALPG-----GDA-IGSRPLDMHQSGLRKLGAH-SEIEHGC--VVAEAQGLHGAQVWLD------FPSvgAtenILM 172
Cdd:COG0128   103 -LLALQPGevvltGDEsLRKRPMGRLLDPLRQLGARiESRGGGYlpLTIRGGPLKGGEYEIPgsassqFKS--A---LLL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 173 AAVLADGTTVIDNAAREPEI--VDICV-MLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDrIVGAT-WAFAAAMTRG 248
Cdd:COG0128   177 AGPLAEGGLEITVTGELESKpyRDHTErMLRAFGVEVEVEGYRRFTVPGGQRYRPGDYTVPGD-ISSAAfFLAAAAITGS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 249 DITVRGVDPKHI---NLVLEKLRTAGATVTTGENEFRVVQEG-RPESVDFVTLPypgfatDLQPFAIALSAVSAGTSMIT 324
Cdd:COG0128   256 EVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITVRGSPlKGIDIDLSDIP------DEAPTLAVLAAFAEGTTRIR 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 325 eNLFEARF----RF---IEEMVRLGADARTDGHHAVVRGVERLSSAPVWAS-DIR---AGAglvLAGLCADGATEVYEIF 393
Cdd:COG0128   330 -GAAELRVkesdRIaamATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYgDHRiamAFA---VAGLRAEGPVTIDDAE 405
                         410
                  ....*....|....*.
gi 2267612541 394 HIERGYPGFVENLRKL 409
Cdd:COG0128   406 CVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
37-409 9.07e-21

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: 93.39  E-value: 9.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  37 EGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATITTPAELNHRADSEA-MGK----LRAsvcvLGPLVGRCKRAVV 111
Cdd:cd01556    25 EGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGLPPEAVLdCGNsgttMRL----LTGLLALQGGDSV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 112 aLPGGDAIGSRPLDMHQSGLRKLGAH--SEIEHGCV-VAEAQGLHG----------AQVwldfpsVGAtenILMAAVLAD 178
Cdd:cd01556   101 -LTGDESLRKRPMGRLVDALRQLGAEieGREGGGYPpLIGGGGLKGgeveipgavsSQF------KSA---LLLAAPLAE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 179 GTTVIDNAAREPEI-VDICV-MLQQMGARIEGAGTSTLTVHGVPELHPTEHRVIGDrIVGAT-WAFAAAMTRGDITVRGV 255
Cdd:cd01556   171 GPTTIIIGELESKPyIDHTErMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGD-ASSAAfFLAAAAITGSEIVIKNV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 256 DP----KHINLVLEKLrtaGATVTTGENEFRVVQEGRPES---VDfvtlpyPGFATDLQPFAIALSAVSAGTSMITeNLF 328
Cdd:cd01556   250 GLnsgdTGIIDVLKEM---GADIEIGNEDTVVVESGGKLKgidID------GNDIPDEAPTLAVLAAFAEGPTRIR-NAA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 329 EARF----RfIEEMV----RLGADAR--TDGhhAVVRGVErLSSAPVWAS---DIRAGAGLVLAGLCADGATEVYEIFHI 395
Cdd:cd01556   320 ELRVkesdR-IAAMAtelrKLGADVEetEDG--LIIEGGP-LKGAGVEVYtygDHRIAMSFAIAGLVAEGGVTIEDPECV 395
                         410
                  ....*....|....
gi 2267612541 396 ERGYPGFVENLRKL 409
Cdd:cd01556   396 AKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
37-411 8.23e-19

