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Conserved domains on  [gi|489079357|ref|WP_002989295|]
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UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Streptococcus pyogenes]

Protein Classification

UDP-N-acetylglucosamine 1-carboxyvinyltransferase( domain architecture ID 10793701)

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
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


:

Pssm-ID: 183779  Cd Length: 417  Bit Score: 740.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHGDTLEIDPRGVQD 80
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  81 IPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNgqKIHGAHIYM 160
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKAD--ELKGAHIYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 161 DTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTY 240
Cdd:PRK12830 159 DVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 241 IALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKTSPYPGFATDLQQPLTPLLLKADG 320
Cdd:PRK12830 239 MILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 321 RGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRGY 400
Cdd:PRK12830 319 RSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGY 398
                        410
                 ....*....|....*....
gi 489079357 401 ASIIAKLTALGADIQLIED 419
Cdd:PRK12830 399 SNIIEKLKALGADIWREED 417
 
Name Accession Description Interval E-value
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 740.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHGDTLEIDPRGVQD 80
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  81 IPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNgqKIHGAHIYM 160
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKAD--ELKGAHIYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 161 DTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTY 240
Cdd:PRK12830 159 DVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 241 IALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKTSPYPGFATDLQQPLTPLLLKADG 320
Cdd:PRK12830 239 MILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 321 RGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRGY 400
Cdd:PRK12830 319 RSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGY 398
                        410
                 ....*....|....*....
gi 489079357 401 ASIIAKLTALGADIQLIED 419
Cdd:PRK12830 399 SNIIEKLKALGADIWREED 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-417 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: 598.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYH-GDTLEIDPRGVQ 79
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdGGTLTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  80 DIPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNGqkIHGAHIY 159
Cdd:COG0766   81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGR--LKGARIY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 160 MDTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGT 239
Cdd:COG0766  159 LDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 240 YIALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKTSPYPGFATDLQQPLTPLLLKAD 319
Cdd:COG0766  239 FLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 320 GRGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRG 399
Cdd:COG0766  319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
                        410
                 ....*....|....*...
gi 489079357 400 YASIIAKLTALGADIQLI 417
Cdd:COG0766  399 YENLEEKLRALGADIERV 416
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-410 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: 547.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  12 LSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHG-DTLEIDPRGVQDIPMPYGKINS 90
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  91 LRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNGqKIHGAHIYMDTVSVGATIN 170
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAG-RLKGARIYLDFPSVGATEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 171 TMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTYIALAAAIGKG 250
Cdd:cd01555  160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 251 VKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVE-KQESLKAITIKTSPYPGFATDLQQPLTPLLLKADGRGTIIDTIY 329
Cdd:cd01555  240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDgDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 330 EKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRGYASIIAKLTA 409
Cdd:cd01555  320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399

                 .
gi 489079357 410 L 410
Cdd:cd01555  400 L 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-415 3.74e-174

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: 492.90  E-value: 3.74e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357    1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHGDTLEIDPRGVQD 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   81 IPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNGqKIHGAHIYM 160
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKG-RLVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  161 DTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTY 240
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  241 IALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVE-KQESLKAITIKTSPYPGFATDLQQPLTPLLLKAD 319
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDmRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  320 GRGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRG 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
                         410
                  ....*....|....*.
gi 489079357  400 YASIIAKLTALGADIQ 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIE 415
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-407 1.07e-87

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 272.25  E-value: 1.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357    7 NGGKALSGEVAVSG-AKNSVVALIPAIILADDIVIlDGVPAISDVDSLIEIMELMGATVNYHGDTLE--IDPRGVQDIPM 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGESTI-TNLLDSDDTLTMLEALRALGAEIIKLDDEKSvvIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   84 PYGKINSLRASYYFYGSLLGRFGQAV--VGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLS--TNGQKIHGAHIY 159
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPlkVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  160 MDTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTD-IITIQGVQKLHGTRHQVIPDRIEAG 238
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  239 TYIALAAAIGKGVKITNVLYEHL---ESFIAKLEEMGVRMTVEEDAIFVEKQ--ESLKAITIKTSPYPGFATDLQQPLTP 313
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPpgLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  314 LLLKADGRGTIIDTIYEKRINHVPELMRMGADISVIG-GQIVYQGPSRLTGAQVKAT-DLRAGAALVTAGLIAEGKTEIT 391
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPdGLIIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 489079357  392 NIEFILRGYASIIAKL 407
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 740.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHGDTLEIDPRGVQD 80
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  81 IPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNgqKIHGAHIYM 160
Cdd:PRK12830  81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKAD--ELKGAHIYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 161 DTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTY 240
Cdd:PRK12830 159 DVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 241 IALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKTSPYPGFATDLQQPLTPLLLKADG 320
Cdd:PRK12830 239 MILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 321 RGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRGY 400
Cdd:PRK12830 319 RSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGY 398
                        410
                 ....*....|....*....
gi 489079357 401 ASIIAKLTALGADIQLIED 419
Cdd:PRK12830 399 SNIIEKLKALGADIWREED 417
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-417 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: 598.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYH-GDTLEIDPRGVQ 79
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdGGTLTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  80 DIPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNGqkIHGAHIY 159
Cdd:COG0766   81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGR--LKGARIY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 160 MDTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGT 239
Cdd:COG0766  159 LDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 240 YIALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKTSPYPGFATDLQQPLTPLLLKAD 319
Cdd:COG0766  239 FLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 320 GRGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRG 399
Cdd:COG0766  319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
                        410
                 ....*....|....*...
gi 489079357 400 YASIIAKLTALGADIQLI 417
Cdd:COG0766  399 YENLEEKLRALGADIERV 416
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-417 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 571.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHGD-TLEIDPRGVQ 79
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  80 DIPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNGqKIHGAHIY 159
Cdd:PRK09369  81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADG-RLKGAHIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 160 MDTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGT 239
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 240 YIALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKTSPYPGFATDLQQPLTPLLLKAD 319
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 320 GRGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRG 399
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
                        410
                 ....*....|....*...
gi 489079357 400 YASIIAKLTALGADIQLI 417
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
12-410 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: 547.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  12 LSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHG-DTLEIDPRGVQDIPMPYGKINS 90
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  91 LRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNGqKIHGAHIYMDTVSVGATIN 170
Cdd:cd01555   81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAG-RLKGARIYLDFPSVGATEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 171 TMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTYIALAAAIGKG 250
Cdd:cd01555  160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 251 VKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVE-KQESLKAITIKTSPYPGFATDLQQPLTPLLLKADGRGTIIDTIY 329
Cdd:cd01555  240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDgDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 330 EKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRGYASIIAKLTA 409
Cdd:cd01555  320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399

                 .
gi 489079357 410 L 410
Cdd:cd01555  400 L 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-415 3.74e-174

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: 492.90  E-value: 3.74e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357    1 MRKIIINGGKALSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHGDTLEIDPRGVQD 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   81 IPMPYGKINSLRASYYFYGSLLGRFGQAVVGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLSTNGqKIHGAHIYM 160
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKG-RLVGAHIVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  161 DTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTY 240
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  241 IALAAAIGKGVKITNVLYEHLESFIAKLEEMGVRMTVEEDAIFVE-KQESLKAITIKTSPYPGFATDLQQPLTPLLLKAD 319
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDmRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  320 GRGTIIDTIYEKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKATDLRAGAALVTAGLIAEGKTEITNIEFILRG 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
                         410
                  ....*....|....*.
gi 489079357  400 YASIIAKLTALGADIQ 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIE 415
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-407 1.07e-87

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 272.25  E-value: 1.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357    7 NGGKALSGEVAVSG-AKNSVVALIPAIILADDIVIlDGVPAISDVDSLIEIMELMGATVNYHGDTLE--IDPRGVQDIPM 83
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGESTI-TNLLDSDDTLTMLEALRALGAEIIKLDDEKSvvIVEGLGGSFEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   84 PYGKINSLRASYYFYGSLLGRFGQAV--VGLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGENMNLS--TNGQKIHGAHIY 159
Cdd:pfam00275  80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPlkVRGLRLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  160 MDTVSVGATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTD-IITIQGVQKLHGTRHQVIPDRIEAG 238
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  239 TYIALAAAIGKGVKITNVLYEHL---ESFIAKLEEMGVRMTVEEDAIFVEKQ--ESLKAITIKTSPYPGFATDLQQPLTP 313
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPpgLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  314 LLLKADGRGTIIDTIYEKRINHVPELMRMGADISVIG-GQIVYQGPSRLTGAQVKAT-DLRAGAALVTAGLIAEGKTEIT 391
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPdGLIIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 489079357  392 NIEFILRGYASIIAKL 407
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-410 1.72e-77

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: 245.98  E-value: 1.72e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  12 LSGEVAVSGAKNSVVALIPAIILADDIVILDGVPAISDVDSLIEIMELMGATVNYHGDTLEIDPRGV---QDIPMPYGKI 88
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMaglKAPQNALNLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  89 NSLRASYYFYGSLLGRFGQavVGLPGGCDLGPRPIDLHLKAFEAMGVEVSY-EGENMNLSTNGQKIHGAHIYMD-TVSVG 166
Cdd:cd01554   81 NSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASISGqEERDLPPLLKGGKNLGPIHYEDpIASAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 167 ATINTMVAATKAQGKTVIENAAREPEIIDVATLLNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGTYIALAAA 246
Cdd:cd01554  159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 247 IGKGVKITNV-LYEHLESFIAKLEEMGVRMTVEEDAIFVEKQEsLKAITIKTSPYPgFATDLQQPLTPLLLKADGRGTII 325
Cdd:cd01554  239 APGRLVLQNVgINETRTGIIDVLRAMGAKIEIGEDTISVESSD-LKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 326 DTIY------EKRINHVPELMRMGADISVIGGQIVYQGPSRLTGAQVKAT-DLRAGAALVTAGLIAEGKTEITNIEFILR 398
Cdd:cd01554  317 DAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAINT 396
                        410
                 ....*....|..
gi 489079357 399 GYASIIAKLTAL 410
Cdd:cd01554  397 SYPSFFDDLESL 408
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-396 1.56e-24

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: 104.56  E-value: 1.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  12 LSGEVAVSGAKN-SVVALIPAIiLADDIVILDGvPAIS-DVDSLIEIMELMGATVNYHGDTLEIDPRGVQdIPMPYGKI- 88
Cdd:cd01556    1 LSGEITVPGSKSiSHRALLLAA-LAEGESRIEN-LLDSdDTLATLEALRALGAKIEEEGGTVEIVGGGGL-GLPPEAVLd 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  89 --NSLRASYYFYGSLLGRFGQAVvgLPGGCDLGPRPIDLHLKAFEAMGVEVSY-EGENMNLSTNGQKIHGAHIYMDtVSV 165
Cdd:cd01556   78 cgNSGTTMRLLTGLLALQGGDSV--LTGDESLRKRPMGRLVDALRQLGAEIEGrEGGGYPPLIGGGGLKGGEVEIP-GAV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 166 GATINT--MVAATKAQGKTVIENAAREPEI-IDVaTL--LNNMGAHIRGAGTDIITIQGVQKLHGTRHQVIPDrIEAGTY 240
Cdd:cd01556  155 SSQFKSalLLAAPLAEGPTTIIIGELESKPyIDH-TErmLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGD-ASSAAF 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 241 IALAAAIGKG-VKITNVLYEHLESFIAK-LEEMGVRMTV-EEDAIFVEKQESLKAITIKTSPYPgfatDLQQPLTPLLLK 317
Cdd:cd01556  233 FLAAAAITGSeIVIKNVGLNSGDTGIIDvLKEMGADIEIgNEDTVVVESGGKLKGIDIDGNDIP----DEAPTLAVLAAF 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 318 ADGrGTIIDTIYEKRINH-------VPELMRMGADISVIG-GQIVYQGPSRLTGAQVKA-TDLRAGAALVTAGLIAEGKT 388
Cdd:cd01556  309 AEG-PTRIRNAAELRVKEsdriaamATELRKLGADVEETEdGLIIEGGPLKGAGVEVYTyGDHRIAMSFAIAGLVAEGGV 387

