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P0A749

- MURA_ECOLI

UniProt

P0A749 - MURA_ECOLI

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Protein

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene

murA

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 PublicationUniRule annotation

Catalytic activityi

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

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. cell wall organization Source: UniProtKB-KW
  4. peptidoglycan biosynthetic process Source: EcoCyc
  5. regulation of cell shape Source: UniProtKB-KW
  6. 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-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.7UniRule annotation)
Alternative name(s):
Enoylpyruvate transferaseUniRule annotation
UDP-N-acetylglucosamine enolpyruvyl transferaseUniRule annotation
Short name:
EPTUniRule annotation
Gene namesi
Name:murAUniRule annotation
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 Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419UDP-N-acetylglucosamine 1-carboxyvinyltransferasePRO_0000178870Add
BLAST

Amino acid modifications

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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A749.

Family & Domainsi

Sequence similaritiesi

Belongs to the EPSP synthase family. MurA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0766.
HOGENOMiHOG000075602.
InParanoidiP0A749.
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

        10         20         30         40         50
MDKFRVQGPT KLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV
60 70 80 90 100
DTSMKLLSQL GAKVERNGSV HIDARDVNVF CAPYDLVKTM RASIWALGPL
110 120 130 140 150
VARFGQGQVS LPGGCTIGAR PVDLHISGLE QLGATIKLEE GYVKASVDGR
160 170 180 190 200
LKGAHIVMDK VSVGATVTIM CAATLAEGTT IIENAAREPE IVDTANFLIT
210 220 230 240 250
LGAKISGQGT DRIVIEGVER LGGGVYRVLP DRIETGTFLV AAAISRGKII
260 270 280 290 300
CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP
310 320 330 340 350
AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGAHAEIESN
360 370 380 390 400
TVICHGVEKL SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE
410
RIEDKLRALG ANIERVKGE
Length:419
Mass (Da):44,818
Last modified:June 7, 2005 - v1
Checksum:i6B75A842255E53F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P0A749.
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: November 26, 2014
This is version 100 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