NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1823152548|gb|QIP12866|]
View 

UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Spirosoma aureum]

Protein Classification

UDP-N-acetylglucosamine 1-carboxyvinyltransferase( domain architecture ID 12380807)

UDP-N-acetylglucosamine 1-carboxyvinyltransferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan

CATH:  3.65.10.10
EC:  2.5.1.7
Gene Ontology:  GO:0008760|GO:0019277|GO:0009252|GO:0008360|GO:0007049|GO:0051301|GO:0071555
SCOP:  4001425

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 1-434 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: 586.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYRFVASDVN 80
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLTIDASNIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 LDYLESDTYKRkaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDandGGYYQVDASNLR 160
Cdd:COG0766    81 STEAPYELVRK----MRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIE---HGYIEARAGRLK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 161 GTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDM 240
Cdd:COG0766   154 GARIYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 241 IEIGSFIGLAAMTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDIFIPAQERYQIetfldggmMTVADSPWPGFTPD 320
Cdd:COG0766   234 IEAGTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKA--------VDIKTAPYPGFPTD 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 321 LLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIILcDPHRATVVGLNRqlpLKGIRMSSPDIRAGVALLIAAM 400
Cdd:COG0766   306 LQAQFMALLTQAEGTSVITETVFENRFMHVDELNRMGADIKL-DGHTAIVRGVTK---LSGAPVMATDLRAGAALVLAGL 381

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1823152548 401 SAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIR 434
Cdd:COG0766   382 AAEGETVIDNIYHIDRGYENLEEKLRALGADIER 415
 
Name Accession Description Interval E-value
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 1-434 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: 586.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYRFVASDVN 80
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLTIDASNIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 LDYLESDTYKRkaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDandGGYYQVDASNLR 160
Cdd:COG0766    81 STEAPYELVRK----MRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIE---HGYIEARAGRLK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 161 GTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDM 240
Cdd:COG0766   154 GARIYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 241 IEIGSFIGLAAMTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDIFIPAQERYQIetfldggmMTVADSPWPGFTPD 320
Cdd:COG0766   234 IEAGTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKA--------VDIKTAPYPGFPTD 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 321 LLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIILcDPHRATVVGLNRqlpLKGIRMSSPDIRAGVALLIAAM 400
Cdd:COG0766   306 LQAQFMALLTQAEGTSVITETVFENRFMHVDELNRMGADIKL-DGHTAIVRGVTK---LSGAPVMATDLRAGAALVLAGL 381

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1823152548 401 SAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIR 434
Cdd:COG0766   382 AAEGETVIDNIYHIDRGYENLEEKLRALGADIER 415
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
 1-435 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 582.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYRFVASDVN 80
Cdd:PRK09369    1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTVTIDASNIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 LDYLESDTYKRkaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDandGGYYQVDASN-L 159
Cdd:PRK09369   81 NTEAPYELVKK----MRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIE---HGYVEAKADGrL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 160 RGTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPD 239
Cdd:PRK09369  154 KGAHIVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 240 MIEIGSFIGLAAMTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDIFIPAQERyqietfldGGMMTVADSPWPGFTP 319
Cdd:PRK09369  234 RIEAGTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGR--------LKAVDIKTAPYPGFPT 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 320 DLLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIIlCDPHRATVVGLNRqlpLKGIRMSSPDIRAGVALLIAA 399
Cdd:PRK09369  306 DMQAQFMALLTQAEGTSVITETIFENRFMHVPELIRMGADIE-VDGHTAVVRGVEK---LSGAPVMATDLRASASLVLAG 381

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1823152548 400 MSAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIRL 435
Cdd:PRK09369  382 LVAEGTTIVDRIYHLDRGYERIEEKLRALGADIERV 417
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
 12-428 1.11e-170

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: 484.28  E-value: 1.11e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  12 LKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYRFVASDVNLDYLESDTYKR 91
Cdd:cd01555     1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINSTEAPYELVRK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  92 kaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDanDGGYYQVDASNLRGTYMLLDEASV 171
Cdd:cd01555    81 ----MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIE--DGYVEAKAAGRLKGARIYLDFPSV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 172 TGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDMIEIGSFIGLAA 251
Cdd:cd01555   155 GATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 252 MTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDIFIPAQERyqietflDGGMMTVADSPWPGFTPDLLSIVLVTAVQ 331
Cdd:cd01555   235 ITGGDITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGG-------RLKAVDIETAPYPGFPTDLQAQFMALLTQ 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 332 AQGTLLIHQKMFESRLFFVDKLIDMGAQIILCDPHrATVVGLNRqlpLKGIRMSSPDIRAGVALLIAAMSAQGTSIIDNI 411
Cdd:cd01555   308 AEGTSVITETIFENRFMHVDELNRMGADIKVEGNT-AIIRGVTK---LSGAPVMATDLRAGAALVLAGLAAEGETIISNI 383

                         410
                  ....*....|....*..
gi 1823152548 412 EQIDRGYQHIDTRLNAI 428
Cdd:cd01555   384 YHIDRGYERIEEKLRAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
 1-434 6.25e-153

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: 439.74  E-value: 6.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGeNSYRFVASDVN 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDN-NTLEINTPNIN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 ---LDYlesdTYKRKaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNydaNDGGYYQVDAS 157
Cdd:TIGR01072  80 steAPY----ELVRK---MRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIV---IEDGYVYASAK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 158 N-LRGTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTM 236
Cdd:TIGR01072 150 GrLVGAHIVLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 237 LPDMIEIGSFIGLAAMTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDI-FIPAQERyqietfldGGMMTVADSPWP 315
Cdd:TIGR01072 230 IPDRIEAGTFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIrVDMRQKR--------LKAVDIETLPYP 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 316 GFTPDLLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIILCdPHRATVVGLNrqlPLKGIRMSSPDIRAGVAL 395
Cdd:TIGR01072 302 GFPTDLQAQFMALLSQAEGTSVITETVFENRFMHVDELIRMGANIKLE-GNTAVIHGVE---QLSGAEVMATDLRAGAAL 377

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1823152548 396 LIAAMSAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIR 434
Cdd:TIGR01072 378 VLAGLVAEGETIVHNVYHLDRGYEDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-421 2.49e-56

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 191.36  E-value: 2.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   7 TGGRKLKGEL-IPQGAKNEALQILCAVLLTkEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKI-GENSYRFVASDVNLdYL 84
Cdd:pfam00275   1 TGGSRLSGEVkIPGSKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLdDEKSVVIVEGLGGS-FE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  85 ESDTYKRKaaaLRGSVMLLGPMLARFKKGRIPR--PGGDKIGRRRLDTHFLGFEKLGAQFNYDANDGGY-YQVDASNLRG 161
Cdd:pfam00275  79 APEDLVLD---MGNSGTALRPLTGRLALQSGEVvlPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYApLKVRGLRLGG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 162 TYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGS-NLLTIEGVSELQGTEHTMLPDM 240
Cdd:pfam00275 156 IHIDGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGEKLPGQEYRVEGDR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 241 IEIGSFIGLAAMTQSEITIKNCRIPEL---GIIPDQFRRLGIQVDFRGDDIFIpaqeryQIETFLDGGMMTVADSPWPGF 317
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIV------VGPPGLRGKAVDIRTAPDPAP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 318 TPDLLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIilcdphRATVVGLNRQLPLKGIR----MSSPDIRAGV 393
Cdd:pfam00275 310 TTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADV------EELPDGLIIIPAVKELKgaevDSYGDHRIAM 383

                         410       420
                  ....*....|....*....|....*...
gi 1823152548 394 ALLIAAMSAQGTSIIDNIEQIDRGYQHI 421
Cdd:pfam00275 384 ALALAGLVAEGETIIDDIECTDRSFPDF 411
 
Name Accession Description Interval E-value
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 1-434 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: 586.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYRFVASDVN 80
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLTIDASNIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 LDYLESDTYKRkaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDandGGYYQVDASNLR 160
Cdd:COG0766    81 STEAPYELVRK----MRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIE---HGYIEARAGRLK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 161 GTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDM 240
Cdd:COG0766   154 GARIYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 241 IEIGSFIGLAAMTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDIFIPAQERYQIetfldggmMTVADSPWPGFTPD 320
Cdd:COG0766   234 IEAGTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKA--------VDIKTAPYPGFPTD 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 321 LLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIILcDPHRATVVGLNRqlpLKGIRMSSPDIRAGVALLIAAM 400
Cdd:COG0766   306 LQAQFMALLTQAEGTSVITETVFENRFMHVDELNRMGADIKL-DGHTAIVRGVTK---LSGAPVMATDLRAGAALVLAGL 381

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1823152548 401 SAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIR 434
Cdd:COG0766   382 AAEGETVIDNIYHIDRGYENLEEKLRALGADIER 415
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
 1-435 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 582.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYRFVASDVN 80
Cdd:PRK09369    1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTVTIDASNIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 LDYLESDTYKRkaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDandGGYYQVDASN-L 159
Cdd:PRK09369   81 NTEAPYELVKK----MRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIE---HGYVEAKADGrL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 160 RGTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPD 239
Cdd:PRK09369  154 KGAHIVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 240 MIEIGSFIGLAAMTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDIFIPAQERyqietfldGGMMTVADSPWPGFTP 319
Cdd:PRK09369  234 RIEAGTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGR--------LKAVDIKTAPYPGFPT 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 320 DLLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIIlCDPHRATVVGLNRqlpLKGIRMSSPDIRAGVALLIAA 399
Cdd:PRK09369  306 DMQAQFMALLTQAEGTSVITETIFENRFMHVPELIRMGADIE-VDGHTAVVRGVEK---LSGAPVMATDLRASASLVLAG 381

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1823152548 400 MSAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIRL 435
Cdd:PRK09369  382 LVAEGTTIVDRIYHLDRGYERIEEKLRALGADIERV 417
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
 12-428 1.11e-170

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: 484.28  E-value: 1.11e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  12 LKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYRFVASDVNLDYLESDTYKR 91
Cdd:cd01555     1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINSTEAPYELVRK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  92 kaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDanDGGYYQVDASNLRGTYMLLDEASV 171
Cdd:cd01555    81 ----MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIE--DGYVEAKAAGRLKGARIYLDFPSV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 172 TGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDMIEIGSFIGLAA 251
Cdd:cd01555   155 GATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 252 MTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDIFIPAQERyqietflDGGMMTVADSPWPGFTPDLLSIVLVTAVQ 331
Cdd:cd01555   235 ITGGDITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGG-------RLKAVDIETAPYPGFPTDLQAQFMALLTQ 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 332 AQGTLLIHQKMFESRLFFVDKLIDMGAQIILCDPHrATVVGLNRqlpLKGIRMSSPDIRAGVALLIAAMSAQGTSIIDNI 411
Cdd:cd01555   308 AEGTSVITETIFENRFMHVDELNRMGADIKVEGNT-AIIRGVTK---LSGAPVMATDLRAGAALVLAGLAAEGETIISNI 383

                         410
                  ....*....|....*..
gi 1823152548 412 EQIDRGYQHIDTRLNAI 428
Cdd:cd01555   384 YHIDRGYERIEEKLRAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
 1-434 6.25e-153

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: 439.74  E-value: 6.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGeNSYRFVASDVN 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDN-NTLEINTPNIN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 ---LDYlesdTYKRKaaaLRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNydaNDGGYYQVDAS 157
Cdd:TIGR01072  80 steAPY----ELVRK---MRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIV---IEDGYVYASAK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 158 N-LRGTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTM 236
Cdd:TIGR01072 150 GrLVGAHIVLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 237 LPDMIEIGSFIGLAAMTQSEITIKNCRIPELGIIPDQFRRLGIQVDFRGDDI-FIPAQERyqietfldGGMMTVADSPWP 315
Cdd:TIGR01072 230 IPDRIEAGTFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIrVDMRQKR--------LKAVDIETLPYP 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 316 GFTPDLLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIILCdPHRATVVGLNrqlPLKGIRMSSPDIRAGVAL 395
Cdd:TIGR01072 302 GFPTDLQAQFMALLSQAEGTSVITETVFENRFMHVDELIRMGANIKLE-GNTAVIHGVE---QLSGAEVMATDLRAGAAL 377

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1823152548 396 LIAAMSAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIR 434
Cdd:TIGR01072 378 VLAGLVAEGETIVHNVYHLDRGYEDLEEKLRALGAKIER 416
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
 1-434 4.83e-101

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 307.17  E-value: 4.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKiGENSYRFVASDVN 80
Cdd:PRK12830    1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKR-DGDTLEIDPTGIQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  81 LDYLESDtykrKAAALRGSVMLLGPMLARFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNydaNDGGYYQVDASNLR 160
Cdd:PRK12830   80 SMPLPNG----KVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVT---NEGGAIYLKADELK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 161 GTYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDM 240
Cdd:PRK12830  153 GAHIYLDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 241 IEIGSFIGLAAMTQSEITIKNCrIPE-LGIIPDQFRRLGIQVDFRGDDIFIPAQERYQietfldggMMTVADSPWPGFTP 319
Cdd:PRK12830  233 IEAGTYMILAAACGGGVTINNV-IPEhLESFIAKLEEMGVRVEVNEDSIFVEKQGNLK--------AVDIKTLPYPGFAT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 320 DLLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIILcDPHRATVVGLNRqlpLKGIRMSSPDIRAGVALLIAA 399
Cdd:PRK12830  304 DLQQPLTPLLLKANGRSVVTDTIYEKRFKHVDELKRMGANIKV-EGRSAIITGPSK---LTGAKVKATDLRAGAALVIAG 379

