P0A750 (MURA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

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:	c3947

Organism

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

199310 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine By similarity. 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
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00111
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the EPSP synthase family. MurA subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete 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 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...

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_0000178872
Sites
	Active site	115	1	Proton donor
Amino acid modifications
	Modified residue	115	1	2-(S-cysteinyl)pyruvic acid O-phosphothioketal By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A750 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 6B75A842255E53F7	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

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CFT073 / ATCC 700928 / UPEC.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN82387.1.
RefSeq	NP_755813.1. NC_004431.1.
3D structure databases
ProteinModelPortal	P0A750.
SMR	P0A750. Positions 1-419.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1224921.
STRING	199310.c3947.
Proteomic databases
PRIDE	P0A750.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN82387; AAN82387; c3947.
GeneID	1040304.
KEGG	ecc:c3947.
PATRIC	18285672. VBIEscCol75197_3716.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000075602.
KO	K00790.
OMA	SIWALAP.
ProtClustDB	PRK09369.
Enzyme and pathway databases
UniPathway	UPA00219.
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	P0A750.

Entry information

Entry name

MURA_ECOL6

Accession

Primary (citable) accession number: P0A750
Secondary accession number(s): P28909

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program