Reviewed, UniProtKB/Swiss-Prot Q4L7Y1 (MURA2_STAHJ)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2
    EC=2.5.1.7
Alternative name(s):
    Enoylpyruvate transferase 2
    UDP-N-acetylglucosamine enolpyruvyl transferase 2
      Short name=EPT 2

Gene names

Name:	murA2
Synonyms:	murA
Ordered Locus Names:	SH0935

Organism

Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]

Taxonomic identifier

279808 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	421 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 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 HAMAP MF_00111.
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 cellular 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 421	421	UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2 HAMAP MF_00111		PRO_0000231267
Sites
	Active site	119	1	Proton donor By similarity
	Binding site	119	1	Phosphoenolpyruvate (covalent) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4L7Y1-1 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: 94F97448C28A9CCB	FASTA	421	45,236
	10 20 30 40 50 60 MDKIVIKGGN RLTGEVKVEG AKNAVLPVLT ASLLASEGQS KLVNVPDLSD VVTINNVLST 70 80 90 100 110 120 LNANVEYNKE EGAVLVDAST TLKEEAPYEY VSKMRASILV MGPLLARLGH AIVALPGGCA 130 140 150 160 170 180 IGARPIEQHI KGFEALGAEI HLENGNIYAS TKDGLKGTDI HLDFPSVGAT QNIIMAASLA 190 200 210 220 230 240 KGKTVIENVA KEPEIVDLAN YINEMGGKVT GAGTDTITIH GVEKLRGVEH SIIPDRIEAG 250 260 270 280 290 300 TLIIAAAITR GDVFVRDAVK EHMTSLIYKL EEMGVNLDFQ EDGVRVTAED ELKPVDVKTL 310 320 330 340 350 360 PHPGFPTDMQ SQMIALLLTA EGHKVITETV FENRFMHVAE FRRMNANITV EGRSAKIQGK 370 380 390 400 410 420 SQLQGAQVKA TDLRAAAALI LAGLVAEGTT QVTELKHLDR GYVNFHEKLK SLGANIERVN Y

References

[1]

"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006716 Genomic DNA. Translation: BAE04244.1.
RefSeq	YP_252850.1.
3D structure databases
SMR	Q4L7Y1. Positions 1-420.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4L7Y1.
Genome annotation databases
GeneID	3482070.
GenomeReviews	Gene locus SH0935 in contig AP006716_GR.
KEGG	sha:SH0935.
NMPDR	fig|279808.3.peg.1287.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0766.
HOGENOM	HBG482701.
OMA	VSRVYHL.
PhylomeDB	Q4L7Y1.
Enzyme and pathway databases
BioCyc	SHAE279808:SH0935-MONOMER.
Family and domain databases
HAMAP	MF_00111. MurA. [Tree]
InterPro	IPR001986. EPSP_synthase_core. IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b. IPR005750. UDP_GlcNAc_COvinyl_MurA. [Graphical view]
Gene3D	G3DSA:3.65.10.10. EPSP_synthase. 1 hit.
PANTHER	PTHR21090:SF4. AcGlu_Tran_MurA. 1 hit.
Pfam	PF00275. EPSP_synthase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01072. murA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURA2_STAHJ

Accession

Primary (citable) accession number: Q4L7Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	August 2, 2005
Last modified:	February 9, 2010
This is version 38 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)