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Conserved domains on  [gi|489084519|ref|WP_002994428|]
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UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Streptococcus pyogenes]

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
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


:

Pssm-ID: 236486  Cd Length: 417  Bit Score: 690.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   1 MDKIIIEGGqTRLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAaNEITVDAS 80
Cdd:PRK09369   1 MDKLVIEGG-KPLSGEVTISGAKNAALPILAASLL-AEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGN-GTVTIDAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQAD-RLQGAM 159
Cdd:PRK09369  78 NINNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADgRLKGAH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 160 IYMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 240 GTFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANtPKLKPVTVKTLPHPGFPTDMQAQFTALMA 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMP-GRLKAVDIKTAPYPGFPTDMQAQFMALLT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 320 VVNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHL 399
Cdd:PRK09369 317 QAEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHL 396
                        410       420
                 ....*....|....*....|
gi 489084519 400 DRGYYQFHEKLAKLGATISR 419
Cdd:PRK09369 397 DRGYERIEEKLRALGADIER 416
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 690.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   1 MDKIIIEGGqTRLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAaNEITVDAS 80
Cdd:PRK09369   1 MDKLVIEGG-KPLSGEVTISGAKNAALPILAASLL-AEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGN-GTVTIDAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQAD-RLQGAM 159
Cdd:PRK09369  78 NINNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADgRLKGAH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 160 IYMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 240 GTFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANtPKLKPVTVKTLPHPGFPTDMQAQFTALMA 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMP-GRLKAVDIKTAPYPGFPTDMQAQFMALLT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 320 VVNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHL 399
Cdd:PRK09369 317 QAEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHL 396
                        410       420
                 ....*....|....*....|
gi 489084519 400 DRGYYQFHEKLAKLGATISR 419
Cdd:PRK09369 397 DRGYERIEEKLRALGADIER 416
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-419 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: 668.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   1 MDKIIIEGGqTRLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAaNEITVDAS 80
Cdd:COG0766    1 MDKLIIEGG-KPLSGEVRISGAKNAALPILAAALL-TDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDG-GTLTIDAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQADRLQGAMI 160
Cdd:COG0766   78 NINSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 161 YMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAG 240
Cdd:COG0766  158 YLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 241 TFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANTpKLKPVTVKTLPHPGFPTDMQAQFTALMAV 320
Cdd:COG0766  238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQ 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 321 VNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHLD 400
Cdd:COG0766  317 AEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHID 396
                        410
                 ....*....|....*....
gi 489084519 401 RGYYQFHEKLAKLGATISR 419
Cdd:COG0766  397 RGYENLEEKLRALGADIER 415
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
13-413 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: 599.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  13 LEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAaNEITVDASGHILDEAPYEYV 92
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALL-TDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGE-NTLVIDASNINSTEAPYELV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  93 SQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQ-ADRLQGAMIYMDFPSVGATQ 171
Cdd:cd01555   79 RKMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKaAGRLKGARIYLDFPSVGATE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 172 NLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAGTFMVAAAMTSG 251
Cdd:cd01555  159 NIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 252 NVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANTPKLKPVTVKTLPHPGFPTDMQAQFTALMAVVNGESTMVETV 331
Cdd:cd01555  239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 332 FENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHLDRGYYQFHEKLA 411
Cdd:cd01555  319 FENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398

                 ..
gi 489084519 412 KL 413
Cdd:cd01555  399 AL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-419 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: 561.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519    1 MDKIIIEGGqTRLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEaaNEITVDAS 80
Cdd:TIGR01072   1 MDKLVVEGG-KPLSGEVTISGAKNAALPIIAATLL-TDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDN--NTLEINTP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQA-DRLQGAM 159
Cdd:TIGR01072  77 NINSTEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAkGRLVGAH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  160 IYMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEA 239
Cdd:TIGR01072 157 IVLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  240 GTFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANTPKLKPVTVKTLPHPGFPTDMQAQFTALMA 319
Cdd:TIGR01072 237 GTFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  320 VVNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHL 399
Cdd:TIGR01072 317 QAEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHL 396
                         410       420
                  ....*....|....*....|
gi 489084519  400 DRGYYQFHEKLAKLGATISR 419
Cdd:TIGR01072 397 DRGYEDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
9-410 1.23e-119