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: 87.72  E-value: 8.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  37 EGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATITTPAElnhrADSEAMGKLRASVCVLGPLVGrckraVVALPGG 116
Cdd:TIGR01356  23 EGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGG----KEPQAELDLGNSGTTARLLTG-----VLALADG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 117 -------DAIGSRPLDMHQSGLRKLGA--HSEIEHGCV-VAEAQGLHGAQVWLDfPSVGA--TENILMAAVLADGTTVID 184
Cdd:TIGR01356  94 evvltgdESLRKRPMGRLVDALRQLGAeiSSLEGGGSLpLTISGPLPGGIVYIS-GSASSqyKSALLLAAPALQAVGITI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 185 NAAREPEIVDICVMLQQMGA---RIEGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAFAAAMTRGDITVRGVDP---- 257
Cdd:TIGR01356 173 VGEPLKSRPYIEITLDLLGSfgvEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAAITGGRVTLENLGInptq 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 258 --KHINLVLEKLrtaGATVTTGENEFRVVQ--EGRPESVDFVTLPypgfatDLQPFAIALSAVSAGTSMITeNLFEARFR 333
Cdd:TIGR01356 253 gdKAIIIVLEEM---GADIEVEEDDLIVEGasGLKGIKIDMDDMI------DELPTLAVLAAFAEGVTRIT-GAEELRVK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 334 -------FIEEMVRLGADARTDGHHAVVRGVERLSSApVWAS--DIRAGAGLVLAGLCADGATEVYEIFHIERGYPGFVE 404
Cdd:TIGR01356 323 esdriaaIAEELRKLGVDVEEFEDGLYIRGKKELKGA-VVDTfgDHRIAMAFAVAGLVAEGEVLIDDPECVAKSFPSFFD 401

                  ....*..
gi 2267612541 405 NLRKLGA 411
Cdd:TIGR01356 402 VLERLGA 408
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
124-414 2.23e-14

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: 74.23  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 124 LDMHQsGLRKLGAHSEIEHGCVVAEAQGLHGAQVWLDFPSVGATENILMAAV-LADGTTVI--DNAAREPEIVDICVMLQ 200
Cdd:TIGR01356  38 LATLD-ALRALGAKIEDGGEVAVIEGVGGKEPQAELDLGNSGTTARLLTGVLaLADGEVVLtgDESLRKRPMGRLVDALR 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 201 QMGARI---EGAGTSTLTVHGVPELHPTEHRVIGDRIVGATWAFAAAMTRGD-ITVRGVDPK---HINLVLEKLRTAGAT 273
Cdd:TIGR01356 117 QLGAEIsslEGGGSLPLTISGPLPGGIVYISGSASSQYKSALLLAAPALQAVgITIVGEPLKsrpYIEITLDLLGSFGVE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 274 VT-TGENEFRVVQEGRPESVDFVTLPYPGFATdlqpFAIALSAVSAGTSMItENLFE----ARFRFIEEMVRLGADARTD 348
Cdd:TIGR01356 197 VErSDGRKIVVPGGQKYGPQGYDVPGDYSSAA----FFLAAAAITGGRVTL-ENLGInptqGDKAIIIVLEEMGADIEVE 271
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2267612541 349 GHHAVVRGVERLSSAPVWASD-IRAGAGLVLAGLCADGATEVYEIFHI-----ERgYPGFVENLRKLGATVE 414
Cdd:TIGR01356 272 EDDLIVEGASGLKGIKIDMDDmIDELPTLAVLAAFAEGVTRITGAEELrvkesDR-IAAIAEELRKLGVDVE 342
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
37-414 2.17e-12

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 68.25  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  37 EGTTTITNCPEILDVPLMADVLRSLGceVTIEGDVATITTPAELNHRADSEA--MGK----LRasvcvlgPLVGrckraV 110
Cdd:PRK02427   37 EGETTITNLLRSEDTLATLNALRALG--VEIEDDEVVVEGVGGGGLKEPEDVldCGNsgttMR-------LLTG-----L 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 111 VAL-PG-----GDA-IGSRPLDMHQSGLRKLGAH-SEIEHGC---VVAEAQGLHGAQVWLDFPSVGATENILMAAVLADG 179
Cdd:PRK02427  103 LALqPGevvltGDEsLRKRPMGRLLDPLRQMGAKiEGRDEGYlplTIRGGKKGGPIEYDGPVSSQFVKSLLLLAPLFAEG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 180 TTVIDnaAREPEI----VDICV-MLQQMGARIE---GAGTSTLTVHGVPELHPTEHRVIGDrIVGAT-WAFAAAMTRG-D 249
Cdd:PRK02427  183 DTETT--VIEPLPsrphTEITLrMLRAFGVEVEnveGWGYRRIVIKGGQRLRGQDITVPGD-PSSAAfFLAAAAITGGsE 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 250 ITVRGVDPKHI---NLVLEKLRTAGATVTTGENEFRVVQEG----RPESVDFVTLPYPGfATDLQPfAIA-LSAVSAGTS 321
Cdd:PRK02427  260 VTITNVGLNSTqggKAIIDVLEKMGADIEIENEREGGEPVGdirvRSSELKGIDIDIPD-IIDEAP-TLAvLAAFAEGTT 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 322 MITeNLFEARF----RfIEEMV----RLGADA--RTDGhhAVVRGVERlssAPVWAS--DIRAGAGLVLAGLCADGATEV 389
Cdd:PRK02427  338 VIR-NAEELRVketdR-IAAMAtelrKLGAEVeeTEDG--LIITGGPL---AGVVDSygDHRIAMAFAIAGLAAEGPVTI 410
                         410       420
                  ....*....|....*....|....*
gi 2267612541 390 YEIFHIERGYPGFVENLRKLGATVE 414
Cdd:PRK02427  411 DDPECVAKSFPDFFEDLASLGANIE 435
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
37-283 3.49e-06

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 48.98  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  37 EGTTTITNCPEILDVPLMADVLRSLGCEVT---------IEGDVATITTPAELNHRAD------SEAMGKLRASVCVLGp 101
Cdd:PLN02338   36 EGTTVVDNLLDSDDIRYMLGALKTLGLNVEedsennravVEGCGGKFPVSGDSKEDVElflgnaGTAMRPLTAAVTAAG- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 102 lvgrcKRAVVALPGGDAIGSRPLDMHQSGLRKLGAHSE--IEHGC---VVAEAQGLHGAQVWLDfPSVGAT--ENILMAA 174
Cdd:PLN02338  115 -----GNASYVLDGVPRMRERPIGDLVDGLKQLGADVEctLGTNCppvRVNAAGGLPGGKVKLS-GSISSQylTALLMAA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 175 VLADGTTVIdnaarepEIVDICV----------MLQQMGARIEGAGT--STLTVHGVPELHPTEHRVIGDRIVGATWAFA 242
Cdd:PLN02338  189 PLALGDVEI-------EIVDKLIsvpyvemtlkLMERFGVSVEHSDSwdRFFIKGGQKYKSPGNAYVEGDASSASYFLAG 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2267612541 243 AAMTRGDITVRGV-------DPKHINlVLEKLrtaGATVTTGENEFRV 283
Cdd:PLN02338  262 AAITGGTVTVEGCgttslqgDVKFAE-VLEKM---GAKVEWTENSVTV 305
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
171-414 6.35e-06

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: 48.16  E-value: 6.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 171 LMAAVLADGTTVIDNAAR-EpeivDICVM---LQQMGARIEGAGTSTLTVHGVPE------------------------- 221
Cdd:COG0128    29 LLLAALAEGESTIRNLLEsD----DTLATleaLRALGAEIEELDGGTLRVTGVGGglkepdavldcgnsgttmrlltgll 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 222 -LHPTEHRVIGD--------------------------------RIVGATWA-------------------FAAAMTRGD 249
Cdd:COG0128   105 aLQPGEVVLTGDeslrkrpmgrlldplrqlgariesrgggylplTIRGGPLKggeyeipgsassqfksallLAGPLAEGG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 250 ITVRGVDP----KHINLVLEKLRTAGATVTT-GENEFRVVQEGRPESVDFVTLPYPGFATdlqpFAIALSAVSAGTSMIT 324
Cdd:COG0128   185 LEITVTGEleskPYRDHTERMLRAFGVEVEVeGYRRFTVPGGQRYRPGDYTVPGDISSAA----FFLAAAAITGSEVTVE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 325 ---ENLFEARFRFIEEMVRLGADARTDGHHAVVRGvERLSS-----------APVwasdiragagLVLAGLCADGATEVY 390
Cdd:COG0128   261 gvgLNSTQGDTGILDILKEMGADIEIENDGITVRG-SPLKGididlsdipdeAPT----------LAVLAAFAEGTTRIR 329
                         330       340
                  ....*....|....*....|....*....
gi 2267612541 391 EIFHIeRGY-----PGFVENLRKLGATVE 414
Cdd:COG0128   330 GAAEL-RVKesdriAAMATELRKLGADVE 357
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
231-409 2.49e-04

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: 42.27  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 231 GDRIVGATWAFAAAMTRGDITVRGVDPKHINL--------VLEKLRTA-GATVTTGE--NEFRVVQEGRPESVDFVTLPY 299
Cdd:cd01553     8 GGGQILRSFLVLAAISGGPITVTGIRPDRAKPgllrqhltFLKALEKIcGATVEGGElgSDRISFRPGTVRGGDVRFAIG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 300 P-GFATD-LQPFAIALsAVSAGTSMITENLF----------EARFRFIEEMVRLGADART------------DGHHAVVR 355
Cdd:cd01553    88 SaGSCTDvLQTILPLL-LFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEEtllrhgfypaggGVVATEVS 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2267612541 356 GVERLSSApvwasDIRAGAGLVLAGlcadGATEVYEIFHIERGYPGFVENLRKL 409
Cdd:cd01553   167 PVEKLNTA-----QLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
15-364 3.78e-04

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 42.77  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  15 GEVDVVGAKNSVLKLMAAALLAEGTTTITNCPEILDVPLMADVLRSLGCEVTIEGDVATI-TTPAELNHRADSEAMGKLR 93
Cdd:PRK11861  253 GTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVgGTRGAFTAKTADLFLGNAG 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541  94 ASVcvlgplvgRCKRAVVALPGGD-------AIGSRPLDMHQSGLRKLGAHSEIEhGCVVAEAQGLHGAQVWLDFP--SV 164
Cdd:PRK11861  333 TAV--------RPLTAALAVNGGEyrihgvpRMHERPIGDLVDGLRQIGARIDYE-GNEGFPPLRIRPATISVDAPirVR 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 165 GATENILMAAVL--------ADGTTVID---NAAREPEIVDICVMLQQMGARIEGAGTSTLTV-HGVPELHPTEHRVIGD 232
Cdd:PRK11861  404 GDVSSQFLTALLmtlplvkaKDGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVpAGVRYRSPGTIMVEGD 483
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 233 RIVGATWAFAAAMTRGDITVRGVDPKHIN---LVLEKLRTAGATVTTGENEFRVVQEGR------PESVDFVTLPYPGfa 303
Cdd:PRK11861  484 ASSASYFLAAGALGGGPLRVEGVGRASIQgdvGFANALMQMGANVTMGDDWIEVRGIGHdhgrlaPIDMDFNLIPDAA-- 561
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2267612541 304 tdlqpFAIALSAVSAGTSMITENLFEARFRFIEEMVRLGADARTDGhHAVVRGVERLSSAP 364
Cdd:PRK11861  562 -----MTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVG-ATVEEGADYLVVTP 616
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
171-281 2.13e-03

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 40.13  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267612541 171 LMAAVLADGTTVIDNAAREPeivDICVM---LQQMGARIEgagTSTLTVHGVPELHPTEHRVIGD--------RIVgatw 239
Cdd:PRK02427   30 LLLAALAEGETTITNLLRSE---DTLATlnaLRALGVEIE---DDEVVVEGVGGGGLKEPEDVLDcgnsgttmRLL---- 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2267612541 240 AFAAAMTRGDITVRGVD-----PkhINLVLEKLRTAGATVTTGENEF 281
Cdd:PRK02427  100 TGLLALQPGEVVLTGDEslrkrP--MGRLLDPLRQMGAKIEGRDEGY 144
 
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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