ID   GALE_MYCTO              Reviewed;         314 AA.
AC   P9WN66; F2GF05; L0TES1; Q6MWV3; Q7D561;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=UDP-glucose 4-epimerase;
DE            EC=5.1.3.2;
DE   AltName: Full=UDP-galactose 4-epimerase;
DE   AltName: Full=Uridine diphosphate galactose 4-epimerase;
GN   Name=galE1; OrderedLocusNames=MT3736;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK48097.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK48097.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70562; C70562.
DR   RefSeq; WP_003419610.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WN66; -.
DR   SMR; P9WN66; -.
DR   EnsemblBacteria; AAK48097; AAK48097; MT3736.
DR   KEGG; mtc:MT3736; -.
DR   PATRIC; fig|83331.31.peg.4020; -.
DR   HOGENOM; CLU_007383_1_7_11; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000001020; 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   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD.
FT   CHAIN           1..314
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000427180"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
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         56..57
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         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  33582 MW;  EED55D1C848C6B67 CRC64;
     MRALVTGAAG FIGSTLVDRL LADGHSVVGL DNFATGRATN LEHLADNSAH VFVEADIVTA
     DLHAILEQHR PEVVFHLAAQ IDVRRSVADP QFDAAVNVIG TVRLAEAARQ TGVRKIVHTS
     SGGSIYGTPP EYPTPETAPT DPASPYAAGK VAGEIYLNTF RHLYGLDCSH IAPANVYGPR
     QDPHGEAGVV AIFAQALLSG KPTRVFGDGT NTRDYVFVDD VVDAFVRVSA DVGGGLRFNI
     GTGKETSDRQ LHSAVAAAVG GPDDPEFHPP RLGDLKRSCL DIGLAERVLG WRPQIELADG
     VRRTVEYFRH KHTD