ID   GALE_MYCPN              Reviewed;         338 AA.
AC   P75517;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=MPN_257; ORFNames=MP576;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96224.1; -; Genomic_DNA.
DR   PIR; S73902; S73902.
DR   RefSeq; NP_109945.1; NC_000912.1.
DR   RefSeq; WP_010874614.1; NC_000912.1.
DR   AlphaFoldDB; P75517; -.
DR   SMR; P75517; -.
DR   IntAct; P75517; 3.
DR   STRING; 272634.MPN_257; -.
DR   EnsemblBacteria; AAB96224; AAB96224; MPN_257.
DR   GeneID; 66609097; -.
DR   KEGG; mpn:MPN_257; -.
DR   PATRIC; fig|272634.6.peg.276; -.
DR   HOGENOM; CLU_007383_1_10_14; -.
DR   OMA; KVMTGQY; -.
DR   BioCyc; MPNE272634:G1GJ3-405-MON; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000000808; 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..338
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183210"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         16..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         37..42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..85
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
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         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         294..297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  38133 MW;  9C50FF3856E68C03 CRC64;
     MSETKSKVLV LGGLGYIGSC FIDQLLKQYP DVTVSVIDIN HTSLALQLLP RQVNVHFVNL
     LDRAQLTDTI AQINPDVVFH FAAKTSVKES TEQPLTYFDH NLVGTLNLLH ALKELQKPIQ
     LFFSSTAAVF GSASTLPIPE NLVLEETLAS NPYGISKFLS EIVLQTLTRS PHFQVIALRY
     FNVAGASNPF GNFNKNTTLL IPNLIKAFME KRTFFLYGDD YDTKDGSCIR DYIHVVDLCD
     AHLLAWKWLQ ANPKVRFESF NLGSGQGFSN WEVINTAQAI FAPEQLQLKI ESRRAGDPPV
     LVVDCTKAKR LLNFQPTRSL HKMLSDETIF YRDFYNRL