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Conserved domains on  [gi|1176198887|gb|OQY11005|]
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MAG: UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Marinitoga sp. 4572_148]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-418 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis


:

Pssm-ID: 440529  Cd Length: 416  Bit Score: 612.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWND-SSLIIKGCSEI 79
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDgGTLTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  80 NSVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKFTRTRGEKIHis 159
Cdd:COG0766    81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIY-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 160 LPFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAG 239
Cdd:COG0766   159 LDFPSVGATENIMMAAVL-AEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 240 TYAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGISKLelSPIDVETATFPGFPTDLQPQLMVLLS 319
Cdd:COG0766   238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRL--KAVDIKTAPYPGFPTDLQAQFMALLT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 320 LIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHI 399
Cdd:COG0766   316 QAEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHI 395
                         410
                  ....*....|....*....
gi 1176198887 400 FRGYEKLFEKLEKLGLKIE 418
Cdd:COG0766   396 DRGYENLEEKLRALGADIE 414
 
Name Accession Description Interval E-value
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-418 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440529  Cd Length: 416  Bit Score: 612.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWND-SSLIIKGCSEI 79
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDgGTLTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  80 NSVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKFTRTRGEKIHis 159
Cdd:COG0766    81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIY-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 160 LPFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAG 239
Cdd:COG0766   159 LDFPSVGATENIMMAAVL-AEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 240 TYAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGISKLelSPIDVETATFPGFPTDLQPQLMVLLS 319
Cdd:COG0766   238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRL--KAVDIKTAPYPGFPTDLQAQFMALLT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 320 LIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHI 399
Cdd:COG0766   316 QAEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHI 395
                         410
                  ....*....|....*....
gi 1176198887 400 FRGYEKLFEKLEKLGLKIE 418
Cdd:COG0766   396 DRGYENLEEKLRALGADIE 414
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-418 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 606.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDS-SLIIKGCSEI 79
Cdd:PRK09369    1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  80 NSVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSK-FTRTRGEKIHi 158
Cdd:PRK09369   81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKaDGRLKGAHIV- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 159 sLPFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEA 238
Cdd:PRK09369  160 -LDFPSVGATENILMAAVL-AEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 239 GTYAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIIngISKLELSPIDVETATFPGFPTDLQPQLMVLL 318
Cdd:PRK09369  238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRV--DMPGRLKAVDIKTAPYPGFPTDMQAQFMALL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 319 SLIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDH 398
Cdd:PRK09369  316 TQAEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYH 395
                         410       420
                  ....*....|....*....|
gi 1176198887 399 IFRGYEKLFEKLEKLGLKIE 418
Cdd:PRK09369  396 LDRGYERIEEKLRALGADIE 415
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
13-413 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.


Pssm-ID: 238796  Cd Length: 400  Bit Score: 554.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  13 NGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDS-SLIIKGCSEINSVLPYGPVRRM 91
Cdd:cd01555     2 SGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRKM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  92 RASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKF-TRTRGEKIHisLPFPSVGATEH 170
Cdd:cd01555    82 RASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAaGRLKGARIY--LDFPSVGATEN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 171 LITTATLLGNTeTILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAGTYAILGAVLGE 250
Cdd:cd01555   160 IMMAAVLAEGT-TVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 251 RVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGiSKLELSPIDVETATFPGFPTDLQPQLMVLLSLIPGRSSITEN 330
Cdd:cd01555   239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDG-DGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITET 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 331 VFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHIFRGYEKLFEKL 410
Cdd:cd01555   318 IFENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKL 397

                  ...
gi 1176198887 411 EKL 413
Cdd:cd01555   398 RAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 162190 [Multi-domain]  Cd Length: 416  Bit Score: 529.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDSSLIIKGCSEIN 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  81 SVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKF-TRTRGEKIHis 159
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAkGRLVGAHIV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 160 LPFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAG 239
Cdd:TIGR01072 159 LDKVSVGATENIIMAAVL-AEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 240 TYAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGISKlELSPIDVETATFPGFPTDLQPQLMVLLS 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQK-RLKAVDIETLPYPGFPTDLQAQFMALLS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 320 LIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHI 399
Cdd:TIGR01072 317 QAEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHL 396
                         410       420
                  ....*....|....*....|
gi 1176198887 400 FRGYEKLFEKLEKLGLKIEY 419
Cdd:TIGR01072 397 DRGYEDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-410 8.45e-103

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 311.15  E-value: 8.45e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   8 GPQRANGEITISGSK-NSALPILAATLLTDEDIIlHNIPNLADVNTMIEILENAGKKIT-WNDSSLIIKGCSEINSVL-P 84
Cdd:pfam00275   2 GGSRLSGEVKIPGSKsNSHRALILAALAAGESTI-TNLLDSDDTLTMLEALRALGAEIIkLDDEKSVVIVEGLGGSFEaP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  85 YGPVRRMRASFNVLGPLTIRNGYAK--VALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKFTRT--RGEKIHISL 160
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRglRLGGIHIDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 161 PFPSVGATEHLITtATLLGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSN-IKIHGVEKLSGAEYTIIPDRIEAG 239
Cdd:pfam00275 161 DVSSQFVTSLLML-AALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 240 TYAILGAVLGERVVLNNVIEDHL---FALLDIFEKIGVRYEFIDNKLIINGISKLELSPIDVETATFPGFPTDLQPQLMV 316
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 317 LLSLIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTK-LSGAPLEAT-DLRASAALLIASLIADGETVIN 394
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 1176198887 395 NVDHIFRGYEKLFEKL 410
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
1-418 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440529  Cd Length: 416  Bit Score: 612.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWND-SSLIIKGCSEI 79
Cdd:COG0766     1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDgGTLTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  80 NSVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKFTRTRGEKIHis 159
Cdd:COG0766    81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIY-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 160 LPFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAG 239
Cdd:COG0766   159 LDFPSVGATENIMMAAVL-AEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 240 TYAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGISKLelSPIDVETATFPGFPTDLQPQLMVLLS 319
Cdd:COG0766   238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRL--KAVDIKTAPYPGFPTDLQAQFMALLT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 320 LIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHI 399
Cdd:COG0766   316 QAEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHI 395
                         410
                  ....*....|....*....
gi 1176198887 400 FRGYEKLFEKLEKLGLKIE 418
Cdd:COG0766   396 DRGYENLEEKLRALGADIE 414
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
1-418 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 606.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDS-SLIIKGCSEI 79
Cdd:PRK09369    1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  80 NSVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSK-FTRTRGEKIHi 158
Cdd:PRK09369   81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKaDGRLKGAHIV- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 159 sLPFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEA 238
Cdd:PRK09369  160 -LDFPSVGATENILMAAVL-AEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 239 GTYAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIIngISKLELSPIDVETATFPGFPTDLQPQLMVLL 318
Cdd:PRK09369  238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRV--DMPGRLKAVDIKTAPYPGFPTDMQAQFMALL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 319 SLIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDH 398
Cdd:PRK09369  316 TQAEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYH 395
                         410       420
                  ....*....|....*....|
gi 1176198887 399 IFRGYEKLFEKLEKLGLKIE 418
Cdd:PRK09369  396 LDRGYERIEEKLRALGADIE 415
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
13-413 0e+00

UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.


Pssm-ID: 238796  Cd Length: 400  Bit Score: 554.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  13 NGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDS-SLIIKGCSEINSVLPYGPVRRM 91
Cdd:cd01555     2 SGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRKM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  92 RASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKF-TRTRGEKIHisLPFPSVGATEH 170
Cdd:cd01555    82 RASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAaGRLKGARIY--LDFPSVGATEN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 171 LITTATLLGNTeTILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAGTYAILGAVLGE 250
Cdd:cd01555   160 IMMAAVLAEGT-TVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 251 RVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGiSKLELSPIDVETATFPGFPTDLQPQLMVLLSLIPGRSSITEN 330
Cdd:cd01555   239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDG-DGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITET 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 331 VFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHIFRGYEKLFEKL 410
Cdd:cd01555   318 IFENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKL 397

                  ...
gi 1176198887 411 EKL 413
Cdd:cd01555   398 RAL 400
murA TIGR01072
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ...
1-419 0e+00

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 162190 [Multi-domain]  Cd Length: 416  Bit Score: 529.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDSSLIIKGCSEIN 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  81 SVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKF-TRTRGEKIHis 159
Cdd:TIGR01072  81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAkGRLVGAHIV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 160 LPFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAG 239
Cdd:TIGR01072 159 LDKVSVGATENIIMAAVL-AEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 240 TYAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGISKlELSPIDVETATFPGFPTDLQPQLMVLLS 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQK-RLKAVDIETLPYPGFPTDLQAQFMALLS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 320 LIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHI 399
Cdd:TIGR01072 317 QAEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHL 396
                         410       420
                  ....*....|....*....|
gi 1176198887 400 FRGYEKLFEKLEKLGLKIEY 419
Cdd:TIGR01072 397 DRGYEDLEEKLRALGAKIER 416
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
1-418 5.96e-148