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 354.30  E-value: 1.23e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519    9 GQTRLEGEVVIEG-AKNAVLPLLAASILpsKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAANEITVDASGHILDEA 87
Cdd:pfam00275   2 GGSRLSGEVKIPGsKSNSHRALILAALA--AGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   88 PYEYVSQMRASIVVLGPILARNGHAK--VSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITA----QADRLQGAMIY 161
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  162 MDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTET-LTITGVTHLRGVEHDVVQDRIEAG 240
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  241 TFMVAAAMTSGNVLIRDAVWEHNRP---LISKLMEMGVSVTEEE-YGIRVQANTPKLKPVTVKTLPHPGFPTDMQAQFTA 316
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLQGdeaLLEILEKMGAEITQEEdADIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  317 LMAVVNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQ-LQGAPVMST-DLRASAALILTGIVAQGVTIVN 394
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 489084519  395 NLVHLDRGYYQFHEKL 410
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 690.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   1 MDKIIIEGGqTRLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAaNEITVDAS 80
Cdd:PRK09369   1 MDKLVIEGG-KPLSGEVTISGAKNAALPILAASLL-AEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGN-GTVTIDAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQAD-RLQGAM 159
Cdd:PRK09369  78 NINNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADgRLKGAH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 160 IYMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 240 GTFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANtPKLKPVTVKTLPHPGFPTDMQAQFTALMA 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMP-GRLKAVDIKTAPYPGFPTDMQAQFMALLT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 320 VVNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHL 399
Cdd:PRK09369 317 QAEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHL 396
                        410       420
                 ....*....|....*....|
gi 489084519 400 DRGYYQFHEKLAKLGATISR 419
Cdd:PRK09369 397 DRGYERIEEKLRALGADIER 416
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-419 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: 668.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   1 MDKIIIEGGqTRLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAaNEITVDAS 80
Cdd:COG0766    1 MDKLIIEGG-KPLSGEVRISGAKNAALPILAAALL-TDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDG-GTLTIDAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQADRLQGAMI 160
Cdd:COG0766   78 NINSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 161 YMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAG 240
Cdd:COG0766  158 YLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 241 TFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANTpKLKPVTVKTLPHPGFPTDMQAQFTALMAV 320
Cdd:COG0766  238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQ 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 321 VNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHLD 400
Cdd:COG0766  317 AEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHID 396
                        410
                 ....*....|....*....
gi 489084519 401 RGYYQFHEKLAKLGATISR 419
Cdd:COG0766  397 RGYENLEEKLRALGADIER 415
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
13-413 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: 599.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  13 LEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAaNEITVDASGHILDEAPYEYV 92
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALL-TDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGE-NTLVIDASNINSTEAPYELV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  93 SQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQ-ADRLQGAMIYMDFPSVGATQ 171
Cdd:cd01555   79 RKMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKaAGRLKGARIYLDFPSVGATE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 172 NLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAGTFMVAAAMTSG 251
Cdd:cd01555  159 NIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 252 NVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANTPKLKPVTVKTLPHPGFPTDMQAQFTALMAVVNGESTMVETV 331
Cdd:cd01555  239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 332 FENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHLDRGYYQFHEKLA 411
Cdd:cd01555  319 FENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398

                 ..
gi 489084519 412 KL 413
Cdd:cd01555  399 AL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-419 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: 561.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519    1 MDKIIIEGGqTRLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEaaNEITVDAS 80
Cdd:TIGR01072   1 MDKLVVEGG-KPLSGEVTISGAKNAALPIIAATLL-TDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDN--NTLEINTP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQA-DRLQGAM 159
Cdd:TIGR01072  77 NINSTEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAkGRLVGAH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  160 IYMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEA 239
Cdd:TIGR01072 157 IVLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  240 GTFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANTPKLKPVTVKTLPHPGFPTDMQAQFTALMA 319
Cdd:TIGR01072 237 GTFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  320 VVNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHL 399
Cdd:TIGR01072 317 QAEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHL 396
                         410       420
                  ....*....|....*....|
gi 489084519  400 DRGYYQFHEKLAKLGATISR 419
Cdd:TIGR01072 397 DRGYEDLEEKLRALGAKIER 416
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-422 4.65e-170

