ID   GALE_YEREN              Reviewed;         336 AA.
AC   Q57301;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
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;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8081C / Serotype O:8;
RX   PubMed=8932701; DOI=10.1099/13500872-142-2-277;
RA   Zhang L., Toivanen P., Skurnik M.;
RT   "The gene cluster directing O-antigen biosynthesis in Yersinia
RT   enterocolitica serotype 0:8: identification of the genes for mannose and
RT   galactose biosynthesis and the gene for the O-antigen polymerase.";
RL   Microbiology 142:277-288(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8081C / Serotype O:8;
RA   Pierson D.E., Carlson S.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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; U46859; AAC60777.1; -; Genomic_DNA.
DR   EMBL; U43708; AAC44470.1; -; Genomic_DNA.
DR   RefSeq; WP_005167749.1; NZ_NBTE02000004.1.
DR   AlphaFoldDB; Q57301; -.
DR   SMR; Q57301; -.
DR   OrthoDB; 1597849at2; -.
DR   UniPathway; UPA00214; -.
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.
FT   CHAIN           1..336
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183223"
FT   ACT_SITE        149
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         58..59
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
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         178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         290..293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   336 AA;  37057 MW;  D9B11A9E875280EE CRC64;
     MSILITGGAG YIGSHTVLTL LEQGRNVVVL DNLINSSAES LARVSKICGR KPNFYHGDIL
     DRSCLKLIFS SHKIDSVIHF AGLKSVGESV EKPIEYYQNN VVGSITLLEE MCLANVKKLI
     FSSSATVYGE PEFVPLTEKA RIGGTTNPYG TSKVMVEQIL KDFSLAHPDY SITALRYFNP
     VGAHPSGLIG EDPNGKPNNL LPFITQVAIG KLSKLLVYGN DYDTPDGSGI RDYIHVMDLA
     EGHLSTLINL TSGFRIYNLG TGVGYSVLHM IKEFERITGK NIPFDIVSRR PGDIAECWAS
     PELAHLELGW YAKRTLVDML QDAWKWQKMN PNGYNC