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 426.58  E-value: 5.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDSSLIIKGCSEIN 80
Cdd:PRK12830    1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  81 SVLPYGPVRRMRASFNVLGPLTIRNGYAKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKFTRTRGEkiHISL 160
Cdd:PRK12830   81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGA--HIYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 161 PFPSVGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAGT 240
Cdd:PRK12830  159 DVVSVGATINIMLAAVK-AKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 241 YAILGAVLGERVVLNNVIEDHLFALLDIFEKIGVRYEFIDNKLIINGisKLELSPIDVETATFPGFPTDLQPQLMVLLSL 320
Cdd:PRK12830  238 YMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEK--QGNLKAVDIKTLPYPGFATDLQQPLTPLLLK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 321 IPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEATDLRASAALLIASLIADGETVINNVDHIF 400
Cdd:PRK12830  316 ANGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHID 395
                         410
                  ....*....|....*...
gi 1176198887 401 RGYEKLFEKLEKLGLKIE 418
Cdd:PRK12830  396 RGYSNIIEKLKALGADIW 413
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-410 8.45e-103

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 311.15  E-value: 8.45e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   8 GPQRANGEITISGSK-NSALPILAATLLTDEDIIlHNIPNLADVNTMIEILENAGKKIT-WNDSSLIIKGCSEINSVL-P 84
Cdd:pfam00275   2 GGSRLSGEVKIPGSKsNSHRALILAALAAGESTI-TNLLDSDDTLTMLEALRALGAEIIkLDDEKSVVIVEGLGGSFEaP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  85 YGPVRRMRASFNVLGPLTIRNGYAK--VALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKFTRT--RGEKIHISL 160
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRglRLGGIHIDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 161 PFPSVGATEHLITtATLLGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSN-IKIHGVEKLSGAEYTIIPDRIEAG 239
Cdd:pfam00275 161 DVSSQFVTSLLML-AALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 240 TYAILGAVLGERVVLNNVIEDHL---FALLDIFEKIGVRYEFIDNKLIINGISKLELSPIDVETATFPGFPTDLQPQLMV 316
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 317 LLSLIPGRSSITENVFKTRFNHVDELNRMGAKIFVESNTAIITGVTK-LSGAPLEAT-DLRASAALLIASLIADGETVIN 394
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
                         410
                  ....*....|....*.
gi 1176198887 395 NVDHIFRGYEKLFEKL 410
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
13-413 6.99e-83

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: 259.84  E-value: 6.99e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  13 NGEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDSSLIIKG------CSEINsvlPYG 86
Cdd:cd01554     2 HGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGvgmaglKAPQN---ALN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  87 PVRRMRASFNVLGPLTIRNGyaKVALPGGCSIGVRPVNFHLEGLKKLGIDSKIEHGFTNSKFTRTRGEK--IHISLPFPS 164
Cdd:cd01554    79 LGNSGTAIRLISGVLAGADF--EVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLgpIHYEDPIAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 165 VGATEHLITTATLlGNTETILTNCAQEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAGTYAIL 244
Cdd:cd01554   157 AQVKSALMFAALL-AKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 245 GAVLGERVVLNNV-IEDHLFALLDIFEKIGVRYEFIDNKLIingISKLELSPIDVETATFPgFPTDLQPQLMVLLSLIPG 323
Cdd:cd01554   236 AAIAPGRLVLQNVgINETRTGIIDVLRAMGAKIEIGEDTIS---VESSDLKATEICGALIP-RLIDELPIIALLALQAQG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 324 RSSITENVF------KTRFNHVDELNRMGAKIFVESNTAIITGVTKLSGAPLEAT-DLRASAALLIASLIADGETVINNV 396
Cdd:cd01554   312 TTVIKDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRA 391
                         410
                  ....*....|....*..
gi 1176198887 397 DHIFRGYEKLFEKLEKL 413
Cdd:cd01554   392 EAINTSYPSFFDDLESL 408
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-414 7.40e-27

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: 111.21  E-value: 7.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  14 GEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDSSLIIKGCseiNSVLPYGPVRrMRA 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGV---GGKEPQAELD-LGN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  94 SFNVLGPLTirnGYA-----KVALPGGCSIGVRPVNFHLEGLKKLG--IDSKIEHGF----TNSKftrTRGEKIHISLPF 162
Cdd:TIGR01356  77 SGTTARLLT---GVLaladgEVVLTGDESLRKRPMGRLVDALRQLGaeISSLEGGGSlpltISGP---LPGGIVYISGSA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 163 PSVGATEHLITTATLLGNTETILTNCA-QEPEIVDLCNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAGTY 241
Cdd:TIGR01356 151 SSQYKSALLLAAPALQAVGITIVGEPLkSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 242 AILGAVLGERVVLNNVIEDHL---FALLDIFEKIGVRYEFIDNKLIINGISKleLSPIDVETATFPgfptDLQPQLMVLL 318
Cdd:TIGR01356 231 LAAAAITGGRVTLENLGINPTqgdKAIIIVLEEMGADIEVEEDDLIVEGASG--LKGIKIDMDDMI----DELPTLAVLA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 319 SLIPGRSSITeNVFKTRFNHVD-------ELNRMGAKIFVESNTAIITGVTKLSGAPLEA-TDLRASAALLIASLIADGE 390
Cdd:TIGR01356 305 AFAEGVTRIT-GAEELRVKESDriaaiaeELRKLGVDVEEFEDGLYIRGKKELKGAVVDTfGDHRIAMAFAVAGLVAEGE 383
                         410       420
                  ....*....|....*....|....
gi 1176198887 391 TVINNVDHIFRGYEKLFEKLEKLG 414
Cdd:TIGR01356 384 VLIDDPECVAKSFPSFFDVLERLG 407
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
13-410 2.03e-26

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: 109.95  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  13 NGEITISGSK---NSALpILAAtlLTDEDIILHNIPNLADVNTMIEILENAGKKITWNDSSLIIKGCSEINSVLPY---- 85
Cdd:cd01556     2 SGEITVPGSKsisHRAL-LLAA--LAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGLPPEAvldc 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  86 ---GPVRRMrasfnVLGPLTIRNGYakVALPGGCSIGVRPVNFHLEGLKKLG--IDSKIEHGF-TNSKFTRTRGEKIHIS 159
Cdd:cd01556    79 gnsGTTMRL-----LTGLLALQGGD--SVLTGDESLRKRPMGRLVDALRQLGaeIEGREGGGYpPLIGGGGLKGGEVEIP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 160 LPFPSVGATEHLITTATLLGNTETILTNCAQEPEIvDL-CNFLISMGAKIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEA 238
Cdd:cd01556   152 GAVSSQFKSALLLAAPLAEGPTTIIIGELESKPYI-DHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDASSA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 239 GTYAILGAVLGERVVLNNV-IEDHLFALLDIFEKIGVRYEFIDNKlIINGISKLELSPIDVETATFPgfptDLQPQLMVL 317
Cdd:cd01556   231 AFFLAAAAITGSEIVIKNVgLNSGDTGIIDVLKEMGADIEIGNED-TVVVESGGKLKGIDIDGNDIP----DEAPTLAVL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 318 LSLIPGRSSITeNVFKTRFNH-------VDELNRMGAKIFVESNTAIITGVTKLSGAPLEAT--DLRASAALLIASLIAD 388
Cdd:cd01556   306 AAFAEGPTRIR-NAAELRVKEsdriaamATELRKLGADVEETEDGLIIEGGPLKGAGVEVYTygDHRIAMSFAIAGLVAE 384
                         410       420
                  ....*....|....*....|....*
gi 1176198887 389 GETVINNVDHI---FRGYEKLFEKL 410
Cdd:cd01556   385 GGVTIEDPECVaksFPNFFEDLESL 409
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-410 3.52e-25

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: 106.33  E-value: 3.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSK---NSALpILAAtlLTDEDIILHNIPNLADVNTMIEILENAGKKITW-NDSSLIIKGC 76
Cdd:COG0128     1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL-LLAA--LAEGESTIRNLLESDDTLATLEALRALGAEIEElDGGTLRVTGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  77 SeinsvlpygpvRRMRASFNVL-----GpLTIR---------NGYakVALPGGCSIGVRPVNFHLEGLKKLGIdsKIEHG 142
Cdd:COG0128    78 G-----------GGLKEPDAVLdcgnsG-TTMRlltgllalqPGE--VVLTGDESLRKRPMGRLLDPLRQLGA--RIESR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 143 FTNSKFTRTRGEK---IHISLPfPSVGA------------TEHLITTaTLLGNTETILTncaqepeiVDLC-NFLISMGA 206
Cdd:COG0128   142 GGGYLPLTIRGGPlkgGEYEIP-GSASSqfksalllagplAEGGLEI-TVTGELESKPY--------RDHTeRMLRAFGV 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 207 KIEGHGTSNIKIHGVEKLSGAEYTIIPDRIEAGTYAILGAVLGERVVLNNVIEDHLF---ALLDIFEKIGVRYEFIDNKL 283
Cdd:COG0128   212 EVEVEGYRRFTVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQgdtGILDILKEMGADIEIENDGI 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 284 IINGiSKLElsPIDVETATFPgfptDLQPQLMVLLSLIPGRSSITeNVFKTRFnH--------VDELNRMGAKIFVESNT 355
Cdd:COG0128   292 TVRG-SPLK--GIDIDLSDIP----DEAPTLAVLAAFAEGTTRIR-GAAELRV-KesdriaamATELRKLGADVEETEDG 362
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1176198887 356 AIITGVTKLSGAPLEA-TDLRASAALLIASLIADGETVINNVDHI---FRGYEKLFEKL 410
Cdd:COG0128   363 LIIEGGPKLKGAEVDSyGDHRIAMAFAVAGLRAEGPVTIDDAECVaksFPDFFELLESL 421
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-418 2.08e-17

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 83.65  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887   1 MGKIKAMGPQRANGEITISGSK---NSALpILAAtlLTDEDIILHNIPNLADVNTMIEILENAGKKITwnDSSLIIKGCS 77
Cdd:PRK02427    2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL-LLAA--LAEGETTITNLLRSEDTLATLNALRALGVEIE--DDEVVVEGVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  78 EINSVLPYGP--------VRRMrasfnVLGPLTIRNGyaKVALPGGCSIGVRPVNFHLEGLKKLG--IDSKIE------- 140
Cdd:PRK02427   77 GGGLKEPEDVldcgnsgtTMRL-----LTGLLALQPG--EVVLTGDESLRKRPMGRLLDPLRQMGakIEGRDEgylplti 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 141 HGftnskftRTRGEKIHISLPFPS--VGAtehLITTATLL--GNTETILTncaqEPEI----VDL-CNFLISMGAKIE-- 209
Cdd:PRK02427  150 RG-------GKKGGPIEYDGPVSSqfVKS---LLLLAPLFaeGDTETTVI----EPLPsrphTEItLRMLRAFGVEVEnv 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 210 -GHGTSNIKIHGVEKLSGAEYTIIPDRIEAGTYAILGAVL-GERVVLNNVIEDHL---FALLDIFEKIGVRYEFIDNKLI 284
Cdd:PRK02427  216 eGWGYRRIVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITgGSEVTITNVGLNSTqggKAIIDVLEKMGADIEIENEREG 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 285 INGISKLE-----LSPIDVETATFPgfptDLQPQLMVLLSLIPGRSSITeNVFKTRFnH--------VDELNRMGAKIFV 351
Cdd:PRK02427  296 GEPVGDIRvrsseLKGIDIDIPDII----DEAPTLAVLAAFAEGTTVIR-NAEELRV-KetdriaamATELRKLGAEVEE 369
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176198887 352 ESNTAIITGVTKlsGAPLEA-TDLRASAALLIASLIADGETVINNVDHI---FRGYeklFEKLEKLGLKIE 418
Cdd:PRK02427  370 TEDGLIITGGPL--AGVVDSyGDHRIAMAFAIAGLAAEGPVTIDDPECVaksFPDF---FEDLASLGANIE 435
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
201-421 4.20e-07

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 51.68  E-value: 4.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 201 LISMGAKIEGHGTSN--IKIHGVEKLSGAEYTiipdrieaGTYA--------ILGAVLGERVVLNNVIE-----DHLFAL 265
Cdd:PRK02427  130 LRQMGAKIEGRDEGYlpLTIRGGKKGGPIEYD--------GPVSsqfvksllLLAPLFAEGDTETTVIEplpsrPHTEIT 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 266 LDIFEKIGVRYEFIDN----KLIINGISKLELSPIDVE----TATFPgfptdlqpqlMVLLSLIPGrSSIT-ENVFK--- 333
Cdd:PRK02427  202 LRMLRAFGVEVENVEGwgyrRIVIKGGQRLRGQDITVPgdpsSAAFF----------LAAAAITGG-SEVTiTNVGLnst 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 334 ---TRFnhVDELNRMGAKIFVESNTAIITGVTKL--SGAPLEATDLRASA------ALLIASLIADGETVINNVDHIfRG 402
Cdd:PRK02427  271 qggKAI--IDVLEKMGADIEIENEREGGEPVGDIrvRSSELKGIDIDIPDiideapTLAVLAAFAEGTTVIRNAEEL-RV 347
                         250       260
                  ....*....|....*....|....
gi 1176198887 403 YEK-----LFEKLEKLGLKIEYYE 421
Cdd:PRK02427  348 KETdriaaMATELRKLGAEVEETE 371
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
14-413 2.32e-04

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 43.20  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  14 GEITISGSKNSALPILAATLLTDEDIILHNIPNLADVNTMIEILENAGKKIT--WNDSSLIIKGCSeinSVLPYGPVRRM 91
Cdd:PLN02338   14 GTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEedSENNRAVVEGCG---GKFPVSGDSKE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887  92 RASFnVLG-------PLTirngyAKVALPGGCSI----GV-----RPVNFHLEGLKKLGIDSKIEHGfTNSKFTRTR--- 152
Cdd:PLN02338   91 DVEL-FLGnagtamrPLT-----AAVTAAGGNASyvldGVprmreRPIGDLVDGLKQLGADVECTLG-TNCPPVRVNaag 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 153 ---GEKIHISLPFPSVGATEHLITTATLLGNTETILTNCAQEPEIVDLCNFLIS-MGAKIEGHGT-SNIKIHGVEKLSGA 227
Cdd:PLN02338  164 glpGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMErFGVSVEHSDSwDRFFIKGGQKYKSP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 228 EYTIIPDRIEAGTYAILGA-VLGERVVLNNVIEDHL-----FAllDIFEKIGVRYEFIDNKLIING-----ISKLELSPI 296
Cdd:PLN02338  244 GNAYVEGDASSASYFLAGAaITGGTVTVEGCGTTSLqgdvkFA--EVLEKMGAKVEWTENSVTVTGpprdaFGGKHLKAI 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 297 DVETATFPgfptDLQPQLMVLLSLIPGRSSItENVFKTRFNH-------VDELNRMGAKIFVESNTAIITGVTKLSGAPL 369
Cdd:PLN02338  322 DVNMNKMP----DVAMTLAVVALFADGPTAI-RDVASWRVKEtermiaiCTELRKLGATVEEGPDYCIITPPKKLKPAEI 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1176198887 370 EA-TDLRASAALliaSLIADGET--VINNVDHIFRGYEKLFEKLEKL 413
Cdd:PLN02338  397 DTyDDHRMAMAF---SLAACGDVpvTINDPGCTRKTFPTYFDVLESI 440
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
204-421 1.08e-03

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 41.52  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 204 MGAKIEG--HGTSNIKIHGVEKLSGAEYTIIPDRIEAGTYAILGAVLGErvVLNNVIE-----DHLFALLDIFekiGVRY 276
Cdd:PRK14806  435 MGAVIETgeEGRPPLSIRGGQRLKGIHYDLPMASAQVKSCLLLAGLYAE--GETSVTEpaptrDHTERMLRGF---GYPV 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 277 EFIDNKLIINGISKLELSPIDV----ETATFpgfptdlqpqLMVLLSLIPGRSSITENV--FKTRFNHVDELNRMGAKIF 350
Cdd:PRK14806  510 KVEGNTISVEGGGKLTATDIEVpadiSSAAF----------FLVAASIAEGSELTLEHVgiNPTRTGVIDILKLMGADIT 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198887 351 VEsNTAIITG--VTKLS--GAPLEATDLRAS---------AALLIASLIADGETVINNVDHIfRGYEK-----LFEKLEK 412
Cdd:PRK14806  580 LE-NEREVGGepVADIRvrGARLKGIDIPEDqvplaidefPVLFVAAACAEGRTVLTGAEEL-RVKESdriqvMADGLKT 657

                  ....*....
gi 1176198887 413 LGLKIEYYE 421
Cdd:PRK14806  658 LGIDCEPTP 666
 
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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