                 ....*...
gi 489079357 389 EITNIEFI 396
Cdd:cd01556  388 TIEDPECV 395
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-413 1.34e-22

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: 98.89  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   14 GEVAVSGAKN-SVVALIPAIiLADDIVILDGVPAISDVDSLIEIMELMGATVNYHGDTLEIDPRGVQdipMPYGKIN--- 89
Cdd:TIGR01356   1 GEIRAPGSKSiTHRALILAA-LAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGK---EPQAELDlgn 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   90 ---SLRasyyFYGSLLGRFGQAVVgLPGGCDLGPRPIDLHLKAFEAMGVEVSY--EGENMNLSTNGqKIHGAHIYMDTvS 164
Cdd:TIGR01356  77 sgtTAR----LLTGVLALADGEVV-LTGDESLRKRPMGRLVDALRQLGAEISSleGGGSLPLTISG-PLPGGIVYISG-S 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  165 VGATINT--MVAATKAQGKTVIENAAREPEIIDVATLLNNMGAH---IRGAGTDIITIQGVQKLHGTRHQVIPDRIEAGT 239
Cdd:TIGR01356 150 ASSQYKSalLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFgveVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAF 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  240 YIALAAAIGKGVKITNVLYEHLE---SFIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKTSPYPgfatDLQQPLTPLLL 316
Cdd:TIGR01356 230 FLAAAAITGGRVTLENLGINPTQgdkAIIIVLEEMGADIEVEEDDLIVEGASGLKGIKIDMDDMI----DELPTLAVLAA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  317 KADGRGTIIDtIYEKRINH-------VPELMRMGADISVIGGQIVYQGPSRLTGAQVKA-TDLRAGAALVTAGLIAEGKT 388
Cdd:TIGR01356 306 FAEGVTRITG-AEELRVKEsdriaaiAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTfGDHRIAMAFAVAGLVAEGEV 384
                         410       420
                  ....*....|....*....|....*
gi 489079357  389 EITNIEFILRGYASIIAKLTALGAD 413
Cdd:TIGR01356 385 LIDDPECVAKSFPSFFDVLERLGAN 409
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-419 2.01e-18

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: 86.68  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKnSV---VALIPAiiLADDIVILDGVPAISDVDSLIEIMELMGATVNYH-GDTLEIDPR 76
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSK-SIshrALLLAA--LAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  77 GVQdIPMPYGKI---NSlrasyyfyGSLLgRFGQAVVGLPGGC-----D--LGPRPIDLHLKAFEAMGVEVSYEGENMN- 145
Cdd:COG0128   78 GGG-LKEPDAVLdcgNS--------GTTM-RLLTGLLALQPGEvvltgDesLRKRPMGRLLDPLRQLGARIESRGGGYLp 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 146 LSTNGQKIHGAHIYMDTV-------SVgatintMVAATKAQGKTVIENAAREPEI--IDVaTL--LNNMGAHIRGAGTDI 214
Cdd:COG0128  148 LTIRGGPLKGGEYEIPGSassqfksAL------LLAGPLAEGGLEITVTGELESKpyRDH-TErmLRAFGVEVEVEGYRR 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 215 ITIQGVQKLHGTRHQVIPDRIEAGTYIALAAAIGKGVKITNVLYEHLES---FIAKLEEMGVRMTVEEDAIFVEKQEsLK 291
Cdd:COG0128  221 FTVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGdtgILDILKEMGADIEIENDGITVRGSP-LK 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 292 AITIktspypgfatdlqqpltplllkaDGrgtiidtiyekriNHVPELMrmgadisviggqivyqgPsrltgaqvkatdl 371
Cdd:COG0128  300 GIDI-----------------------DL-------------SDIPDEA-----------------P------------- 313
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489079357 372 ragaALVTAGLIAEGKTEITNIEfILRGY-----ASIIAKLTALGADIQLIED 419
Cdd:COG0128  314 ----TLAVLAAFAEGTTRIRGAA-ELRVKesdriAAMATELRKLGADVEETED 361
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-419 3.94e-13

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 70.56  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   1 MRKIIINGGKALSGEVAVSGAKN-SVVALIPAIiLADDIVILDGvPAIS-DVDSLIEIMELMGATVnyHGDTLEIDPRGV 78
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSiSHRALLLAA-LAEGETTITN-LLRSeDTLATLNALRALGVEI--EDDEVVVEGVGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  79 QDIPMPYGKIN------SLRasyyFYGSLLGRFGQAVVgLPGGCDLGPRPIDLHLKAFEAMGVEVSYEGE-NMNLSTNGq 151
Cdd:PRK02427  78 GGLKEPEDVLDcgnsgtTMR----LLTGLLALQPGEVV-LTGDESLRKRPMGRLLDPLRQMGAKIEGRDEgYLPLTIRG- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 152 KIHGAHIYMDT-VS---VGATIntMVAATKAQGKTVIEnaAREPEI----IDV-ATLLNNMGAHIR---GAGTDIITIQG 219
Cdd:PRK02427 152 GKKGGPIEYDGpVSsqfVKSLL--LLAPLFAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveGWGYRRIVIKG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 220 VQKLHGTRHQVIPDrIEAGTYIALAAAIGKG--VKITNVLYEHL---ESFIAKLEEMGVRMTVEEDAIFVEKQESlkaIT 294
Cdd:PRK02427 228 GQRLRGQDITVPGD-PSSAAFFLAAAAITGGseVTITNVGLNSTqggKAIIDVLEKMGADIEIENEREGGEPVGD---IR 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 295 IKTSPYpgfatdlqqpltplllkadgRGTIIDtiyekrINHVPELMrmgadisviggqivyqgPsrltgaqvkatdlrag 374
Cdd:PRK02427 304 VRSSEL--------------------KGIDID------IPDIIDEA-----------------P---------------- 324
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 489079357 375 aALVTAGLIAEGKTEITNIEFiLRG-----YASIIAKLTALGADIQLIED 419
Cdd:PRK02427 325 -TLAVLAAFAEGTTVIRNAEE-LRVketdrIAAMATELRKLGAEVEETED 372
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
4-256 1.84e-08

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: 55.86  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357   4 IIINGGKALSGEVAVSGAKNSVV--ALIPAIILADD---IVILDGVPAISDVDSLIEIMELMGATVNYHG-DTLEIDPRG 77
Cdd:COG0128  148 LTIRGGPLKGGEYEIPGSASSQFksALLLAGPLAEGgleITVTGELESKPYRDHTERMLRAFGVEVEVEGyRRFTVPGGQ 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  78 V---QDIPMPyGKINSlrASYYFYGSLLGrfGQAVVgLPGgcdLGPRPIDLH---LKAFEAMGVEVSYEGENmnLSTNGQ 151
Cdd:COG0128  228 RyrpGDYTVP-GDISS--AAFFLAAAAIT--GSEVT-VEG---VGLNSTQGDtgiLDILKEMGADIEIENDG--ITVRGS 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 152 KIHGAHIYMDTVSVGA-TIntMVAATKAQGKTVIENAA--REPE---IIDVATLLNNMGAHIRgAGTDIITIQGVQKLHG 225
Cdd:COG0128  297 PLKGIDIDLSDIPDEApTL--AVLAAFAEGTTRIRGAAelRVKEsdrIAAMATELRKLGADVE-ETEDGLIIEGGPKLKG 373
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489079357 226 TrhqvipdRIEagTY----IALAAAI-----GKGVKITNV 256
Cdd:COG0128  374 A-------EVD--SYgdhrIAMAFAVaglraEGPVTIDDA 404
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
28-297 1.67e-07

