ID   GALE_STRTR              Reviewed;         332 AA.
AC   P21977;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, 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   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=A147;
RX   PubMed=1694527; DOI=10.1128/jb.172.7.4037-4047.1990;
RA   Poolman B., Royer T.J., Mainzer S.E., Schmidt B.F.;
RT   "Carbohydrate utilization in Streptococcus thermophilus: characterization
RT   of the genes for aldose 1-epimerase (mutarotase) and UDPglucose 4-
RT   epimerase.";
RL   J. Bacteriol. 172:4037-4047(1990).
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.
CC       {ECO:0000269|PubMed:1694527}.
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; M38175; AAA26944.1; -; Genomic_DNA.
DR   PIR; A44509; A44509.
DR   AlphaFoldDB; P21977; -.
DR   SMR; P21977; -.
DR   STRING; 322159.STER_1369; -.
DR   eggNOG; COG1087; Bacteria.
DR   BioCyc; MetaCyc:MON-6142; -.
DR   BRENDA; 5.1.3.2; 5956.
DR   SABIO-RK; P21977; -.
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; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005886; UDP_G4E.
DR   Pfam; PF01370; Epimerase; 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..332
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183221"
FT   ACT_SITE        143
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         32..37
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         52..53
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283..286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  36940 MW;  642D84CF72E2532E CRC64;
     MAILVLGGAG YIGSHMVDRL VEKGQEKVVV VDSLVTGHRA AVHPDAIFYQ GDLSDQDFMR
     KVFKENPDVD AVIHFAAYSL VGESMEKPLK YFDNNTAGMV KLLEVMNECG VKYIVFSSTA
     ATYGIPEEIP ILETTPQNPI NPYGESKLMM ETIMKWSDQA YGIKYVPLRY FNVAGANLMV
     RLVRTRSETH LLPIILQVAQ GVREKIMIFG DDYNTPDGTN VRDYVHPFDL ADAHLLAVEY
     LRKGNESTAF NLGSSTGFSN LQILEAARKV TGKEIPAEKA DRRPGDPDIL IASSEKARTV
     LGWKPQFDNI EKIIASAWAW HSSHPKGYDD RG