Reviewed, UniProtKB/Swiss-Prot P33038 (MURA_ENTCL)

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

Organism

Enterobacter cloacae

Taxonomic identifier

550 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 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...

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

1

Proton donor HAMAP MF_00111

Binding site

115

1

Phosphoenolpyruvate (covalent) HAMAP MF_00111

Experimental info

Mutagenesis

115

1

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

Secondary structure

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419

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Beta strand

13 – 17

5

Helix

22 – 31

10

Helix

32 – 34

3

Beta strand

35 – 37

3

Beta strand

39 – 43

5

Helix

48 – 59

12

Beta strand

63 – 73

11

Helix

84 – 87

4

Helix

91 – 96

6

Helix

97 – 104

8

Beta strand

105 – 110

6

Beta strand

115 – 119

5

Helix

123 – 131

9

Beta strand

135 – 139

5

Beta strand

142 – 146

5

Beta strand

148 – 150

3

Beta strand

155 – 160

6

Helix

163 – 173

11

Beta strand

176 – 183

8

Helix

189 – 200

12

Beta strand

204 – 206

3

Beta strand

210 – 216

7

Beta strand

224 – 227

4

Helix

232 – 243

12

Turn

244 – 246

3

Beta strand

248 – 253

6

Helix

256 – 258

3

Helix

260 – 268

9

Beta strand

272 – 275

4

Beta strand

277 – 283

7

Helix

304 – 306

3

Helix

307 – 315

9

Beta strand

317 – 324

8

Helix

334 – 340

7

Beta strand

344 – 348

5

Beta strand

351 – 355

5

Helix

370 – 382

13

Beta strand

383 – 389

7

Helix

393 – 398

6

Helix

402 – 407

6

Turn

408 – 410

3

Beta strand

412 – 417

6

Sequences

	Sequence		Length	Mass (Da)
	P33038-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 19C976B098245A68	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

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. Strain: ATCC 13047 / DSM 30054 / IFO 13535 / JCM 1232 / NCTC 10005.
[2]	"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).
[3]	"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.
[4]	"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

EMBLGenBankDDBJ

Z11835 Genomic DNA. Translation: CAA77856.1.

PIR

S22372.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.5.1.7. 1834.

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...

Entry information

Entry name

MURA_ENTCL

Accession

Primary (citable) accession number: P33038

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 77 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)