ID   GALE_VIBCL              Reviewed;         328 AA.
AC   Q56623; O87141; Q9S1B8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=UDP-glucose 4-epimerase;
DE            EC=5.1.3.2;
DE   AltName: Full=Galactowaldenase;
DE   AltName: Full=UDP-galactose 4-epimerase;
GN   Name=galE; Synonyms=wbfT;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AI-1837 / Serotype O139;
RX   PubMed=8820651; DOI=10.1046/j.1365-2958.1996.407928.x;
RA   Comstock L.E., Michalski J.M., Johnson J.A., Morris J.G. Jr., Kaper J.B.;
RT   "Cloning and sequence of a region encoding a surface polysaccharide of
RT   Vibrio cholerae O139 and characterization of the insertion site in the
RT   chromosome of Vibrio cholerae O1.";
RL   Mol. Microbiol. 19:815-826(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51394 / MO45 / Serotype O139, and O22;
RX   PubMed=10521656; DOI=10.1016/s0378-1119(99)00344-3;
RA   Yamasaki S., Shimizu T., Hoshino K., Ho S.-T., Shimada T., Nair G.B.,
RA   Takeda Y.;
RT   "The genes responsible for O-antigen synthesis of Vibrio cholerae O139 are
RT   closely related to those of Vibrio cholerae O22.";
RL   Gene 237:321-332(1999).
CC   -!- FUNCTION: Involved in the metabolism of galactose. Catalyzes the
CC       conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through
CC       a mechanism involving the transient reduction of NAD (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC         Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC         EC=5.1.3.2;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA33640.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U47057; AAC46247.1; -; Genomic_DNA.
DR   EMBL; AB012956; BAA33610.1; -; Genomic_DNA.
DR   EMBL; AB012957; BAA33640.1; ALT_INIT; Genomic_DNA.
DR   PIR; S70885; S70885.
DR   PIR; T44336; T44336.
DR   RefSeq; WP_000337357.1; NZ_VMQN01000077.1.
DR   AlphaFoldDB; Q56623; -.
DR   SMR; Q56623; -.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD.
FT   CHAIN           1..328
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183222"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         20..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..58
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..81
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         133
FT                   /note="V -> M (in strain: O22)"
FT   VARIANT         242
FT                   /note="G -> D (in strain: O22 and MO45)"
SQ   SEQUENCE   328 AA;  35811 MW;  0A922FA429971F3F CRC64;
     MCTGDRKMPK SILLTGSTGF VGTNLVKSLT LKSDYIVKSA VRHAVNKDDG LLFEVGDINA
     STDFELPLKN TTVVVHCAAR AHVMDDKEAE PLTLYREVNT AGTVNLAKQA IDSGVKRFIF
     ISSIKVNGEG TLVGCPFKTE DNHAPEDDYG LSKSEAEKQL VALAKDSSME VVIIRPTIVY
     GPGVKANFAS LMRLVSKGIP LPFGSITQNK RSLVSINNLV DLIVTCIDHP KAANQVFLVS
     DGHDVSTAEM VRELAIALDK PTWQLPVPIW CYKLFGKLFG KSDIVDRLTG TLQVDISHTK
     ETLGWKPPQT LQEGFKQTAQ AFLQANNR