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Protein

UDP-N-acetylenolpyruvoylglucosamine reductase

Gene

murB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell wall formation.

Catalytic activityi

UDP-N-acetyl-alpha-D-muramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH.

Cofactori

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591
Binding sitei190 – 1901Substrate
Active sitei229 – 2291Proton donor
Active sitei325 – 3251

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoliWiki
  • UDP-N-acetylmuramate dehydrogenase activity Source: EcoCyc

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cell wall organization Source: EcoliWiki
  • peptidoglycan biosynthetic process Source: EcoliWiki
  • regulation of cell shape Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciEcoCyc:UDPNACETYLMURAMATEDEHYDROG-MONOMER.
ECOL316407:JW3940-MONOMER.
MetaCyc:UDPNACETYLMURAMATEDEHYDROG-MONOMER.
SABIO-RKP08373.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylenolpyruvoylglucosamine reductase (EC:1.3.1.98)
Alternative name(s):
UDP-N-acetylmuramate dehydrogenase
Gene namesi
Name:murB
Synonyms:yijB
Ordered Locus Names:b3972, JW3940
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11205. murB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5526.
DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342UDP-N-acetylenolpyruvoylglucosamine reductasePRO_0000179207Add
BLAST

Proteomic databases

EPDiP08373.
PaxDbiP08373.
PRIDEiP08373.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262982. 592 interactions.
DIPiDIP-10277N.
IntActiP08373. 12 interactions.
MINTiMINT-1275566.
STRINGi511145.b3972.

Chemistry

BindingDBiP08373.

Structurei

Secondary structure

1
342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi16 – 2510Combined sources
Helixi26 – 3813Combined sources
Beta strandi43 – 486Combined sources
Beta strandi52 – 543Combined sources
Beta strandi58 – 658Combined sources
Beta strandi70 – 745Combined sources
Beta strandi76 – 849Combined sources
Helixi89 – 9810Combined sources
Helixi105 – 1073Combined sources
Helixi114 – 1163Combined sources
Turni117 – 1215Combined sources
Helixi129 – 1313Combined sources
Beta strandi133 – 1408Combined sources
Turni141 – 1433Combined sources
Beta strandi146 – 1505Combined sources
Helixi152 – 1543Combined sources
Helixi162 – 1643Combined sources
Turni165 – 1706Combined sources
Beta strandi171 – 18313Combined sources
Helixi191 – 1955Combined sources
Turni198 – 2003Combined sources
Helixi203 – 21715Combined sources
Turni221 – 2233Combined sources
Beta strandi226 – 2316Combined sources
Helixi238 – 24710Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi261 – 2633Combined sources
Helixi265 – 2717Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi291 – 2944Combined sources
Helixi300 – 31819Combined sources
Beta strandi326 – 3305Combined sources
Beta strandi333 – 3353Combined sources
Helixi337 – 3415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MBBX-ray2.30A1-342[»]
1MBTX-ray3.00A1-342[»]
1UXYX-ray1.80A3-342[»]
2MBRX-ray1.80A3-342[»]
2Q85X-ray2.51A1-342[»]
ProteinModelPortaliP08373.
SMRiP08373. Positions 3-342.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08373.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 183171FAD-binding PCMH-typeAdd
BLAST

Sequence similaritiesi

Belongs to the MurB family.Curated
Contains 1 FAD-binding PCMH-type domain.Curated