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1823152548 400 MSAQGTSIIDNIEQIDRGYQHIDTRLNAIGAEIIR 434
Cdd:PRK12830  380 LMAEGVTEITNIEHIDRGYSNIIEKLKALGADIWR 414
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-421 2.49e-56

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 191.36  E-value: 2.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   7 TGGRKLKGEL-IPQGAKNEALQILCAVLLTkEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKI-GENSYRFVASDVNLdYL 84
Cdd:pfam00275   1 TGGSRLSGEVkIPGSKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLdDEKSVVIVEGLGGS-FE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  85 ESDTYKRKaaaLRGSVMLLGPMLARFKKGRIPR--PGGDKIGRRRLDTHFLGFEKLGAQFNYDANDGGY-YQVDASNLRG 161
Cdd:pfam00275  79 APEDLVLD---MGNSGTALRPLTGRLALQSGEVvlPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYApLKVRGLRLGG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 162 TYMLLDEASVTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGS-NLLTIEGVSELQGTEHTMLPDM 240
Cdd:pfam00275 156 IHIDGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTeLSITVKGGEKLPGQEYRVEGDR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 241 IEIGSFIGLAAMTQSEITIKNCRIPEL---GIIPDQFRRLGIQVDFRGDDIFIpaqeryQIETFLDGGMMTVADSPWPGF 317
Cdd:pfam00275 236 SSAAYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIV------VGPPGLRGKAVDIRTAPDPAP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 318 TPDLLSIVLVTAVQAQGTLLIHQKMFESRLFFVDKLIDMGAQIilcdphRATVVGLNRQLPLKGIR----MSSPDIRAGV 393
Cdd:pfam00275 310 TTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADV------EELPDGLIIIPAVKELKgaevDSYGDHRIAM 383

                         410       420
                  ....*....|....*....|....*...
gi 1823152548 394 ALLIAAMSAQGTSIIDNIEQIDRGYQHI 421
Cdd:pfam00275 384 ALALAGLVAEGETIIDDIECTDRSFPDF 411
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
 12-428 1.08e-47

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: 168.55  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  12 LKGELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKiGENSYRFVASDVNLDYLESDTYKR 91
Cdd:cd01554     1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIED-KDGVITIQGVGMAGLKAPQNALNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  92 kAAALRGSVMLLGPMLARfkKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNY-DANDGGYYQVDASNLRGTYMLLDEAS 170
Cdd:cd01554    80 -GNSGTAIRLISGVLAGA--DFEVELFGDDSLSKRPMDRVTLPLKKMGASISGqEERDLPPLLKGGKNLGPIHYEDPIAS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 171 VTGTANVLMAAVMAEGTTTIYNAACEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDMIEIGSFIGLA 250
Cdd:cd01554   157 AQVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 251 AMTQSEITIKNCRIPELGI-IPDQFRRLGIQVDFrGDDIFIPAQERyqietfLDGGMMTVADSPWPgftPDLLSIVLVTA 329
Cdd:cd01554   237 AIAPGRLVLQNVGINETRTgIIDVLRAMGAKIEI-GEDTISVESSD------LKATEICGALIPRL---IDELPIIALLA 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 330 VQAQGTLLIHQ------KMFESRLFFVDKLIDMGAQI------ILCDPHRAtvvglnrqlpLKGIR-MSSPDIRAGVALL 396
Cdd:cd01554   307 LQAQGTTVIKDaeelkvKETDRIFVVADELNSMGADIeptadgMIIKGKEK----------LHGARvNTFGDHRIGMMTA 376

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1823152548 397 IAAMSAQGTSIIDNIEQIDRGYQHIDTRLNAI 428
Cdd:cd01554   377 LAALVADGEVELDRAEAINTSYPSFFDDLESL 408
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 12-412 1.32e-15

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: 77.98  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  12 LKGELIPQGAK---NEALqiLCAvLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGE------NSYRFVASDVNLD 82
Cdd:cd01556     1 LSGEITVPGSKsisHRAL--LLA-ALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGtveivgGGGLGLPPEAVLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  83 YLESDTykrkaaALRgsvmLLGPMLArFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDANDGGYYQVDASNLRGT 162
Cdd:cd01556    78 CGNSGT------TMR----LLTGLLA-LQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 163 YMLLD-EAS---VTGtanVLMAAVMAEGTTTIYNAACE--PYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTM 236
Cdd:cd01556   147 EVEIPgAVSsqfKSA---LLLAAPLAEGPTTIIIGELEskPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTV 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 237 LPDmieIGS---FIGLAAMTQSEITIKNCRIPELGI-IPDQFRRLGIQVDF-RGDDIFIPAQEryqietFLDGGMMTVAD 311
Cdd:cd01556   224 EGD---ASSaafFLAAAAITGSEIVIKNVGLNSGDTgIIDVLKEMGADIEIgNEDTVVVESGG------KLKGIDIDGND 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 312 spwpgfTPDLLSIVLVTAVQAQGTLLI----HQKMFES-RLF-FVDKLIDMGAQiilCDPHRATVVGLNRQLPLKGIRMS 385
Cdd:cd01556   295 ------IPDEAPTLAVLAAFAEGPTRIrnaaELRVKESdRIAaMATELRKLGAD---VEETEDGLIIEGGPLKGAGVEVY 365

                         410       420
                  ....*....|....*....|....*...
gi 1823152548 386 SP-DIRAGVALLIAAMSAQGTSIIDNIE 412
Cdd:cd01556   366 TYgDHRIAMSFAIAGLVAEGGVTIEDPE 393
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 1-412 8.93e-15

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: 75.51  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAK---NEALqILCAvlLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGENSYR---- 73
Cdd:COG0128     1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL-LLAA--LAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRvtgv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  74 ---FVASDVNLDYLESdtykrkaaalrGSVM-LLGPMLArfkkgriPRPG-----GDK-IGRRRLDTHFLGFEKLGAQFN 143
Cdd:COG0128    78 gggLKEPDAVLDCGNS-----------GTTMrLLTGLLA-------LQPGevvltGDEsLRKRPMGRLLDPLRQLGARIE 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 144 YDanDGGY--YQVDASNLRG-TYMLLDEAS---VTGtanVLMAAVMAE-GTTTIYNAACE--PYLQQLSKMLNSMGAKIS 214
Cdd:COG0128   140 SR--GGGYlpLTIRGGPLKGgEYEIPGSASsqfKSA---LLLAGPLAEgGLEITVTGELEskPYRDHTERMLRAFGVEVE 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 215 GVGSNLLTIEGVSELQGTEHTMLPDmieIGS---FIGLAAMTQSEITIKNCRIPEL----GIIpDQFRRLGIQVDFRGDD 287
Cdd:COG0128   215 VEGYRRFTVPGGQRYRPGDYTVPGD---ISSaafFLAAAAITGSEVTVEGVGLNSTqgdtGIL-DILKEMGADIEIENDG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 288 IFIPAQEryqietfLDGGMMTVADspwpgfTPDLLSIVLVTAVQAQGTLLI----HQKMFES-RLF-FVDKLIDMGAQII 361
Cdd:COG0128   291 ITVRGSP-------LKGIDIDLSD------IPDEAPTLAVLAAFAEGTTRIrgaaELRVKESdRIAaMATELRKLGADVE 357

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1823152548 362 LcDPHRATVVGLNrqlPLKGIRMSS-PDIRAGVALLIAAMSAQGTSIIDNIE 412
Cdd:COG0128   358 E-TEDGLIIEGGP---KLKGAEVDSyGDHRIAMAFAVAGLRAEGPVTIDDAE 405
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 14-431 3.38e-10

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: 61.52  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  14 GELIPQGAKNEALQILCAVLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVWVTKIGE----NSYRFVASDVNLDYLESDTY 89
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEvaviEGVGGKEPQAELDLGNSGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  90 KR----KAAALRGSVMLLGPmlARFKKgripRPGGDKIGrrrldthflGFEKLGAQFNYDANDGGYYQVDASNLRG--TY 163
Cdd:TIGR01356  81 ARlltgVLALADGEVVLTGD--ESLRK----RPMGRLVD---------ALRQLGAEISSLEGGGSLPLTISGPLPGgiVY 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 164 MLLDEASVTGTANVLMAAVMAEGTTTIYNAA--CEPYLQQLSKMLNSMGAKISGVGSNLLTIEGVSELQGTEHTMLPDMI 241
Cdd:TIGR01356 146 ISGSASSQYKSALLLAAPALQAVGITIVGEPlkSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYS 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 242 EIGSFIGLAAMTQSEITIKNCRI----PELGIIpDQFRRLGIQVDFRGDDIFIpaqeryqieTFLDGGMMTVADSPwpgF 317
Cdd:TIGR01356 226 SAAFFLAAAAITGGRVTLENLGInptqGDKAII-IVLEEMGADIEVEEDDLIV---------EGASGLKGIKIDMD---D 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 318 TPDLLSIVLVTAVQAQGTLLI----HQKMFES-RL-FFVDKLIDMGAQiilCDPhRA---TVVGLNRqlpLKGIRMSS-P 387
Cdd:TIGR01356 293 MIDELPTLAVLAAFAEGVTRItgaeELRVKESdRIaAIAEELRKLGVD---VEE-FEdglYIRGKKE---LKGAVVDTfG 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1823152548 388 DIRAGVALLIAAMSAQGTSIIDNIEQIDRGYQHIDTRLNAIGAE 431
Cdd:TIGR01356 366 DHRIAMAFAVAGLVAEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 206-432 1.17e-04

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 44.36  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 206 LNSMGAKISGVGSNL--LTIEGVSELQGTEHTMlpdmiEIGS-FI-------GLAAMTQSEITIKNcRIPELG---IIPD 272
Cdd:PRK02427  130 LRQMGAKIEGRDEGYlpLTIRGGKKGGPIEYDG-----PVSSqFVksllllaPLFAEGDTETTVIE-PLPSRPhteITLR 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 273 QFRRLGIQVDFRGDD----IFIPAQERYQietfldGGMMTVadspwPGftpDLLSIV--LVTAVQAQG-TLLIHQKMFES 345
Cdd:PRK02427  204 MLRAFGVEVENVEGWgyrrIVIKGGQRLR------GQDITV-----PG---DPSSAAffLAAAAITGGsEVTITNVGLNS 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 346 R---LFFVDKLIDMGAQIILCDPHRATVVGLN---RQLPLKGIRMSSPD-IRAGVALLIAAMSAQGTSIIDNIEQI---- 414
Cdd:PRK02427  270 TqggKAIIDVLEKMGADIEIENEREGGEPVGDirvRSSELKGIDIDIPDiIDEAPTLAVLAAFAEGTTVIRNAEELrvke 349

                         250       260
                  ....*....|....*....|..
gi 1823152548 415 -DRgyqhID---TRLNAIGAEI 432
Cdd:PRK02427  350 tDR----IAamaTELRKLGAEV 367
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 1-335 5.78e-04

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 42.05  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548   1 MASFQITGGRKLKGELIPQGAK---NEALqiLCAvLLTKEPVTIHNIPNIRDVNQLIDLLGDLGVwvtKIGENSYRFVAS 77
Cdd:PRK02427    2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL--LLA-ALAEGETTITNLLRSEDTLATLNALRALGV---EIEDDEVVVEGV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548  78 DVnldylesDTYKRKAAAL----RGSVM-LLGPMLArFKKGRIPRPGGDKIGRRRLDTHFLGFEKLGAQFNYDAND---- 148
Cdd:PRK02427   76 GG-------GGLKEPEDVLdcgnSGTTMrLLTGLLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGylpl 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 149 -------GGYYQVDASnlrgtymlldEAS--VTGTanVLMAAVMAEGTTTIY---NAACEPYLQQLSKMLNSMGAKISGV 216
Cdd:PRK02427  148 tirggkkGGPIEYDGP----------VSSqfVKSL--LLLAPLFAEGDTETTviePLPSRPHTEITLRMLRAFGVEVENV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823152548 217 GSN---LLTIEGVSELQGTEHTMLPDmieIGS---FIGLAAMTQ-SEITIKNCRIPEL---GIIPDQFRRLGIQVDFRGD 286
Cdd:PRK02427  216 EGWgyrRIVIKGGQRLRGQDITVPGD---PSSaafFLAAAAITGgSEVTITNVGLNSTqggKAIIDVLEKMGADIEIENE 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1823152548 287 DIFIPAQERYQIET-FLDGGMMTVADspwpgfTPDLLSIVLVTAVQAQGT 335
Cdd:PRK02427  293 REGGEPVGDIRVRSsELKGIDIDIPD------IIDEAPTLAVLAAFAEGT 336
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH