UDP-N-acetylglucosamine 1-carboxyvinyltransferase - Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)

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P33038 (MURA_ENTCC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. History...

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

Documents (3) |

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:	ECL_04571

Organism

Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56) [Complete proteome] [HAMAP]

Taxonomic identifier

716541 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex

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 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	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 cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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: EC
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 MF_00111

PRO_0000178873

Sites

Active site

115

Proton donor

Amino acid modifications

Modified residue

115

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

Experimental info

Mutagenesis

115

C → S: Loss of activity, but not of substrate binding.

Secondary structure

419

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P33038 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 19C976B098245A68
Show »

FASTA

419

44,777

        10         20         30         40         50         60 
MDKFRVQGPT RLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDI DTTMKLLTQL 

        70         80         90        100        110        120 
GTKVERNGSV WIDASNVNNF SAPYDLVKTM RASIWALGPL VARFGQGQVS LPGGCAIGAR 

       130        140        150        160        170        180 
PVDLHIFGLE KLGAEIKLEE GYVKASVNGR LKGAHIVMDK VSVGATVTIM SAATLAEGTT 

       190        200        210        220        230        240 
IIENAAREPE IVDTANFLVA LGAKISGQGT DRITIEGVER LGGGVYRVLP DRIETGTFLV 

       250        260        270        280        290        300 
AAAISGGKIV CRNAQPDTLD AVLAKLREAG ADIETGEDWI SLDMHGKRPK AVTVRTAPHP 

       310        320        330        340        350        360 
AFPTDMQAQF TLLNLVAEGT GVITETIFEN RFMHVPELIR MGAHAEIESN TVICHGVEKL 

       370        380        390        400        410 
SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE RIEDKLRALG ANIERVKGE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The UDP-N-acetylglucosamine 1-carboxyvinyl-transferase of Enterobacter cloacae. Molecular cloning, sequencing of the gene and overexpression of the enzyme." Wanke C., Falchetto R., Amrhein N. FEBS Lett. 301:271-276(1992) [PubMed: 1577165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Complete genome sequence of Enterobacter cloacae subsp. cloacae type strain ATCC 13047." Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L. J. Bacteriol. 192:2463-2464(2010) [PubMed: 20207761] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56.
[3]	"Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin." Schoenbrunn E., Sack S., Eschenburg S., Perrakis A., Krekel N., Mandelkow E. Structure 4:1065-1075(1996) [PubMed: 8805592] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[4]	"Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme murA." Schoenbrunn E., Eschenburg S., Krekel F., Luger K., Amrhein N. Biochemistry 39:2164-2173(2000) [PubMed: 10694381] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANT SER-115.
[5]	"Comparative X-ray analysis of the un-liganded fosfomycin-target murA." Eschenburg S., Schoenbrunn E. Proteins 40:290-298(2000) [PubMed: 10842342] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z11835 Genomic DNA. Translation: CAA77856.1.
CP001918 Genomic DNA. Translation: ADF64099.1.

PIR

S22372.

RefSeq

YP_003615048.1. NC_014121.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DLG	X-ray	1.90	A/B	1-419	[»]
1EJC	X-ray	1.80	A	1-419	[»]
1EJD	X-ray	1.55	A/B	1-419	[»]
1EYN	X-ray	1.70	A	1-419	[»]
1NAW	X-ray	2.00	A/B	1-419	[»]
1Q3G	X-ray	2.65	A/B/C/D/E/F/G/H/I/J/K/L/W/X/Y/Z	1-419	[»]
1RYW	X-ray	2.30	A/B/C/D/E/F/G/H	1-419	[»]
1YBG	X-ray	2.60	A/B/C/D	1-419	[»]
3KQA	X-ray	2.25	A/B/C/D	1-419	[»]
3LTH	X-ray	1.75	A	1-419	[»]

ProteinModelPortal

P33038.

SMR

P33038. Positions 1-419.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

9127042.

GenomeReviews

Gene locus ECL_04571 in contig CP001918_GR.

KEGG

enc:ECL_04571.

PATRIC

38460057. VBIEntClo148801_4720.

Organism-specific databases

CMR

Search...

Phylogenomic databases

ProtClustDB

PRK09369.

Family and domain databases

HAMAP

MF_00111. MurA.
[Tree]

InterPro

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

Gene3D

G3DSA:3.65.10.10. EPSP_synthase. 2 hits.

K00790.

PANTHER

PTHR21090:SF4. AcGlu_Tran_MurA. 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...

Entry information

Entry name

MURA_ENTCC

Accession

Primary (citable) accession number: P33038
Secondary accession number(s): D5CCD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	January 25, 2012
This is version 92 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

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

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents