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Protein

UDP-N-acetylglucosamine 2-epimerase

Gene

wecB

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

Functioni

Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption.5 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine.UniRule annotation2 Publications

Enzyme regulationi

Allosterically activated by its substrate, UDP-GlcNAc.1 Publication

Kineticsi

kcat is 7.1 sec(-1).1 Publication

  1. KM=0.6 mM for UDP-GlcNAc1 Publication

    Pathwayi: enterobacterial common antigen biosynthesis

    This protein is involved in the pathway enterobacterial common antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation1 Publication
    View all proteins of this organism that are known to be involved in the pathway enterobacterial common antigen biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101SubstrateUniRule annotation2 Publications
    Binding sitei15 – 151SubstrateUniRule annotation1 Publication
    Binding sitei95 – 951SubstrateUniRule annotation1 Publication
    Binding sitei117 – 1171SubstrateUniRule annotation1 Publication
    Binding sitei213 – 2131SubstrateUniRule annotation2 Publications
    Binding sitei271 – 2711Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation2 Publications
    Binding sitei276 – 2761SubstrateUniRule annotation2 Publications
    Binding sitei296 – 2961SubstrateUniRule annotation2 Publications
    Binding sitei313 – 3131SubstrateUniRule annotation1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc
    • UDP-N-acetylglucosamine 2-epimerase activity Source: EcoCyc

    GO - Biological processi

    • enterobacterial common antigen biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BioCyciEcoCyc:UDPGLCNACEPIM-MONOMER.
    ECOL316407:JW5600-MONOMER.
    MetaCyc:UDPGLCNACEPIM-MONOMER.
    BRENDAi3.2.1.183. 1960.
    5.1.3.14. 2026.
    SABIO-RKP27828.
    UniPathwayiUPA00566.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylglucosamine 2-epimeraseUniRule annotationCurated (EC:5.1.3.14UniRule annotation2 Publications)
    Alternative name(s):
    Bacteriophage N4 adsorption protein C1 Publication
    UDP-GlcNAc-2-epimeraseUniRule annotationCurated
    Gene namesi
    Name:wecBUniRule annotationImported
    Synonyms:nfrC1 Publication, rffE1 Publication, yifF
    Ordered Locus Names:b3786, JW5600
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11451. wecB.

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151K → A: More than 100-fold increase in KM for UDP-GlcNAc. 1 Publication
    Mutagenesisi95 – 951D → N: Strong decrease in activity. 1 Publication
    Mutagenesisi117 – 1171E → Q: Strong decrease in activity. 1 Publication
    Mutagenesisi131 – 1311E → Q: Strong decrease in activity. 1 Publication
    Mutagenesisi213 – 2131H → N: 30-fold increase in KM for UDP-GlcNAc and 50-fold decrease in kcat. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 376376UDP-N-acetylglucosamine 2-epimerasePRO_0000208527Add
    BLAST

    Proteomic databases

    PaxDbiP27828.
    PRIDEiP27828.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4263321. 147 interactions.
    STRINGi511145.b3786.

    Structurei

    Secondary structure

    1
    376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76Combined sources
    Helixi10 – 2516Combined sources
    Beta strandi30 – 356Combined sources
    Helixi40 – 434Combined sources
    Helixi44 – 496Combined sources
    Beta strandi55 – 573Combined sources
    Beta strandi62 – 654Combined sources
    Helixi67 – 8519Combined sources
    Beta strandi88 – 936Combined sources
    Helixi97 – 10711Combined sources
    Turni108 – 1103Combined sources
    Beta strandi113 – 1175Combined sources
    Helixi131 – 1399Combined sources
    Beta strandi143 – 1497Combined sources
    Helixi150 – 1589Combined sources
    Helixi163 – 1653Combined sources
    Beta strandi166 – 1683Combined sources
    Helixi172 – 18312Combined sources
    Turni184 – 1863Combined sources
    Helixi188 – 1958Combined sources
    Beta strandi205 – 2117Combined sources
    Beta strandi215 – 2173Combined sources
    Helixi220 – 23516Combined sources
    Beta strandi239 – 2446Combined sources
    Helixi249 – 25911Combined sources
    Beta strandi265 – 2684Combined sources
    Helixi273 – 28210Combined sources
    Beta strandi284 – 2918Combined sources
    Helixi293 – 2953Combined sources
    Helixi297 – 3004Combined sources
    Beta strandi304 – 3096Combined sources
    Helixi314 – 3185Combined sources
    Beta strandi321 – 3255Combined sources
    Helixi329 – 34113Combined sources
    Helixi343 – 3508Combined sources
    Helixi361 – 37111Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F6DX-ray2.50A/B/C/D1-376[»]
    1VGVX-ray2.31A/B/C/D2-376[»]
    ProteinModelPortaliP27828.
    SMRiP27828. Positions 1-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27828.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 2923Substrate bindingUniRule annotation2 Publications

    Sequence similaritiesi

    Belongs to the UDP-N-acetylglucosamine 2-epimerase family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105EAG. Bacteria.
    COG0381. LUCA.
    HOGENOMiHOG000076048.
    InParanoidiP27828.
    KOiK01791.
    OMAiIMKERQT.
    OrthoDBiEOG6HXJ6F.
    PhylomeDBiP27828.

    Family and domain databases

    HAMAPiMF_02028. WecB_RffE.
    InterProiIPR003331. UDP_GlcNAc_Epimerase_2_dom.
    IPR032892. WecB.
    IPR029767. WecB-like.
    [Graphical view]
    PANTHERiPTHR18964:SF2. PTHR18964:SF2. 1 hit.
    PfamiPF02350. Epimerase_2. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00236. wecB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P27828-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKVLTVFGTR PEAIKMAPLV HALAKDPFFE AKVCVTAQHR EMLDQVLKLF
    60 70 80 90 100
    SIVPDYDLNI MQPGQGLTEI TCRILEGLKP ILAEFKPDVV LVHGDTTTTL
    110 120 130 140 150
    ATSLAAFYQR IPVGHVEAGL RTGDLYSPWP EEANRTLTGH LAMYHFSPTE
    160 170 180 190 200
    TSRQNLLREN VADSRIFITG NTVIDALLWV RDQVMSSDKL RSELAANYPF
    210 220 230 240 250
    IDPDKKMILV TGHRRESFGR GFEEICHALA DIATTHQDIQ IVYPVHLNPN
    260 270 280 290 300
    VREPVNRILG HVKNVILIDP QEYLPFVWLM NHAWLILTDS GGIQEEAPSL
    310 320 330 340 350
    GKPVLVMRDT TERPEAVTAG TVRLVGTDKQ RIVEEVTRLL KDENEYQAMS
    360 370
    RAHNPYGDGQ ACSRILEALK NNRISL
    Length:376
    Mass (Da):42,245
    Last modified:July 1, 1993 - v2
    Checksum:i7B02EE6C2630DD77
    GO

    Sequence cautioni

    The sequence AAA67586.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911Missing in AAA67586 (PubMed:1379743).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L18799 Unassigned DNA. Translation: AAC36847.1.
    M87049 Genomic DNA. Translation: AAA67586.1. Different initiation.
    U00096 Genomic DNA. Translation: AAT48211.1.
    AP009048 Genomic DNA. Translation: BAE77512.1.
    PIRiE65182.
    RefSeqiYP_026253.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAT48211; AAT48211; b3786.
    BAE77512; BAE77512; BAE77512.
    GeneIDi944789.
    KEGGiecj:JW5600.
    eco:b3786.
    PATRICi32123065. VBIEscCol129921_3902.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L18799 Unassigned DNA. Translation: AAC36847.1.
    M87049 Genomic DNA. Translation: AAA67586.1. Different initiation.
    U00096 Genomic DNA. Translation: AAT48211.1.
    AP009048 Genomic DNA. Translation: BAE77512.1.
    PIRiE65182.
    RefSeqiYP_026253.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F6DX-ray2.50A/B/C/D1-376[»]
    1VGVX-ray2.31A/B/C/D2-376[»]
    ProteinModelPortaliP27828.
    SMRiP27828. Positions 1-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263321. 147 interactions.
    STRINGi511145.b3786.

    Proteomic databases

    PaxDbiP27828.
    PRIDEiP27828.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAT48211; AAT48211; b3786.
    BAE77512; BAE77512; BAE77512.
    GeneIDi944789.
    KEGGiecj:JW5600.
    eco:b3786.
    PATRICi32123065. VBIEscCol129921_3902.

    Organism-specific databases

    EchoBASEiEB1420.
    EcoGeneiEG11451. wecB.

    Phylogenomic databases

    eggNOGiENOG4105EAG. Bacteria.
    COG0381. LUCA.
    HOGENOMiHOG000076048.
    InParanoidiP27828.
    KOiK01791.
    OMAiIMKERQT.
    OrthoDBiEOG6HXJ6F.
    PhylomeDBiP27828.

    Enzyme and pathway databases

    UniPathwayiUPA00566.
    BioCyciEcoCyc:UDPGLCNACEPIM-MONOMER.
    ECOL316407:JW5600-MONOMER.
    MetaCyc:UDPGLCNACEPIM-MONOMER.
    BRENDAi3.2.1.183. 1960.
    5.1.3.14. 2026.
    SABIO-RKP27828.

    Miscellaneous databases

    EvolutionaryTraceiP27828.
    PROiP27828.

    Family and domain databases

    HAMAPiMF_02028. WecB_RffE.
    InterProiIPR003331. UDP_GlcNAc_Epimerase_2_dom.
    IPR032892. WecB.
    IPR029767. WecB-like.
    [Graphical view]
    PANTHERiPTHR18964:SF2. PTHR18964:SF2. 1 hit.
    PfamiPF02350. Epimerase_2. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00236. wecB. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A cytoplasmic protein, NfrC, is required for bacteriophage N4 adsorption."
      Kiino D.R., Licudine R., Wilt K., Yang D.H.C., Rothman-Denes L.B.
      J. Bacteriol. 175:7074-7080(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    2. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: SEQUENCE REVISION TO 191.
    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. "Biosynthesis of enterobacterial common antigen in Escherichia coli. Biochemical characterization of Tn10 insertion mutants defective in enterobacterial common antigen synthesis."
      Meier-Dieter U., Starman R., Barr K., Mayer H., Rick P.D.
      J. Biol. Chem. 265:13490-13497(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PATHWAY.
    7. "Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene."
      Marolda C.L., Valvano M.A.
      J. Bacteriol. 177:5539-5546(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: O7:K1 / VW187.
    8. "Characterization of the dTDP-rhamnose biosynthetic genes encoded in the rfb locus of Shigella flexneri."
      Macpherson D.F., Manning P.A., Morona R.
      Mol. Microbiol. 11:281-292(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Enzymatic formation and release of a stable glycal intermediate: the mechanism of the reaction catalyzed by UDP-N-acetylglucosamine 2-epimerase."
      Sala R.F., Morgan P.M., Tanner M.E.
      J. Am. Chem. Soc. 118:3033-3034(1996)
      Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.
    10. "Active site mutants of the 'non-hydrolyzing' UDP-N-acetylglucosamine 2-epimerase from Escherichia coli."
      Samuel J., Tanner M.E.
      Biochim. Biophys. Acta 1700:85-91(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-15; ASP-95; GLU-117; GLU-131 AND HIS-213.
    11. "The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases."
      Campbell R.E., Mosimann S.C., Tanner M.E., Strynadka N.C.
      Biochemistry 39:14993-15001(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH UDP, SUBUNIT.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-376 IN COMPLEX WITH UDP-N-ACETYL-ALPHA-D-GLUCOSAMINE.

    Entry informationi

    Entry nameiWECB_ECOLI
    AccessioniPrimary (citable) accession number: P27828
    Secondary accession number(s): P76753, Q2M894
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: July 1, 1993
    Last modified: March 16, 2016
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, 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.