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


Pssm-ID: 439898  Cd Length: 421  Bit Score: 53.17  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  28 LIPAIILADDIVILDGVPAIS--DVDSLIEIMELMGATVNYHGDT---LEIDPRGVQ--DIPMPyGKINS-------LRA 93
Cdd:COG0128  100 LTGLLALQPGEVVLTGDESLRkrPMGRLLDPLRQLGARIESRGGGylpLTIRGGPLKggEYEIP-GSASSqfksallLAG 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357  94 SYYFYGSLLgrfgqAVVGlpggcDLGPRP-IDLHLKAFEAMGVEVSYEGENMNLSTNGQKIHGAHIymdTV----SVGAT 168
Cdd:COG0128  179 PLAEGGLEI-----TVTG-----ELESKPyRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYRPGDY---TVpgdiSSAAF 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 169 IntMVAATKAQGKTVIENAAREP-----EIIDVatlLNNMGAHIRgAGTDIITIQGvQKLHGTR---HQvIPDriEAGTy 240
Cdd:COG0128  246 F--LAAAAITGSEVTVEGVGLNStqgdtGILDI---LKEMGADIE-IENDGITVRG-SPLKGIDidlSD-IPD--EAPT- 314
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489079357 241 IALAAAIGKGV-KITNVlyEHL---ES-----FIAKLEEMGVRMTVEEDAIFVEKQESLKAITIKT 297
Cdd:COG0128  315 LAVLAAFAEGTtRIRGA--AELrvkESdriaaMATELRKLGADVEETEDGLIIEGGPKLKGAEVDS 378
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
232-410 1.36e-06

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: 48.81  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 232 PDRIEAGTYIALAAAIGKGVKITNV--------LYEHLESFIAKLEEMgVRMTVEE----DAIFVEKQESLKAITIKTSP 299
Cdd:cd01553    8 GGGQILRSFLVLAAISGGPITVTGIrpdrakpgLLRQHLTFLKALEKI-CGATVEGgelgSDRISFRPGTVRGGDVRFAI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 300 YP-GFATDLQQPLTPLLLKADGRGTIIDTIY----------EKRINHVPELMRMGA------------DISVIGGQIVYQ 356
Cdd:cd01553   87 GSaGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAhqeetllrhgfyPAGGGVVATEVS 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489079357 357 GPSRLTGAQVKATDLragaalvtaGLIAEGKTEITNIEFILRGYASIIAKLTAL 410
Cdd:cd01553  167 PVEKLNTAQLRQLVL---------PMLLASGAVEFTVAHPSCHLLTNFAVLEAL 211
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
112-303 5.20e-03

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 39.21  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 112 LPGGCDLGPRPIDLHLKAFEAMG--VEVSYEGENMNLSTNGQKIHGAHIYMDTVSVGATINTMVAATKAQGKTVIenaaR 189
Cdd:PRK14806 414 LTGDASLSKRPMERVAKPLREMGavIETGEEGRPPLSIRGGQRLKGIHYDLPMASAQVKSCLLLAGLYAEGETSV----T 489
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079357 190 EPEIIDVAT--LLNNMGAHIRGAGtDIITIQGVQKLHGTrHQVIPDRIEAGTYIALAAAIGKGVKITnvlYEHL------ 261
Cdd:PRK14806 490 EPAPTRDHTerMLRGFGYPVKVEG-NTISVEGGGKLTAT-DIEVPADISSAAFFLVAASIAEGSELT---LEHVginptr 564
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489079357 262 ESFIAKLEEMGVRMTVEEDAIFveKQESLKAITIKTSPYPGF 303
Cdd:PRK14806 565 TGVIDILKLMGADITLENEREV--GGEPVADIRVRGARLKGI 604
 
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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