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 482.82  E-value: 4.65e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   1 MDKIIIEGGQTrLEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEaaNEITVDAS 80
Cdd:PRK12830   1 MEKIVINGGKP-LSGEVTISGAKNSAVALIPAAIL-ADGPVTLDGVPDISDVHSLVDILEELGGKVKRDG--DTLEIDPT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  81 GHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQADRLQGAMI 160
Cdd:PRK12830  77 GIQSMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGAHI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 161 YMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAG 240
Cdd:PRK12830 157 YLDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 241 TFMVAAAMTSGNVLIRDAVWEHNRPLISKLMEMGVSVTEEEYGIRVQANTPkLKPVTVKTLPHPGFPTDMQAQFTALMAV 320
Cdd:PRK12830 237 TYMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGN-LKAVDIKTLPYPGFATDLQQPLTPLLLK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 321 VNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTDLRASAALILTGIVAQGVTIVNNLVHLD 400
Cdd:PRK12830 316 ANGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHID 395
                        410       420
                 ....*....|....*....|..
gi 489084519 401 RGYYQFHEKLAKLGATISRSSE 422
Cdd:PRK12830 396 RGYSNIIEKLKALGADIWREED 417
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
9-410 1.23e-119

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 354.30  E-value: 1.23e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519    9 GQTRLEGEVVIEG-AKNAVLPLLAASILpsKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAANEITVDASGHILDEA 87
Cdd:pfam00275   2 GGSRLSGEVKIPGsKSNSHRALILAALA--AGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   88 PYEYVSQMRASIVVLGPILARNGHAK--VSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITA----QADRLQGAMIY 161
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  162 MDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTET-LTITGVTHLRGVEHDVVQDRIEAG 240
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  241 TFMVAAAMTSGNVLIRDAVWEHNRP---LISKLMEMGVSVTEEE-YGIRVQANTPKLKPVTVKTLPHPGFPTDMQAQFTA 316
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLQGdeaLLEILEKMGAEITQEEdADIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  317 LMAVVNGESTMVETVFENRFQHLEEMRRMGLQSEILRETAMIHGGRQ-LQGAPVMST-DLRASAALILTGIVAQGVTIVN 394
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 489084519  395 NLVHLDRGYYQFHEKL 410
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
13-413 1.47e-78

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: 248.67  E-value: 1.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  13 LEGEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAANEIT-VDASGHILDEAPYEY 91
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASL-AEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQgVGMAGLKAPQNALNL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  92 VSQMRASIVVLGPILARNGhaKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQAD---RLQGAMIYMD-FPSV 167
Cdd:cd01554   80 GNSGTAIRLISGVLAGADF--EVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLkggKNLGPIHYEDpIASA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 168 GATQNLMMAATLADGVTTIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAGTFMVAAA 247
Cdd:cd01554  158 QVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 248 MTSGNVLIRDAVWEHNR-PLISKLMEMGVSVTEEEYGIRVQANtpKLKPVTVKTLPHPgFPTDMQAQFTALMAVVNGEST 326
Cdd:cd01554  238 IAPGRLVLQNVGINETRtGIIDVLRAMGAKIEIGEDTISVESS--DLKATEICGALIP-RLIDELPIIALLALQAQGTTV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 327 MVETVF------ENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMST-DLRASAALILTGIVAQGVTIVNNLVHL 399
Cdd:cd01554  315 IKDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAI 394
                        410
                 ....*....|....
gi 489084519 400 DRGYYQFHEKLAKL 413
Cdd:cd01554  395 NTSYPSFFDDLESL 408
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-395 1.91e-20

