Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911UDP-N-acetylglucosamineUniRule annotation
Active sitei115 – 1151Proton donorCombined sources2 Publications
Binding sitei305 – 3051UDP-N-acetylglucosamineCombined sources2 Publications
Binding sitei327 – 3271UDP-N-acetylglucosamine; via carbonyl oxygenCombined sources2 Publications

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

BioCyciECLO716541:GH13-4626-MONOMER.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi115 – 1151C → D: Significantly lower binding of phosphoenolpyruvate. 1 Publication
Mutagenesisi115 – 1151C → S: Loss of activity, but not of substrate binding.
Mutagenesisi120 – 1201R → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419UDP-N-acetylglucosamine 1-carboxyvinyltransferasePRO_0000178873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 11512-(S-cysteinyl)pyruvic acid O-phosphothioketal1 Publication

Interactioni

Protein-protein interaction databases

STRINGi716541.ECL_04571.

Chemistry

BindingDBiP33038.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi13 – 175Combined sources
Helixi22 – 3110Combined sources
Helixi32 – 343Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 435Combined sources
Helixi48 – 5912Combined sources
Beta strandi63 – 653Combined sources
Beta strandi70 – 734Combined sources
Helixi84 – 874Combined sources
Helixi91 – 966Combined sources
Helixi97 – 1048Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi114 – 1163Combined sources
Turni117 – 1193Combined sources
Helixi120 – 1223Combined sources
Helixi123 – 1319Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi142 – 1465Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi155 – 1573Combined sources
Helixi163 – 17311Combined sources
Beta strandi176 – 1838Combined sources
Helixi189 – 20012Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi210 – 2167Combined sources
Beta strandi224 – 2274Combined sources
Helixi232 – 24312Combined sources
Turni244 – 2463Combined sources
Beta strandi248 – 2536Combined sources
Helixi256 – 2583Combined sources
Helixi260 – 2689Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi277 – 2837Combined sources
Beta strandi293 – 2953Combined sources
Helixi304 – 3063Combined sources
Helixi307 – 3159Combined sources
Beta strandi317 – 3248Combined sources
Beta strandi326 – 3283Combined sources
Turni329 – 3335Combined sources
Helixi334 – 3407Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi351 – 3555Combined sources
Beta strandi364 – 3663Combined sources
Helixi370 – 38213Combined sources
Beta strandi383 – 3897Combined sources
Helixi393 – 3986Combined sources
Beta strandi399 – 4013Combined sources
Helixi402 – 4076Combined sources
Turni408 – 4103Combined sources
Beta strandi412 – 4176Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33038.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 232Phosphoenolpyruvate bindingCombined sources1 Publication
Regioni120 – 1245UDP-N-acetylglucosamine bindingCombined sources2 Publications
Regioni160 – 1634UDP-N-acetylglucosamine bindingCombined sources1 Publication

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

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
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. Positions 1-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi716541.ECL_04571.

Chemistry

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.
BioCyciECLO716541:GH13-4626-MONOMER.
BRENDAi2.5.1.7. 155.

Miscellaneous databases

EvolutionaryTraceiP33038.
PROiP33038.

Family and domain databases

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: September 7, 2016
This is version 127 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.