Phylogenomic databases

eggNOGiENOG4105D4A. Bacteria.
COG0812. LUCA.
HOGENOMiHOG000284356.
InParanoidiP08373.
KOiK00075.
OMAiMQNIGAY.
OrthoDBiEOG60CWQ3.
PhylomeDBiP08373.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.78.10. 1 hit.
HAMAPiMF_00037. MurB.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR003170. MurB.
IPR011601. MurB_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
PANTHERiPTHR21071. PTHR21071. 1 hit.
PfamiPF01565. FAD_binding_4. 1 hit.
PF02873. MurB_C. 1 hit.
[Graphical view]
SUPFAMiSSF56176. SSF56176. 1 hit.
SSF56194. SSF56194. 1 hit.
TIGRFAMsiTIGR00179. murB. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNHSLKPWNT FGIDHNAQHI VCAEDEQQLL NAWQYATAEG QPVLILGEGS
60 70 80 90 100
NVLFLEDYRG TVIINRIKGI EIHDEPDAWY LHVGAGENWH RLVKYTLQEG
110 120 130 140 150
MPGLENLALI PGCVGSSPIQ NIGAYGVELQ RVCAYVDSVE LATGKQVRLT
160 170 180 190 200
AKECRFGYRD SIFKHEYQDR FAIVAVGLRL PKEWQPVLTY GDLTRLDPTT
210 220 230 240 250
VTPQQVFNAV CHMRTTKLPD PKVNGNAGSF FKNPVVSAET AKALLSQFPT
260 270 280 290 300
APNYPQADGS VKLAAGWLID QCQLKGMQIG GAAVHRQQAL VLINEDNAKS
310 320 330 340
EDVVQLAHHV RQKVGEKFNV WLEPEVRFIG ASGEVSAVET IS
Length:342
Mass (Da):37,851
Last modified:August 1, 1988 - v1
Checksum:iF43CFE29251E45C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351Y → H in AAA24185 (PubMed:1311302).Curated
Sequence conflicti138 – 1381S → C in AAA24185 (PubMed:1311302).Curated
Sequence conflicti242 – 2421K → E in AAA24185 (PubMed:1311302).Curated
Sequence conflicti279 – 2791I → M in AAA24185 (PubMed:1311302).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10123 Genomic DNA. Translation: AAA23519.1.
L14557 Genomic DNA. Translation: AAA24185.1.
U00006 Genomic DNA. Translation: AAC43074.1.
U00096 Genomic DNA. Translation: AAC76950.1.
AP009048 Genomic DNA. Translation: BAE77343.1.
V00348 Genomic DNA. No translation available.
PIRiA24029. QQECB8.
RefSeqiNP_418403.1. NC_000913.3.
WP_001016699.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76950; AAC76950; b3972.
BAE77343; BAE77343; BAE77343.
GeneIDi948470.
KEGGiecj:JW3940.
eco:b3972.
PATRICi32123465. VBIEscCol129921_4089.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10123 Genomic DNA. Translation: AAA23519.1.
L14557 Genomic DNA. Translation: AAA24185.1.
U00006 Genomic DNA. Translation: AAC43074.1.
U00096 Genomic DNA. Translation: AAC76950.1.
AP009048 Genomic DNA. Translation: BAE77343.1.
V00348 Genomic DNA. No translation available.
PIRiA24029. QQECB8.
RefSeqiNP_418403.1. NC_000913.3.
WP_001016699.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MBBX-ray2.30A1-342[»]
1MBTX-ray3.00A1-342[»]
1UXYX-ray1.80A3-342[»]
2MBRX-ray1.80A3-342[»]
2Q85X-ray2.51A1-342[»]
ProteinModelPortaliP08373.
SMRiP08373. Positions 3-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262982. 592 interactions.
DIPiDIP-10277N.
IntActiP08373. 12 interactions.
MINTiMINT-1275566.
STRINGi511145.b3972.

Chemistry

BindingDBiP08373.
ChEMBLiCHEMBL5526.
DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

EPDiP08373.
PaxDbiP08373.
PRIDEiP08373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76950; AAC76950; b3972.
BAE77343; BAE77343; BAE77343.
GeneIDi948470.
KEGGiecj:JW3940.
eco:b3972.
PATRICi32123465. VBIEscCol129921_4089.

Organism-specific databases

EchoBASEiEB1190.
EcoGeneiEG11205. murB.

Phylogenomic databases

eggNOGiENOG4105D4A. Bacteria.
COG0812. LUCA.
HOGENOMiHOG000284356.
InParanoidiP08373.
KOiK00075.
OMAiMQNIGAY.
OrthoDBiEOG60CWQ3.
PhylomeDBiP08373.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciEcoCyc:UDPNACETYLMURAMATEDEHYDROG-MONOMER.
ECOL316407:JW3940-MONOMER.
MetaCyc:UDPNACETYLMURAMATEDEHYDROG-MONOMER.
SABIO-RKP08373.

Miscellaneous databases

EvolutionaryTraceiP08373.
PROiP08373.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.78.10. 1 hit.
HAMAPiMF_00037. MurB.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR003170. MurB.
IPR011601. MurB_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
PANTHERiPTHR21071. PTHR21071. 1 hit.
PfamiPF01565. FAD_binding_4. 1 hit.
PF02873. MurB_C. 1 hit.
[Graphical view]
SUPFAMiSSF56176. SSF56176. 1 hit.
SSF56194. SSF56194. 1 hit.
TIGRFAMsiTIGR00179. murB. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the birA gene encoding the biotin operon repressor and biotin holoenzyme synthetase functions of Escherichia coli."
    Howard P.K., Shaw J., Otsuka A.J.
    Gene 35:321-331(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B.
  2. "Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductase."
    Pucci M.J., Discotto L.F., Dougherty T.J.
    J. Bacteriol. 174:1690-1693(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli."
    Brosius J., Dull T.J., Sleeter D.D., Noller H.F.
    J. Mol. Biol. 148:107-127(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197.
  7. "Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase."
    Benson T.E., Marquardt J.L., Marquardt A.C., Etzkorn F.A., Walsh C.T.
    Biochemistry 32:2024-2030(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls."
    Benson T.E., Walsh C.T., Hogle J.M.
    Structure 4:47-54(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  9. "X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution."
    Benson T.E., Walsh C.T., Hogle J.M.
    Biochemistry 36:806-811(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  10. "Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes."
    Constantine K.L., Mueller L., Goldfarb V., Wittekind M., Metzler W.J., Yanchunas J. Jr., Robertson J.G., Malley M.F., Friedrichs M.S., Farmer B.T. II
    J. Mol. Biol. 267:1223-1246(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiMURB_ECOLI
AccessioniPrimary (citable) accession number: P08373
Secondary accession number(s): Q2M8R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 13, 2016
This is version 164 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.