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: 92.84  E-value: 1.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   1 MDKIIIEGGqTRLEGEVVIEGAKN----AvlpLLAASIlpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDfNEAANEIT 76
Cdd:COG0128    1 MSSLTIAPP-SPLKGTVRVPGSKSishrA---LLLAAL--AEGESTIRNLLESDDTLATLEALRALGAEIE-ELDGGTLR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  77 VDASGHILDEaPYEYV------SQMRasivVLGPILA-RNGHAKVSmpGGCTIGSRPINLHLKGLEAMGATITQKGGD-- 147
Cdd:COG0128   74 VTGVGGGLKE-PDAVLdcgnsgTTMR----LLTGLLAlQPGEVVLT--GDESLRKRPMGRLLDPLRQLGARIESRGGGyl 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 148 -ITAQADRLQGamIYMDFPSVGATQ---NLMMAATLADGVTTIENAAREPEI--VDLA-QFLNKMGARIRGAGTETLTIT 220
Cdd:COG0128  147 pLTIRGGPLKG--GEYEIPGSASSQfksALLLAGPLAEGGLEITVTGELESKpyRDHTeRMLRAFGVEVEVEGYRRFTVP 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 221 GVTHLRGVEHDVVQDRIEAGTFMVAAAMTSGNVLIRDavWEHN-----RPLISKLMEMGVSVTEEEYGIRVQANtpKLKP 295
Cdd:COG0128  225 GGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEG--VGLNstqgdTGILDILKEMGADIEIENDGITVRGS--PLKG 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 296 VTVktlphPG------FPTdmqaqFTALMAVVNGESTMV--------ETvfeNRFQHL-EEMRRMGLQSEILRETAMIHG 360
Cdd:COG0128  301 IDI-----DLsdipdeAPT-----LAVLAAFAEGTTRIRgaaelrvkES---DRIAAMaTELRKLGADVEETEDGLIIEG 367
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 489084519 361 GRQLQGAPVMS-TDLR-ASAALILtGIVAQGVTIVNN 395
Cdd:COG0128  368 GPKLKGAEVDSyGDHRiAMAFAVA-GLRAEGPVTIDD 403
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
15-415 2.92e-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: 88.87  E-value: 2.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   15 GEVVIEGAKNAVLPLLAASILpSKGKTILRNVPILSDVFTMNNVVRglDIRVDFNEAANEITVDASGHILDEAPYEyvsq 94
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAAL-AEGETRVRNLLRSEDTLATLDALR--ALGAKIEDGGEVAVIEGVGGKEPQAELD---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   95 MRAS---IVVLGPILARNGhAKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITAQAD---RLQGAMIYMDfPSVG 168
Cdd:TIGR01356  74 LGNSgttARLLTGVLALAD-GEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTisgPLPGGIVYIS-GSAS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  169 AtQ---NLMMAATLADGVT---TIENAAREPEIVDLAQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAGTF 242
Cdd:TIGR01356 152 S-QyksALLLAAPALQAVGitiVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  243 MVAAAMTSGNVLIRDaVWEH----NRPLISKLMEMGVSVTEEEYGIRVQANtPKLKPVTVKTlphPGFPtDMQAQFTALM 318
Cdd:TIGR01356 231 LAAAAITGGRVTLEN-LGINptqgDKAIIIVLEEMGADIEVEEDDLIVEGA-SGLKGIKIDM---DDMI-DELPTLAVLA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  319 AVVNGESTM--VET--VFE-NRFQHL-EEMRRMGLQSEILRETAMIHGGRQLQGAPVMS-TDLRASAALILTGIVAQGVT 391
Cdd:TIGR01356 305 AFAEGVTRItgAEElrVKEsDRIAAIaEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTfGDHRIAMAFAVAGLVAEGEV 384
                         410       420
                  ....*....|....*....|....
gi 489084519  392 IVNNLVHLDRGYYQFHEKLAKLGA 415
Cdd:TIGR01356 385 LIDDPECVAKSFPSFFDVLERLGA 408
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
29-413 7.66e-17

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: 81.83  E-value: 7.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  29 LLAASIlpSKGKTILRNVPILSDVFTMNNVVRGLdiRVDFNEAANEITVDASGHILDEAPYE-YV----SQMRASIVVLG 103
Cdd:cd01556   18 LLLAAL--AEGESRIENLLDSDDTLATLEALRAL--GAKIEEEGGTVEIVGGGGLGLPPEAVlDCgnsgTTMRLLTGLLA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 104 piLARNghaKVSMPGGCTIGSRPINLHLKGLEAMGATITQKGGDITA---QADRLQGAMIYMDFPS----VGAtqnLMMA 176
Cdd:cd01556   94 --LQGG---DSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPpliGGGGLKGGEVEIPGAVssqfKSA---LLLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 177 ATLADGVTTIENAAREPEI-VDL-AQFLNKMGARIRGAGTETLTITGVTHLRGVEHDVVQDRIEAGTFMVAAAMTSGNVL 254
Cdd:cd01556  166 APLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDASSAAFFLAAAAITGSEIV 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 255 IRDavWEHN---RPLISKLMEMGVSVTEEEYGIRVQANTPKLKPVTVKTLPHPG-FPTdmqaqFTALMAVVNGESTMV-- 328
Cdd:cd01556  246 IKN--VGLNsgdTGIIDVLKEMGADIEIGNEDTVVVESGGKLKGIDIDGNDIPDeAPT-----LAVLAAFAEGPTRIRna 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 329 ------ETvfeNRFQHL-EEMRRMGLQSEILRETAMIHGGRQLQGAPVMST--DLRASAALILTGIVAQGVTIVNNLVHL 399
Cdd:cd01556  319 aelrvkES---DRIAAMaTELRKLGADVEETEDGLIIEGGPLKGAGVEVYTygDHRIAMSFAIAGLVAEGGVTIEDPECV 395
                        410
                 ....*....|....
gi 489084519 400 DRGYYQFHEKLAKL 413
Cdd:cd01556  396 AKSFPNFFEDLESL 409
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
134-258 1.81e-12

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: 68.58  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 134 LEAMGATITQKGGDITAQADRLQGAMIYMD-----FPSvgatqnLMMAATLADGVTTIENAA--REPE---IVDLAQFLN 203
Cdd:COG0128  277 LKEMGADIEIENDGITVRGSPLKGIDIDLSdipdeAPT------LAVLAAFAEGTTRIRGAAelRVKEsdrIAAMATELR 350
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489084519 204 KMGARIRgAGTETLTITGVTHLRGVE----HDvvqDRIeAGTFMVAAAMTSGNVLIRDA 258
Cdd:COG0128  351 KLGADVE-ETEDGLIIEGGPKLKGAEvdsyGD---HRI-AMAFAVAGLRAEGPVTIDDA 404
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
134-258 1.45e-11

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 65.93  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 134 LEAMGATITQK--------GGDITAQADRLQGamIYMDFPSVG-ATQNLMMAATLADGVTTIENAA--REPE---IVDLA 199
Cdd:PRK02427 280 LEKMGADIEIEnereggepVGDIRVRSSELKG--IDIDIPDIIdEAPTLAVLAAFAEGTTVIRNAEelRVKEtdrIAAMA 357
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489084519 200 QFLNKMGARIrgagTET---LTITGVTHLRGVE-HDvvqD-RIeAGTFMVAAAMTSGNVLIRDA 258
Cdd:PRK02427 358 TELRKLGAEV----EETedgLIITGGPLAGVVDsYG---DhRI-AMAFAIAGLAAEGPVTIDDP 413
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
235-413 7.53e-11

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: 61.53  E-value: 7.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 235 DRIEAGTFMVAAAMTSGNVLIRDAVWEHNRP--------LISKLMEM-GVSVTEEEYGIRVQANTP-KLKPVTVKTLPHP 304
Cdd:cd01553    9 GGQILRSFLVLAAISGGPITVTGIRPDRAKPgllrqhltFLKALEKIcGATVEGGELGSDRISFRPgTVRGGDVRFAIGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 305 -GFPTDMQAQFTALMAVVNGESTMVETVF----------ENRFQHLEEMRRMGLQSEILRETAMIHGGRQLQGAPVMSTD 373
Cdd:cd01553   89 aGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETLLRHGFYPAGGGVVATEVSPV 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489084519 374 LRASAALI---LTGIVAQGVTIVNNLVHLDRGYYQFHEKLAKL 413
Cdd:cd01553  169 EKLNTAQLrqlVLPMLLASGAVEFTVAHPSCHLLTNFAVLEAL 211
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
11-418 1.15e-06

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 50.53  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  11 TRLEGEVVIEGAKN----AvlpLLAASIlpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDfneaANEITVDASGHILDE 86
Cdd:PRK02427  11 SPLSGTVRVPGSKSishrA---LLLAAL--AEGETTITNLLRSEDTLATLNALRALGVEIE----DDEVVVEGVGGGGLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  87 APYEYV------SQMRASIVVLGpilARNGHAKVSmpGGCTIGSRPINLHLKGLEAMGATITQKGGD-----ITAQAdRL 155
Cdd:PRK02427  82 EPEDVLdcgnsgTTMRLLTGLLA---LQPGEVVLT--GDESLRKRPMGRLLDPLRQMGAKIEGRDEGylpltIRGGK-KG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 156 QGAMIYMDFPSVGATQNLMMAATLADGVTTIEnaAREPEI--------VDLaqfLNKMGARIR---GAGTETLTITGVTH 224
Cdd:PRK02427 156 GPIEYDGPVSSQFVKSLLLLAPLFAEGDTETT--VIEPLPsrphteitLRM---LRAFGVEVEnveGWGYRRIVIKGGQR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 225 LRGVEHDVVQDRIEAGTFMVAAAMTSG-NVLIRDavWEHN-----RPLISKLMEMGVSVTEE------EYGIRVQANTPK 292
Cdd:PRK02427 231 LRGQDITVPGDPSSAAFFLAAAAITGGsEVTITN--VGLNstqggKAIIDVLEKMGADIEIEnereggEPVGDIRVRSSE 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 293 LKPVTVkTLPHPG--FPTdmqaqFTALMAVVNGESTMV--------ETvfeNRFQHL-EEMRRMGLQSEILRETAMIHGG 361
Cdd:PRK02427 309 LKGIDI-DIPDIIdeAPT-----LAVLAAFAEGTTVIRnaeelrvkET---DRIAAMaTELRKLGAEVEETEDGLIITGG 379
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 362 RqlqGAPVMST--DLR-ASAALILtGIVAQGVTIVNNLVHLDRGYYQFHEKLAKLGATIS 418
Cdd:PRK02427 380 P---LAGVVDSygDHRiAMAFAIA-GLAAEGPVTIDDPECVAKSFPDFFEDLASLGANIE 435
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
91-259 1.76e-03

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 40.75  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  91 YVSQMRASIVVLGPILArnGHA-KVSMPGGCTIGSRPINLHLKGLEAMGATI-TQKGG----DITAQAdRLQGamIYMDF 164
Cdd:PRK14806 390 YMGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIeTGEEGrpplSIRGGQ-RLKG--IHYDL 464
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519 165 PsVGATQ---NLMMAATLADGVTTIenaaREPEIV--DLAQFLNKMGARIRGAGtETLTITGVTHLRGVEHDVVQDRIEA 239
Cdd:PRK14806 465 P-MASAQvksCLLLAGLYAEGETSV----TEPAPTrdHTERMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPADISSA 538
                        170       180
                 ....*....|....*....|
gi 489084519 240 GTFMVAAAMTSGNVLIRDAV 259
Cdd:PRK14806 539 AFFLVAASIAEGSELTLEHV 558
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
2-189 8.03e-03

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: 38.35  E-value: 8.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519   2 DKIIIEGGQTRLEGEVVIEG-AKNAVLPLLAASIlpSKGKTILRNVPILSDVFTMNNVVRGLDIRVDFNEAANEITV-DA 79
Cdd:cd01554  205 KKIVVQGPQKLTGQKYVVPGdISSAAFFLVAAAI--APGRLVLQNVGINETRTGIIDVLRAMGAKIEIGEDTISVESsDL 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489084519  80 SGHILDEAPYEYVSQMRASIVVLGPILARNGHAKVSMPGGCTIGSRpINLHLKGLEAMGATITQKG-GDITAQADRLQGA 158
Cdd:cd01554  283 KATEICGALIPRLIDELPIIALLALQAQGTTVIKDAEELKVKETDR-IFVVADELNSMGADIEPTAdGMIIKGKEKLHGA 361
                        170       180       190
                 ....*....|....*....|....*....|.
gi 489084519 159 MIyMDFPSVGATQNLMMAATLADGVTTIENA 189
Cdd:cd01554  362 RV-NTFGDHRIGMMTALAALVADGEVELDRA 391
 
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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