WECB_ECO57
ID WECB_ECO57 Reviewed; 376 AA.
AC Q8XAR8;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028};
DE EC=5.1.3.14 {ECO:0000255|HAMAP-Rule:MF_02028};
DE AltName: Full=UDP-GlcNAc-2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028};
GN Name=wecB {ECO:0000255|HAMAP-Rule:MF_02028}; Synonyms=nfrC, rffE;
GN OrderedLocusNames=Z5297, ECs4719;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N-
CC acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-
CC N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc
CC residues. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:68623; EC=5.1.3.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02028};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB38142.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58981.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB38142.1; ALT_INIT; Genomic_DNA.
DR PIR; A86065; A86065.
DR PIR; G91218; G91218.
DR RefSeq; NP_312746.2; NC_002695.1.
DR RefSeq; WP_000866672.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XAR8; -.
DR SMR; Q8XAR8; -.
DR STRING; 155864.EDL933_5106; -.
DR PRIDE; Q8XAR8; -.
DR EnsemblBacteria; AAG58981; AAG58981; Z5297.
DR EnsemblBacteria; BAB38142; BAB38142; ECs_4719.
DR GeneID; 60902505; -.
DR GeneID; 915240; -.
DR KEGG; ece:Z5297; -.
DR KEGG; ecs:ECs_4719; -.
DR PATRIC; fig|386585.9.peg.4923; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_6; -.
DR OMA; RYNTERP; -.
DR SABIO-RK; Q8XAR8; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02028; WecB_RffE; 1.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR032892; WecB.
DR InterPro; IPR029767; WecB-like.
DR PANTHER; PTHR43174; PTHR43174; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR TIGRFAMs; TIGR00236; wecB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..376
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /id="PRO_0000208528"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 290..292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
SQ SEQUENCE 376 AA; 42248 MW; AA92FCF1BD6C1AEA CRC64;
MKVLTVFGTR PEAIKMAPLV HALAKDPFFE AKVCVTAQHR EMLDQVLKLF SIVPDYDLNI
MQPGQGLTEI TCRILEGLKP ILAEFKPDVV LVHGDTTTTL ATSLAAFYQR IPVGHVEAGL
RTGDLYSPWP EEANRTLTGH LAMYHFSPTE TSRQNLLREN VADSRIFITG NTVIDALLWV
RDQVMSSDTL RSELAANYPF IDPDKKMILV TGHRRESFGR GFEEICHALA DIATTHQDIQ
IVYPVHLNPN VREPVNRILG HVKNVILIDP QEYLPFVWLM NHAWLILTDS GGIQEEAPSL
GKPVLVMRDT TERPEAVTAG TVRLVGTDKQ RIVEEVTRLL KDENEYQTMS RAHNPYGDGQ
ACSRILEALK NNRISL
