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P0A749 (MURA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase

EC=2.5.1.7
Alternative name(s):
Enoylpyruvate transferase
UDP-N-acetylglucosamine enolpyruvyl transferase
Short name=EPT
Gene names
Name:murA
Synonyms:murZ
Ordered Locus Names:b3189, JW3156
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin. HAMAP-Rule MF_00111

Catalytic activity

Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine. HAMAP-Rule MF_00111

Enzyme regulation

Competitively inhibited by UDP-N-acetylglucosamine 3'-phosphate, with a Ki of 7 µM. Ref.5

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00111

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00111.

Sequence similarities

Belongs to the EPSP synthase family. MurA subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=15 µM for UDP-N-acetylglucosamine Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419UDP-N-acetylglucosamine 1-carboxyvinyltransferase HAMAP-Rule MF_00111
PRO_0000178870

Sites

Active site1151Proton donor

Amino acid modifications

Modified residue11512-(S-cysteinyl)pyruvic acid O-phosphothioketal HAMAP-Rule MF_00111

Secondary structure

....................................................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A749 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 6B75A842255E53F7

FASTA41944,818
        10         20         30         40         50         60 
MDKFRVQGPT KLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV DTSMKLLSQL 

        70         80         90        100        110        120 
GAKVERNGSV HIDARDVNVF CAPYDLVKTM RASIWALGPL VARFGQGQVS LPGGCTIGAR 

       130        140        150        160        170        180 
PVDLHISGLE QLGATIKLEE GYVKASVDGR LKGAHIVMDK VSVGATVTIM CAATLAEGTT 

       190        200        210        220        230        240 
IIENAAREPE IVDTANFLIT LGAKISGQGT DRIVIEGVER LGGGVYRVLP DRIETGTFLV 

       250        260        270        280        290        300 
AAAISRGKII CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP 

       310        320        330        340        350        360 
AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGAHAEIESN TVICHGVEKL 

       370        380        390        400        410 
SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE RIEDKLRALG ANIERVKGE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase."
Marquardt J.L., Siegele D.A., Kolter R., Walsh C.T.
J. Bacteriol. 174:5748-5752(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: K12 / AB1157.
[2]"Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26."
Horii T., Kimura T., Sato K., Shibayama K., Ohta M.
Antimicrob. Agents Chemother. 43:789-793(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O26 / NGY47.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis."
Mutschler H., Gebhardt M., Shoeman R.L., Meinhart A.
PLoS Biol. 9:E1001033-E1001033(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin."
Skarzynski T., Mistry A., Wonacott A., Hutchinson S.E., Kelly V.A., Duncan K.
Structure 4:1465-1474(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND FOSFOMYCIN.
[7]"Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA."
Skarzynski T., Kim D.H., Lees W.J., Walsh C.T., Duncan K.
Biochemistry 37:2572-2577(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M92358 Genomic DNA. Translation: AAA24187.1.
U18997 Genomic DNA. Translation: AAA57990.1.
U00096 Genomic DNA. Translation: AAC76221.1.
AP009048 Genomic DNA. Translation: BAE77233.1.
AB028039 Genomic DNA. Translation: BAA78107.1.
PIRA44917.
RefSeqNP_417656.1. NC_000913.3.
YP_491374.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2NX-ray2.80A1-419[»]
1UAEX-ray1.80A1-419[»]
2Z2CX-ray2.05A/B/C/D1-419[»]
3ISSX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
3KQJX-ray1.70A1-419[»]
3KR6X-ray1.70A1-419[»]
3SWDX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
ProteinModelPortalP0A749.
SMRP0A749. Positions 1-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48060N.
IntActP0A749. 23 interactions.
MINTMINT-1224932.
STRING511145.b3189.

Chemistry

BindingDBP0A749.
ChEMBLCHEMBL1984.
DrugBankDB00828. Fosfomycin.

Proteomic databases

PaxDbP0A749.
PRIDEP0A749.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76221; AAC76221; b3189.
BAE77233; BAE77233; BAE77233.
GeneID12933444.
947703.
KEGGecj:Y75_p3109.
eco:b3189.
PATRIC32121798. VBIEscCol129921_3283.

Organism-specific databases

EchoBASEEB1333.
EcoGeneEG11358. murA.

Phylogenomic databases

eggNOGCOG0766.
HOGENOMHOG000075602.
KOK00790.
OMAGYEHIED.
OrthoDBEOG68M4GK.
PhylomeDBP0A749.
ProtClustDBPRK09369.

Enzyme and pathway databases

BioCycEcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
ECOL316407:JW3156-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
BRENDA2.5.1.7. 2026.
UniPathwayUPA00219.

Gene expression databases

GenevestigatorP0A749.

Family and domain databases

Gene3D3.65.10.10. 2 hits.
HAMAPMF_00111. MurA.
InterProIPR001986. Enolpyruvate_Tfrase_dom.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view]
PANTHERPTHR21090:SF4. PTHR21090:SF4. 1 hit.
PfamPF00275. EPSP_synthase. 1 hit.
[Graphical view]
SUPFAMSSF55205. SSF55205. 1 hit.
TIGRFAMsTIGR01072. murA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A749.
PROP0A749.

Entry information

Entry nameMURA_ECOLI
AccessionPrimary (citable) accession number: P0A749
Secondary accession number(s): P28909, Q2M923
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene