UDP-N-acetylglucosamine 1-carboxyvinyltransferase

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Reviewed, UniProtKB/Swiss-Prot P0A749 (MURA_ECOLI)

Last modified November 3, 2009. Version 54. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin. HAMAP MF_00111
Catalytic activity	Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine. HAMAP MF_00111
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00111
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the EPSP synthase family. MurA subfamily.

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Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	UDP-N-acetylgalactosamine biosynthetic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 419

419

UDP-N-acetylglucosamine 1-carboxyvinyltransferase HAMAP MF_00111

PRO_0000178870

Sites

Active site

115

Proton donor HAMAP MF_00111

Binding site

115

Phosphoenolpyruvate (covalent) HAMAP MF_00111

Secondary structure

419

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A749-1 [UniParc].

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

419

44,818

        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

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References

	« Hide 'large scale' referencesShow '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: 1512209] [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: 10103182] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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: 8994972] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND FOSFOMYCIN.
[6]	"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: 9485407] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

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Cross-references

Sequence databases

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.

PIR

A44917.

RefSeq

AP_003732.1.
NP_417656.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2N	X-ray	2.80	A	1-419	[»]
1UAE	X-ray	1.80	A	1-419	[»]
2Z2C	X-ray	2.05	A/B/C/D	1-419	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A749.

Genome annotation databases

GeneID

947703.

GenomeReviews

Gene locus JW3156 in contig AP009048_GR.
Gene locus b3189 in contig U00096_GR.

KEGG

ecj:JW3156.
eco:b3189.

Organism-specific databases

EchoBASE

EB1333.

EcoGene

EG11358. murA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A749.

OMA

VSRVYHL.

Enzyme and pathway databases

BioCyc

EcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MON.
MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MON.

BRENDA

2.5.1.7. 246.

Gene expression databases

Genevestigator

P0A749.

Family and domain databases

HAMAP

MF_00111.
[Tree]

InterPro

IPR001986. EPSP_synthase_core.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view]

Gene3D

G3DSA:3.65.10.10. EPSP_synthase. 2 hits.

PANTHER

PTHR21090:SF4. AcGlu_Tran_MurA. 1 hit.

Pfam

PF00275. EPSP_synthase. 1 hit.
[Graphical view]

ProDom

PD001867. EPSP_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01072. murA. 1 hit.

ProtoNet

Search...

Other Resources

DrugBank

DB00828. Fosfomycin.

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Entry information

Entry name

MURA_ECOLI

Accession

Primary (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:	November 3, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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