ID   GALE_ALKHC              Reviewed;         334 AA.
AC   Q9KDV3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
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; OrderedLocusNames=BH1108;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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: Carbohydrate metabolism; galactose metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; BA000004; BAB04827.1; -; Genomic_DNA.
DR   PIR; D83788; D83788.
DR   RefSeq; WP_010897278.1; NC_002570.2.
DR   AlphaFoldDB; Q9KDV3; -.
DR   SMR; Q9KDV3; -.
DR   STRING; 272558.10173723; -.
DR   EnsemblBacteria; BAB04827; BAB04827; BAB04827.
DR   KEGG; bha:BH1108; -.
DR   eggNOG; COG1087; Bacteria.
DR   HOGENOM; CLU_007383_1_10_9; -.
DR   OMA; GEHLICN; -.
DR   OrthoDB; 1597849at2; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005886; UDP_G4E.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01179; galE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD;
KW   Reference proteome.
FT   CHAIN           1..334
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183199"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         31..36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..51
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..76
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205..207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         281..284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  37078 MW;  2CDFA3DE7336EC14 CRC64;
     MAILVTGGAG YIGSHTVLFL LEQGEQVIVL DNLQKGHAGA LSDVTFYHGD IRDDQLLDTI
     FTTHSIDTVI HFAANSLVGE SVKQPIEYYE NNVIGTHTLL KKMLEHDVKK IVFSSTAATY
     GEPVQIPIQE SDPTIPTNPY GETKLAIEKM FHWCQEAYGL QYVCLRYFNA AGADPNGRIG
     EDHSPESHLI PIVLQVALGQ RERVAIFGDD YQTEDGSCIR DYIHVMDLAN AHYLACEHLR
     KDGQSGSFNL GNGKGFSVKE VIEVCRQVTG HPIPAEIAPR RSGDPASLIA SSEKAQTILG
     WEPKYPSLET MVEHAWNWHK EHPHGYSTEN KDKQ