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Protein

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene

murA

Organism
Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine (PubMed:20392080, PubMed:22378791). Target for the antibiotic fosfomycin.2 Publications

Catalytic activityi

Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.UniRule annotation2 Publications

Enzyme regulationi

In vitro inhibited by covalent binding of fosfomycin and the fungal product terreic acid in the presence of substrate UDP-N-acetylglucosamine, with an inactivation rate constant of 130 M(-1)s(-1) for terreic acid.1 Publication

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei91UDP-N-acetylglucosamineUniRule annotation1
Active sitei115Proton donorCombined sources2 Publications1
Binding sitei305UDP-N-acetylglucosamineCombined sources2 Publications1
Binding sitei327UDP-N-acetylglucosamine; via carbonyl oxygenCombined sources2 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Pyruvate

Enzyme and pathway databases

BRENDAi2.5.1.7. 155.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylglucosamine 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.7UniRule annotation)
Alternative name(s):
Enoylpyruvate transferaseUniRule annotation
UDP-N-acetylglucosamine enolpyruvyl transferaseUniRule annotation
Short name:
EPTUniRule annotation
Gene namesi
Name:murAUniRule annotation
Synonyms:murZ
Ordered Locus Names:ECL_04571
OrganismiEnterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)
Taxonomic identifieri716541 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex
Proteomesi
  • UP000002363 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi115C → D: Significantly lower binding of phosphoenolpyruvate. 1 Publication1
Mutagenesisi115C → S: Loss of activity, but not of substrate binding. 1
Mutagenesisi120R → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001788731 – 419UDP-N-acetylglucosamine 1-carboxyvinyltransferaseAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1152-(S-cysteinyl)pyruvic acid O-phosphothioketal1 Publication1

Interactioni

Protein-protein interaction databases

STRINGi716541.ECL_04571.

Chemistry databases

BindingDBiP33038.

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Beta strandi13 – 17Combined sources5
Helixi22 – 31Combined sources10
Helixi32 – 34Combined sources3
Beta strandi35 – 37Combined sources3
Beta strandi39 – 43Combined sources5
Helixi48 – 59Combined sources12
Beta strandi63 – 65Combined sources3
Beta strandi70 – 73Combined sources4
Helixi84 – 87Combined sources4
Helixi91 – 96Combined sources6
Helixi97 – 104Combined sources8
Beta strandi105 – 110Combined sources6
Beta strandi114 – 116Combined sources3
Turni117 – 119Combined sources3
Helixi120 – 122Combined sources3
Helixi123 – 131Combined sources9
Beta strandi135 – 139Combined sources5
Beta strandi142 – 146Combined sources5
Beta strandi148 – 150Combined sources3
Beta strandi155 – 157Combined sources3
Helixi163 – 173Combined sources11
Beta strandi176 – 183Combined sources8
Helixi189 – 200Combined sources12
Beta strandi204 – 206Combined sources3
Beta strandi210 – 216Combined sources7
Beta strandi224 – 227Combined sources4
Helixi232 – 243Combined sources12
Turni244 – 246Combined sources3
Beta strandi248 – 253Combined sources6
Helixi256 – 258Combined sources3
Helixi260 – 268Combined sources9
Beta strandi272 – 275Combined sources4
Beta strandi277 – 283Combined sources7
Beta strandi293 – 295Combined sources3
Helixi304 – 306Combined sources3
Helixi307 – 315Combined sources9
Beta strandi317 – 324Combined sources8
Beta strandi326 – 328Combined sources3
Turni329 – 333Combined sources5
Helixi334 – 340Combined sources7
Beta strandi344 – 348Combined sources5
Beta strandi351 – 355Combined sources5
Beta strandi364 – 366Combined sources3
Helixi370 – 382Combined sources13
Beta strandi383 – 389Combined sources7
Helixi393 – 398Combined sources6
Beta strandi399 – 401Combined sources3
Helixi402 – 407Combined sources6
Turni408 – 410Combined sources3
Beta strandi412 – 417Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DLGX-ray1.90A/B1-419[»]
1EJCX-ray1.80A1-419[»]
1EJDX-ray1.55A/B1-419[»]
1EYNX-ray1.70A1-419[»]
1NAWX-ray2.00A/B1-419[»]
1Q3GX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L/W/X/Y/Z1-419[»]
1RYWX-ray2.30A/B/C/D/E/F/G/H1-419[»]
1YBGX-ray2.60A/B/C/D1-419[»]
3KQAX-ray2.25A/B/C/D1-419[»]
3LTHX-ray1.75A1-419[»]
3SPBX-ray2.30A/B/C/D1-419[»]
3SU9X-ray2.20A1-419[»]
3SWAX-ray1.90A/B1-419[»]
3SWIX-ray2.80A1-419[»]
3SWQX-ray1.83A1-419[»]
3UPKX-ray2.00A1-419[»]
3V4TX-ray2.50A/B/C/D/E/F/G/H1-419[»]
3V5VX-ray2.70A/B/C/D1-419[»]
4E7BX-ray2.00A/B/C/D1-419[»]
4E7CX-ray2.10A/B/C/D1-419[»]
4E7DX-ray2.50A/B/C/D1-419[»]
4E7EX-ray2.30A/B/C/D1-419[»]
4E7FX-ray2.15A/B/C/D1-419[»]
4E7GX-ray1.60A1-419[»]
4EIIX-ray1.95A1-419[»]
ProteinModelPortaliP33038.
SMRiP33038.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33038.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 23Phosphoenolpyruvate bindingCombined sources1 Publication2
Regioni120 – 124UDP-N-acetylglucosamine bindingCombined sources2 Publications5
Regioni160 – 163UDP-N-acetylglucosamine bindingCombined sources1 Publication4

Sequence similaritiesi

Belongs to the EPSP synthase family. MurA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDF. Bacteria.
COG0766. LUCA.
HOGENOMiHOG000075602.
KOiK00790.
OMAiIRTAPHP.
OrthoDBiPOG091H01PG.

Family and domain databases

CDDicd01555. UdpNAET. 1 hit.
Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00111. MurA. 1 hit.
InterProiIPR001986. Enolpyruvate_Tfrase_dom.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view]
PfamiPF00275. EPSP_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01072. murA. 1 hit.

Sequencei

Sequence statusi: Complete.

P33038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKFRVQGPT RLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDI
60 70 80 90 100
DTTMKLLTQL GTKVERNGSV WIDASNVNNF SAPYDLVKTM RASIWALGPL
110 120 130 140 150
VARFGQGQVS LPGGCAIGAR PVDLHIFGLE KLGAEIKLEE GYVKASVNGR
160 170 180 190 200
LKGAHIVMDK VSVGATVTIM SAATLAEGTT IIENAAREPE IVDTANFLVA
210 220 230 240 250
LGAKISGQGT DRITIEGVER LGGGVYRVLP DRIETGTFLV AAAISGGKIV
260 270 280 290 300
CRNAQPDTLD AVLAKLREAG ADIETGEDWI SLDMHGKRPK AVTVRTAPHP
310 320 330 340 350
AFPTDMQAQF TLLNLVAEGT GVITETIFEN RFMHVPELIR MGAHAEIESN
360 370 380 390 400
TVICHGVEKL SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE
410
RIEDKLRALG ANIERVKGE
Length:419
Mass (Da):44,777
Last modified:October 1, 1993 - v1
Checksum:i19C976B098245A68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11835 Genomic DNA. Translation: CAA77856.1.
CP001918 Genomic DNA. Translation: ADF64099.1.
PIRiS22372.
RefSeqiWP_013098931.1. NC_014121.1.
YP_003615048.1. NC_014121.1.

Genome annotation databases

EnsemblBacteriaiADF64099; ADF64099; ECL_04571.
GeneIDi9127042.
KEGGienc:ECL_04571.
PATRICi38460057. VBIEntClo148801_4720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11835 Genomic DNA. Translation: CAA77856.1.
CP001918 Genomic DNA. Translation: ADF64099.1.
PIRiS22372.
RefSeqiWP_013098931.1. NC_014121.1.
YP_003615048.1. NC_014121.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DLGX-ray1.90A/B1-419[»]
1EJCX-ray1.80A1-419[»]
1EJDX-ray1.55A/B1-419[»]
1EYNX-ray1.70A1-419[»]
1NAWX-ray2.00A/B1-419[»]
1Q3GX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L/W/X/Y/Z1-419[»]
1RYWX-ray2.30A/B/C/D/E/F/G/H1-419[»]
1YBGX-ray2.60A/B/C/D1-419[»]
3KQAX-ray2.25A/B/C/D1-419[»]
3LTHX-ray1.75A1-419[»]
3SPBX-ray2.30A/B/C/D1-419[»]
3SU9X-ray2.20A1-419[»]
3SWAX-ray1.90A/B1-419[»]
3SWIX-ray2.80A1-419[»]
3SWQX-ray1.83A1-419[»]
3UPKX-ray2.00A1-419[»]
3V4TX-ray2.50A/B/C/D/E/F/G/H1-419[»]
3V5VX-ray2.70A/B/C/D1-419[»]
4E7BX-ray2.00A/B/C/D1-419[»]
4E7CX-ray2.10A/B/C/D1-419[»]
4E7DX-ray2.50A/B/C/D1-419[»]
4E7EX-ray2.30A/B/C/D1-419[»]
4E7FX-ray2.15A/B/C/D1-419[»]
4E7GX-ray1.60A1-419[»]
4EIIX-ray1.95A1-419[»]
ProteinModelPortaliP33038.
SMRiP33038.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi716541.ECL_04571.

Chemistry databases

BindingDBiP33038.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADF64099; ADF64099; ECL_04571.
GeneIDi9127042.
KEGGienc:ECL_04571.
PATRICi38460057. VBIEntClo148801_4720.

Phylogenomic databases

eggNOGiENOG4105CDF. Bacteria.
COG0766. LUCA.
HOGENOMiHOG000075602.
KOiK00790.
OMAiIRTAPHP.
OrthoDBiPOG091H01PG.

Enzyme and pathway databases

UniPathwayiUPA00219.
BRENDAi2.5.1.7. 155.

Miscellaneous databases

EvolutionaryTraceiP33038.
PROiP33038.

Family and domain databases

CDDicd01555. UdpNAET. 1 hit.
Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00111. MurA. 1 hit.
InterProiIPR001986. Enolpyruvate_Tfrase_dom.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view]
PfamiPF00275. EPSP_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01072. murA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMURA_ENTCC
AccessioniPrimary (citable) accession number: P33038
Secondary accession number(s): D5CCD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 2, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.