ID   GALE_LACHE              Reviewed;         330 AA.
AC   Q7WTB1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 74.
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   Lactobacillus helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TRANSCRIPTIONAL
RP   EXPRESSION.
RC   STRAIN=ATCC 15009 / DSM 20075 / BCRC 12936 / JCM 1120 / NBRC 15019 / NCIMB
RC   11971 / NRRL B-4526 / Lh12;
RX   PubMed=12788721; DOI=10.1128/aem.69.6.3238-3243.2003;
RA   Fortina M.G., Ricci G., Mora D., Guglielmetti S., Manachini P.L.;
RT   "Unusual organization for lactose and galactose gene clusters in
RT   Lactobacillus helveticus.";
RL   Appl. Environ. Microbiol. 69:3238-3243(2003).
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. It also could be
CC       involved in preparation of carbohydrate residues for incorporation into
CC       complex polymers, such as exopolysaccharides.
CC       {ECO:0000269|PubMed:12788721}.
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   -!- INDUCTION: Seems to be constitutively expressed.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ512879; CAD55502.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7WTB1; -.
DR   SMR; Q7WTB1; -.
DR   STRING; 326425.lhe_1444; -.
DR   eggNOG; COG1087; Bacteria.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD.
FT   CHAIN           1..330
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183208"
FT   ACT_SITE        141
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         51..52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         282..285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  36429 MW;  6C9161AC65C15066 CRC64;
     MKVLVIGGAG YIGSHAVREL VKEGNDVLVL DALYTGHRKA VDPKAKFYQG DIEDTFLVSK
     ILRDEKIDAV MHFAAYSLVP ESVKKPLKYY DNNVTGMISL LQAMNDANVK YLVFSSSAAT
     YGIPKKLPIT EDTPLNPINP YGETKMMMEK IMAWADKADG IKYTALRYFN VAGASSDGSI
     GEDHAPETHL IPNILKSAIS GDGKFTIFGD DYDTKDGTNV RDYVQVEDLI DAHILALKHM
     MKTNKSDVFN LGTAHGYSNL EILESAKKVT GIDIPYTMGP RRGGDPDSLV ADSTKARTVL
     GWKPKHENVD DVIATAWKWH KSHPKGYEDK