SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A749

- MURA_ECOLI

UniProt

P0A749 - MURA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene
murA, murZ, b3189, JW3156
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic fosfomycin.1 Publication

Catalytic activityi

Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.1 Publication

Enzyme regulationi

Competitively inhibited by UDP-N-acetylglucosamine 3'-phosphate, with a Ki of 7 µM.1 Publication

Kineticsi

  1. KM=15 µM for UDP-N-acetylglucosamine1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei115 – 1151Proton donor

GO - Molecular functioni

  1. UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity Source: EcoCyc

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. peptidoglycan biosynthetic process Source: EcoCyc
  4. regulation of cell shape Source: UniProtKB-KW
  5. UDP-N-acetylgalactosamine biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Pyruvate

Enzyme and pathway databases

BioCyciEcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
ECOL316407:JW3156-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
BRENDAi2.5.1.7. 2026.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
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 namesi
Name:murA
Synonyms:murZ
Ordered Locus Names:b3189, JW3156
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11358. murA.

Subcellular locationi

Cytoplasm Inferred UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419UDP-N-acetylglucosamine 1-carboxyvinyltransferaseUniRule annotationPRO_0000178870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 11512-(S-cysteinyl)pyruvic acid O-phosphothioketalUniRule annotation

Proteomic databases

PaxDbiP0A749.
PRIDEiP0A749.

Expressioni

Gene expression databases

GenevestigatoriP0A749.

Interactioni

Protein-protein interaction databases

DIPiDIP-48060N.
IntActiP0A749. 23 interactions.
MINTiMINT-1224932.
STRINGi511145.b3189.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Beta strandi14 – 174
Helixi22 – 3110
Helixi32 – 343
Beta strandi35 – 373
Beta strandi39 – 435
Helixi48 – 5912
Beta strandi63 – 653
Beta strandi70 – 734
Helixi74 – 763
Helixi84 – 874
Helixi92 – 965
Helixi97 – 1048
Beta strandi105 – 1106
Beta strandi116 – 1183
Helixi123 – 1319
Beta strandi135 – 1395
Beta strandi142 – 1465
Beta strandi148 – 1503
Beta strandi155 – 1573
Helixi163 – 17311
Beta strandi176 – 1849
Helixi189 – 20012
Beta strandi204 – 2063
Beta strandi210 – 2167
Beta strandi224 – 2274
Helixi232 – 24514
Beta strandi248 – 2536
Helixi256 – 2583
Helixi260 – 2689
Beta strandi272 – 2754
Beta strandi277 – 2837
Beta strandi293 – 2953
Helixi304 – 3063
Helixi307 – 31610
Beta strandi317 – 3248
Beta strandi326 – 3283
Turni329 – 3335
Helixi334 – 3396
Turni340 – 3423
Beta strandi344 – 3485
Beta strandi351 – 3555
Beta strandi364 – 3663
Helixi370 – 38213
Beta strandi383 – 3908
Helixi392 – 3976
Beta strandi399 – 4013
Helixi402 – 4087
Beta strandi412 – 4176

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2NX-ray2.80A1-419[»]
1UAEX-ray1.80A1-419[»]
2Z2CX-ray2.05A/B/C/D1-419[»]
3ISSX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
3KQJX-ray1.70A1-419[»]
3KR6X-ray1.70A1-419[»]
3SWDX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
ProteinModelPortaliP0A749.
SMRiP0A749. Positions 1-419.

Miscellaneous databases

EvolutionaryTraceiP0A749.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0766.
HOGENOMiHOG000075602.
KOiK00790.
OMAiHGLEQMG.
OrthoDBiEOG68M4GK.
PhylomeDBiP0A749.

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00111. MurA.
InterProiIPR001986. Enolpyruvate_Tfrase_dom.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view]
PANTHERiPTHR21090:SF4. PTHR21090:SF4. 1 hit.
PfamiPF00275. EPSP_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01072. murA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A749-1 [UniParc]FASTAAdd to Basket

« Hide

MDKFRVQGPT KLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV    50
DTSMKLLSQL GAKVERNGSV HIDARDVNVF CAPYDLVKTM RASIWALGPL 100
VARFGQGQVS LPGGCTIGAR PVDLHISGLE QLGATIKLEE GYVKASVDGR 150
LKGAHIVMDK VSVGATVTIM CAATLAEGTT IIENAAREPE IVDTANFLIT 200
LGAKISGQGT DRIVIEGVER LGGGVYRVLP DRIETGTFLV AAAISRGKII 250
CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP 300
AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGAHAEIESN 350
TVICHGVEKL SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE 400
RIEDKLRALG ANIERVKGE 419
Length:419
Mass (Da):44,818
Last modified:June 7, 2005 - v1
Checksum:i6B75A842255E53F7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA44917.
RefSeqiNP_417656.1. NC_000913.3.
YP_491374.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76221; AAC76221; b3189.
BAE77233; BAE77233; BAE77233.
GeneIDi12933444.
947703.
KEGGiecj:Y75_p3109.
eco:b3189.
PATRICi32121798. VBIEscCol129921_3283.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A44917.
RefSeqi NP_417656.1. NC_000913.3.
YP_491374.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0A749.
SMRi P0A749. Positions 1-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48060N.
IntActi P0A749. 23 interactions.
MINTi MINT-1224932.
STRINGi 511145.b3189.

Chemistry

BindingDBi P0A749.
ChEMBLi CHEMBL1984.
DrugBanki DB00828. Fosfomycin.

Proteomic databases

PaxDbi P0A749.
PRIDEi P0A749.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76221 ; AAC76221 ; b3189 .
BAE77233 ; BAE77233 ; BAE77233 .
GeneIDi 12933444.
947703.
KEGGi ecj:Y75_p3109.
eco:b3189.
PATRICi 32121798. VBIEscCol129921_3283.

Organism-specific databases

EchoBASEi EB1333.
EcoGenei EG11358. murA.

Phylogenomic databases

eggNOGi COG0766.
HOGENOMi HOG000075602.
KOi K00790.
OMAi HGLEQMG.
OrthoDBi EOG68M4GK.
PhylomeDBi P0A749.

Enzyme and pathway databases

UniPathwayi UPA00219 .
BioCyci EcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
ECOL316407:JW3156-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
BRENDAi 2.5.1.7. 2026.

Miscellaneous databases

EvolutionaryTracei P0A749.
PROi P0A749.

Gene expression databases

Genevestigatori P0A749.

Family and domain databases

Gene3Di 3.65.10.10. 2 hits.
HAMAPi MF_00111. MurA.
InterProi IPR001986. Enolpyruvate_Tfrase_dom.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view ]
PANTHERi PTHR21090:SF4. PTHR21090:SF4. 1 hit.
Pfami PF00275. EPSP_synthase. 1 hit.
[Graphical view ]
SUPFAMi SSF55205. SSF55205. 1 hit.
TIGRFAMsi TIGR01072. murA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    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. 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).

Entry informationi

Entry nameiMURA_ECOLI
AccessioniPrimary (citable) accession number: P0A749
Secondary accession number(s): P28909, Q2M923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi