UDP-N-acetylglucosamine 1-carboxyvinyltransferase

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P0A749 (MURA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=15 µM for UDP-N-acetylglucosamine Ref.5

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 Reference proteome
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 peptidoglycan biosynthetic process Inferred from mutant phenotype PubMed 4555418. Source: EcoCyc 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 direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

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-Rule MF_00111

PRO_0000178870

Sites

Active site

115

Proton donor

Amino acid modifications

Modified residue

115

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

Secondary structure

419

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A749 [UniParc].

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

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

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] [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 277:1453-1474(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.

PIR

A44917.

RefSeq

NP_417656.1. NC_000913.2.
YP_491374.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3ISS	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	1-418	[»]
3KQJ	X-ray	1.70	A	1-419	[»]
3KR6	X-ray	1.70	A	1-419	[»]
3SWD	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	1-418	[»]

ProteinModelPortal

P0A749.

SMR

P0A749. Positions 1-419.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48060N.

IntAct

P0A749. 20 interactions.

MINT

MINT-1224932.

STRING

511145.b3189.

Proteomic databases

PaxDb

P0A749.

PRIDE

P0A749.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76221; AAC76221; b3189.
BAE77233; BAE77233; BAE77233.

GeneID

12933444.
947703.

KEGG

ecj:Y75_p3109.
eco:b3189.

PATRIC

32121798. VBIEscCol129921_3283.

Organism-specific databases

EchoBASE

EB1333.

EcoGene

EG11358. murA.

Phylogenomic databases

eggNOG

COG0766.

HOGENOM

HOG000075602.

K00790.

OMA

SIWALAP.

ProtClustDB

PRK09369.

Enzyme and pathway databases

BioCyc

EcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
ECOL316407:JW3156-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.

BRENDA

2.5.1.7. 2026.

UniPathway

UPA00219.

Gene expression databases

Genevestigator

P0A749.

Family and domain databases

Gene3D

3.65.10.10. 2 hits.

HAMAP

MF_00111. MurA.

InterPro

IPR001986. Enolpyruvate_Tfrase_dom.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view]

PANTHER

PTHR21090:SF4. PTHR21090:SF4. 1 hit.

Pfam

PF00275. EPSP_synthase. 1 hit.
[Graphical view]

SUPFAM

SSF55205. RNA3'_cycl/enolpyr_transf_A/B. 1 hit.

TIGRFAMs

TIGR01072. murA. 1 hit.

ProtoNet

Search...

Other

BindingDB

P0A749.

ChEMBL

CHEMBL1984.

DrugBank

DB00828. Fosfomycin.

EvolutionaryTrace

P0A749.

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:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents