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Conserved domains on  [gi|653772739|ref|WP_027680232|]
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MULTISPECIES: UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Ralstonia]

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: 759.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKvEFDGNGTVTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLAdgaKRLRGAR 159
Cdd:PRK09369  81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAD---GRLKGAH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 240 GTFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQ 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 320 AEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:PRK09369 318 AEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLD 397
                        410       420
                 ....*....|....*....|
gi 653772739 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:PRK09369 398 RGYERIEEKLRALGADIERV 417
 
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: 759.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKvEFDGNGTVTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLAdgaKRLRGAR 159
Cdd:PRK09369  81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAD---GRLKGAH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 240 GTFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQ 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 320 AEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:PRK09369 318 AEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLD 397
                        410       420
                 ....*....|....*....|
gi 653772739 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:PRK09369 398 RGYERIEEKLRALGADIERV 417
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: 738.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladgAKRLRGAR 159
Cdd:COG0766   81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEAR----AGRLKGAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEA 239
Cdd:COG0766  157 IYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 240 GTFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:COG0766  237 GTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQ 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 320 AEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:COG0766  317 AEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHID 396
                        410       420
                 ....*....|....*....|
gi 653772739 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:COG0766  397 RGYENLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-412 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: 660.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  12 LSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHN-LTLDAATIHTPEASYDLVKT 90
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENtLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  91 MRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARIVTDMVTVTGT 170
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAK---AAGRLKGARIYLDFPSVGAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 171 ENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEAGTFLCAVAAAG 250
Cdd:cd01555  158 ENIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 251 GDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAIAEGSATVTET 329
Cdd:cd01555  238 GDITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITET 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 330 IFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLDRGYDRIEDKL 409
Cdd:cd01555  318 IFENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKL 397

                 ...
gi 653772739 410 SAV 412
Cdd:cd01555  398 RAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-418 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: 618.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739    1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHT 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   81 PEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARI 160
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYAS---AKGRLVGAHI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  161 VTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  241 TFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  320 AEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
                         410
                  ....*....|....*....
gi 653772739  400 RGYDRIEDKLSAVGAKIRR 418
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-409 5.40e-129

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 378.18  E-value: 5.40e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739    7 EGNGPLSGEIRVSG-AKNAALPIMCAALLTAEPLaLSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLT--LDAATIHTPEA 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGEST-ITNLLDSDDTLTMLEALRALGAEIIKLDDEKSvvIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   84 SYDLVKTMRASILVLGPLLARFGHAR--VSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIV 161
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  162 TDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTD-RLVIQGVEALHGAAHTVIADRIEAG 240
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  241 TFLCAVAAAGGDVTLRGVPPGIL---DAVLDKLREAGVTLTTGDD-WIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMM 315
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  316 LNAIAEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQ-LSGATVMAT-DLRASASLVIAGLIAQGETLVD 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 653772739  394 RIYHLDRGYDRIEDKL 409
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: 759.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKvEFDGNGTVTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLAdgaKRLRGAR 159
Cdd:PRK09369  81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAD---GRLKGAH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 240 GTFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQ 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 320 AEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:PRK09369 318 AEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLD 397
                        410       420
                 ....*....|....*....|
gi 653772739 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:PRK09369 398 RGYERIEEKLRALGADIERV 417
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: 738.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladgAKRLRGAR 159
Cdd:COG0766   81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEAR----AGRLKGAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEA 239
Cdd:COG0766  157 IYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 240 GTFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:COG0766  237 GTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQ 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 320 AEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:COG0766  317 AEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHID 396
                        410       420
                 ....*....|....*....|
gi 653772739 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:COG0766  397 RGYENLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-412 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: 660.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  12 LSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHN-LTLDAATIHTPEASYDLVKT 90
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENtLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  91 MRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARIVTDMVTVTGT 170
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAK---AAGRLKGARIYLDFPSVGAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 171 ENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEAGTFLCAVAAAG 250
Cdd:cd01555  158 ENIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 251 GDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAIAEGSATVTET 329
Cdd:cd01555  238 GDITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITET 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 330 IFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLDRGYDRIEDKL 409
Cdd:cd01555  318 IFENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKL 397

                 ...
gi 653772739 410 SAV 412
Cdd:cd01555  398 RAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-418 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: 618.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739    1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHT 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   81 PEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARI 160
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYAS---AKGRLVGAHI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  161 VTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  241 TFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  320 AEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
                         410
                  ....*....|....*....
gi 653772739  400 RGYDRIEDKLSAVGAKIRR 418
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIER 416
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-420 1.12e-174

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 494.37  E-value: 1.12e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHT 80
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  81 PEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladgAKRLRGARI 160
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLK----ADELKGAHI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 161 VTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEAG 240
Cdd:PRK12830 157 YLDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 241 TFLCAVAAAGGDVTLRGVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAIA 320
Cdd:PRK12830 237 TYMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 321 EGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLDR 400
Cdd:PRK12830 317 NGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDR 396
                        410       420
                 ....*....|....*....|
gi 653772739 401 GYDRIEDKLSAVGAKIRRIQ 420
Cdd:PRK12830 397 GYSNIIEKLKALGADIWREE 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-409 5.40e-129

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 378.18  E-value: 5.40e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739    7 EGNGPLSGEIRVSG-AKNAALPIMCAALLTAEPLaLSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLT--LDAATIHTPEA 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGEST-ITNLLDSDDTLTMLEALRALGAEIIKLDDEKSvvIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   84 SYDLVKTMRASILVLGPLLARFGHAR--VSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIV 161
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  162 TDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTD-RLVIQGVEALHGAAHTVIADRIEAG 240
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  241 TFLCAVAAAGGDVTLRGVPPGIL---DAVLDKLREAGVTLTTGDD-WIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMM 315
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  316 LNAIAEGSATVTETIFENRFMHVQELNRLGANIVIDGKTAVVTGVEQ-LSGATVMAT-DLRASASLVIAGLIAQGETLVD 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 653772739  394 RIYHLDRGYDRIEDKL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-412 4.44e-112

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: 334.96  E-value: 4.44e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  12 LSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDA---ATIHTPEASYDLV 88
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGvgmAGLKAPQNALNLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  89 KTMRASILVLGPLLARFGhaRVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIVTDMVTVT 168
Cdd:cd01554   81 NSGTAIRLISGVLAGADF--EVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 169 GTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGTDRLVIQGVEALHGAAHTVIADRIEAGTFLCAVAA 248
Cdd:cd01554  159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 249 AGGDVTLRGVPPG-ILDAVLDKLREAGVTLTTGDDWIRVQMtGRPKAVSFRTSEYPaFPTDMQAQFMMLNAIAEGSATVT 327
Cdd:cd01554  239 APGRLVLQNVGINeTRTGIIDVLRAMGAKIEIGEDTISVES-SDLKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 328 ETIF------ENRFMHVQELNRLGANIVIDGKTAVVTGVEQLSGATVMAT-DLRASASLVIAGLIAQGETLVDRIYHLDR 400
Cdd:cd01554  317 DAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAINT 396
                        410
                 ....*....|..
gi 653772739 401 GYDRIEDKLSAV 412
Cdd:cd01554  397 SYPSFFDDLESL 408
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-393 3.72e-32

5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439898  Cd Length: 421  Bit Score: 125.97  E-value: 3.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAK---NAALpiMCAALltAE-PLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLD- 74
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL--LLAAL--AEgESTIRNLLESDDTLATLEALRALGAEiEELDGGTLRVTg 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  75 -AATIHTPEASYDlVK----TMR--ASILVLGPLLARF-GHARvslpggcgIGARPVDQHIKGLQLMGAEIV-IEHGYie 145
Cdd:COG0128   77 vGGGLKEPDAVLD-CGnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMGRLLDPLRQLGARIEsRGGGY-- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 146 AKLADGAKRLRGARIVTDMVT----VTGtenLLMAAALADGETVLE-NAAREPEVT-DLA-NLLVKMGARIDGIGTDRLV 218
Cdd:COG0128  146 LPLTIRGGPLKGGEYEIPGSAssqfKSA---LLLAGPLAEGGLEITvTGELESKPYrDHTeRMLRAFGVEVEVEGYRRFT 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 219 IQGVEALHGAAHTVIADRIEAGTFLCAVAAAGGDVTLRGVPPGIL---DAVLDKLREAGVTLTTGDDWIRVQmTGRPKAV 295
Cdd:COG0128  223 VPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITVR-GSPLKGI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 296 SFRTSEYP-AFPTdmqaqFMMLNAIAEGsatvtETIFEN----RF--------MhVQELNRLGANIVIDGKTAVVTGVEQ 362
Cdd:COG0128  302 DIDLSDIPdEAPT-----LAVLAAFAEG-----TTRIRGaaelRVkesdriaaM-ATELRKLGADVEETEDGLIIEGGPK 370
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 653772739 363 LSGATV-------MATdlrasaSLVIAGLIAQGETLVD 393
Cdd:COG0128  371 LKGAEVdsygdhrIAM------AFAVAGLRAEGPVTID 402
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
235-412 4.68e-21

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: 90.80  E-value: 4.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 235 DRIEAGTFLCAVAAAGGDVTLRGVPPG--------ILDAVLDKLREA-GVTL---TTGDDWIRVQMtGRPKAVSFRTSEY 302
Cdd:cd01553    9 GGQILRSFLVLAAISGGPITVTGIRPDrakpgllrQHLTFLKALEKIcGATVeggELGSDRISFRP-GTVRGGDVRFAIG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 303 PA-FPTDMQAQFMMLNAIAEGSATVTETIF----------ENRFMHVQELNRLGANIVI------------DGKTAVVTG 359
Cdd:cd01553   88 SAgSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEEtllrhgfypaggGVVATEVSP 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 653772739 360 VEQLSGAtvmatDLRASASLVIAGliaqGETLVDRIYHLDRGYDRIEDKLSAV 412
Cdd:cd01553  168 VEKLNTA-----QLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-397 2.12e-19

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: 89.54  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  12 LSGEIRVSGAK---NAALpiMCAALLTAEplalSNVPNL---QDVRTMLKLLRQMGVEgvLDGHNLTLdaaTIHTPEASY 85
Cdd:cd01556    1 LSGEITVPGSKsisHRAL--LLAALAEGE----SRIENLldsDDTLATLEALRALGAK--IEEEGGTV---EIVGGGGLG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  86 DLVK----------TMRasiLVLGPLLARFGHARVSlpGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKrL 155
Cdd:cd01556   70 LPPEavldcgnsgtTMR---LLTGLLALQGGDSVLT--GDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGG-L 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 156 RGARIVTDMVT----VTGtenLLMAAALADGETVLENAAREPEVT-DL-ANLLVKMGARIDGIGTDRLVIQGVEALHGAA 229
Cdd:cd01556  144 KGGEVEIPGAVssqfKSA---LLLAAPLAEGPTTIIIGELESKPYiDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 230 HTVIADRIEAGTFLCAVAAAGGDVTLRGVPPGILD-AVLDKLREAGVTLTTGD-DWIRVQMTGRPKAVSFRTSEYP-AFP 306
Cdd:cd01556  221 YTVEGDASSAAFFLAAAAITGSEIVIKNVGLNSGDtGIIDVLKEMGADIEIGNeDTVVVESGGKLKGIDIDGNDIPdEAP 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 307 TdmqaqFMMLNAIAEGSATVT--------ETifeNRF--MhVQELNRLGANI-------VIDGKTAVVTGVEQLSGatvm 369
Cdd:cd01556  301 T-----LAVLAAFAEGPTRIRnaaelrvkES---DRIaaM-ATELRKLGADVeetedglIIEGGPLKGAGVEVYTY---- 367
                        410       420
                 ....*....|....*....|....*...
gi 653772739 370 aTDLRASASLVIAGLIAQGETLVDRIYH 397
Cdd:cd01556  368 -GDHRIAMSFAIAGLVAEGGVTIEDPEC 394
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-395 1.44e-13

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 72.10  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAK---NAALpiMCAALLTAEplalSNVPNL---QDVRTMLKLLRQMGVEgvLDGHNLTLD 74
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL--LLAALAEGE----TTITNLlrsEDTLATLNALRALGVE--IEDDEVVVE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  75 AATIHTPEASYDLVK------TMR--ASILVLGPLLARF-GHARvslpggcgIGARPVDQHIKGLQLMGAEIV-IEHGYI 144
Cdd:PRK02427  74 GVGGGGLKEPEDVLDcgnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMGRLLDPLRQMGAKIEgRDEGYL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 145 EAKLaDGAKRLRGARIVTDMVT--VTGtenLLMAAAL-ADGETVLEnaAREPEV----TDL-ANLLVKMGARIDGIGTD- 215
Cdd:PRK02427 146 PLTI-RGGKKGGPIEYDGPVSSqfVKS---LLLLAPLfAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVENVEGWg 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 216 --RLVIQGVEALHGAAHTVIADRIEAGTFLCAVAAAGG-DVTLRGVP-----PGilDAVLDKLREAGVTLTTGDDW---- 283
Cdd:PRK02427 220 yrRIVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNVGlnstqGG--KAIIDVLEKMGADIEIENERegge 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 284 ----IRVQmTGRPKAVSFRTSEYP-AFPTdmqaqFMMLNAIAEGsatvtETIFEN----RF--------MhVQELNRLGA 346
Cdd:PRK02427 298 pvgdIRVR-SSELKGIDIDIPDIIdEAPT-----LAVLAAFAEG-----TTVIRNaeelRVketdriaaM-ATELRKLGA 365
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 653772739 347 NIVIDGKTAVVTGVEqlSGATV-------MATdlrasaSLVIAGLIAQGETLVDRI 395
Cdd:PRK02427 366 EVEETEDGLIITGGP--LAGVVdsygdhrIAM------AFAIAGLAAEGPVTIDDP 413
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
174-419 6.10e-13

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: 69.89  E-value: 6.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 174 LMAAALADGETVLENAAREPEVTDLANLLVKMGARIDGIGtDRLVIQGVEALHGAAHTVIaDRIEAGT---FLCAVAA-A 249
Cdd:cd01556   18 LLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG-GTVEIVGGGGLGLPPEAVL-DCGNSGTtmrLLTGLLAlQ 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 250 GGDVTLRGVP-----PgiLDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTsEYPAfptDMQAQF----MMLNAIA 320
Cdd:cd01556   96 GGDSVLTGDEslrkrP--MGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEV-EIPG---AVSSQFksalLLAAPLA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 321 EGSATVTETIFEN---RFMHVQELNRLGANI-VIDGKTAVVTGVEQLSGA--TVMAtDLRASASLVIAGLIAQGETLVdR 394
Cdd:cd01556  170 EGPTTIIIGELESkpyIDHTERMLRAFGAEVeVDGYRTITVKGGQKYKGPeyTVEG-DASSAAFFLAAAAITGSEIVI-K 247
                        250       260
                 ....*....|....*....|....*
gi 653772739 395 IYHLDRGYDRIEDKLSAVGAKIRRI 419
Cdd:cd01556  248 NVGLNSGDTGIIDVLKEMGADIEIG 272
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
174-419 2.24e-10

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 62.08  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 174 LMAAALADGETVLENAAREPEVTDLANLLVKMGARIDgigTDRLVIQGVEALHGAAHTVIADRIEAGT---FLCAVAA-A 249
Cdd:PRK02427  30 LLLAALAEGETTITNLLRSEDTLATLNALRALGVEIE---DDEVVVEGVGGGGLKEPEDVLDCGNSGTtmrLLTGLLAlQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 250 GGDVTLRGVP-----PgiLDAVLDKLREAGVTLTTGDDW---IRVQMTGRPKAVSFRTSEYPAFPTDMqaqfMM---LNA 318
Cdd:PRK02427 107 PGEVVLTGDEslrkrP--MGRLLDPLRQMGAKIEGRDEGylpLTIRGGKKGGPIEYDGPVSSQFVKSL----LLlapLFA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 319 IAEGSATVTETI-----FEnrfMHVQELNRLGANIVIDGKTAVVTGVEQlSGATVMATDLR-----ASAS-LVIAGLIAQ 387
Cdd:PRK02427 181 EGDTETTVIEPLpsrphTE---ITLRMLRAFGVEVENVEGWGYRRIVIK-GGQRLRGQDITvpgdpSSAAfFLAAAAITG 256
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 653772739 388 GETLvdRIYHLD----RGYDRIEDKLSAVGAKIRRI 419
Cdd:PRK02427 257 GSEV--TITNVGlnstQGGKAIIDVLEKMGADIEIE 290
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
10-290 1.10e-07

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 53.94  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  10 GPLS---GEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHTPEASYD 86
Cdd:PRK11861 246 GPFShaqGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAFTAKTAD 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  87 L--------VKTMRASILVLGpllarfGHARVSlpGGCGIGARPVDQHIKGLQLMGAEIVIE--HGYIEAKLADGAKRLR 156
Cdd:PRK11861 326 LflgnagtaVRPLTAALAVNG------GEYRIH--GVPRMHERPIGDLVDGLRQIGARIDYEgnEGFPPLRIRPATISVD 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 157 GARIVTDMVTVTGTENLLMAAALA---DGETVLE---NAAREPEVTDLANLLVKMGARIDGIGTDRLVI-QGVEALHGAA 229
Cdd:PRK11861 398 APIRVRGDVSSQFLTALLMTLPLVkakDGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVpAGVRYRSPGT 477
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653772739 230 HTVIADRIEAGTFLCAVAAAGGDVTLRGVPPGILD---AVLDKLREAGVTLTTGDDWIRVQMTG 290
Cdd:PRK11861 478 IMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQgdvGFANALMQMGANVTMGDDWIEVRGIG 541
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
10-278 1.91e-05

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 46.91  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  10 GPLSGEIRVSGAKNAA-LPIMCAALltAEPLA-LSNVPNLQDVRTMLKLLRQMGV--EGVLDGHnLTLDAATIH--TPEA 83
Cdd:PRK14806 310 GAVKGTIRVPGDKSIShRSIMLGSL--AEGVTeVEGFLEGEDALATLQAFRDMGVviEGPHNGR-VTIHGVGLHglKAPP 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  84 SYDLVKTMRASILVLGPLLArfGHA-RVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIVT 162
Cdd:PRK14806 387 GPLYMGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIETGEEGRPPLSIRGGQRLKGIHYDL 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 163 DMVTVTGTENLLMAAALADGETvlenAAREPEVT--DLANLLVKMGARIDGIGtDRLVIQGVEALHGAAHTVIADRIEAG 240
Cdd:PRK14806 465 PMASAQVKSCLLLAGLYAEGET----SVTEPAPTrdHTERMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPADISSAA 539
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 653772739 241 TFLCAVA-AAGGDVTLRGVppGI---LDAVLDKLREAGVTLT 278
Cdd:PRK14806 540 FFLVAASiAEGSELTLEHV--GInptRTGVIDILKLMGADIT 579
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
174-418 2.36e-05

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: 46.11  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  174 LMAAALADGETVLENAAREPEVTDLANLLVKMGARIdGIGTDRLVIQGVEALHGAAHTVIAdriEAGT---FLCAVAAA- 249
Cdd:TIGR01356  16 LILAALAEGETRVRNLLRSEDTLATLDALRALGAKI-EDGGEVAVIEGVGGKEPQAELDLG---NSGTtarLLTGVLALa 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  250 GGDVTLRGVP-----PgiLDAVLDKLREAGVTL--TTGDDWIRVQMTGRPKAVSFRTSeypafpTDMQAQF---MMLNAI 319
Cdd:TIGR01356  92 DGEVVLTGDEslrkrP--MGRLVDALRQLGAEIssLEGGGSLPLTISGPLPGGIVYIS------GSASSQYksaLLLAAP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  320 AEGSATVTETIFENR-----FMHVQELNRLGANIVI-DGKTAVVTGVEQLSGATV-MATDLRASASLVIAGLIAQGETlv 392
Cdd:TIGR01356 164 ALQAVGITIVGEPLKsrpyiEITLDLLGSFGVEVERsDGRKIVVPGGQKYGPQGYdVPGDYSSAAFFLAAAAITGGRV-- 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 653772739  393 dRIYHL----DRGYDRIEDKLSAVGAKIRR 418
Cdd:TIGR01356 242 -TLENLginpTQGDKAIIIVLEEMGADIEV 270
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
1-257 6.57e-04

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 41.66  E-value: 6.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739   1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTldaATIHT 80
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNR---AVVEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739  81 PEASYDLVKTMRASI-LVLG-------PLLARF----GHARVSLPGGCGIGARPVDQHIKGLQLMGAEI--VIEHGYIEA 146
Cdd:PLN02338  78 CGGKFPVSGDSKEDVeLFLGnagtamrPLTAAVtaagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVecTLGTNCPPV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 147 KLaDGAKRLRGARI-VTDMVTVTGTENLLMAAALADGE---TVLENAAREPEVTDLANLLVKMGARIDGIGT-DRLVIQG 221
Cdd:PLN02338 158 RV-NAAGGLPGGKVkLSGSISSQYLTALLMAAPLALGDveiEIVDKLISVPYVEMTLKLMERFGVSVEHSDSwDRFFIKG 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 653772739 222 VEALH--GAAHtVIADRIEAGTFLCAVAAAGGDVTLRG 257
Cdd:PLN02338 237 GQKYKspGNAY-VEGDASSASYFLAGAAITGGTVTVEG 273
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
130-258 5.57e-03

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 39.21  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653772739 130 LQLMGAEIVIEH-----GYIEAKLADGAKRLRGARIVTDMVTVTGTE--NLLMAAALADGETVLENAarepevtdlANLL 202
Cdd:PRK14806 571 LKLMGADITLENerevgGEPVADIRVRGARLKGIDIPEDQVPLAIDEfpVLFVAAACAEGRTVLTGA---------EELR 641
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653772739 203 VKMGARI----DGIGT---------DRLVIQGVEALHGAAHTVIADRIeAGTFLCAVAAAGGDVTLRGV 258
Cdd:PRK14806 642 VKESDRIqvmaDGLKTlgidceptpDGIIIEGGIFGGGEVESHGDHRI-AMSFSVASLRASGPITIHDC 709
 
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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