ID   GALE_NEIGO              Reviewed;         338 AA.
AC   Q05026;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=MS11;
RX   PubMed=8355614; DOI=10.1111/j.1365-2958.1993.tb01635.x;
RA   Robertson B.D., Frosch M., van Putten J.P.M.;
RT   "The role of galE in the biosynthesis and function of gonococcal
RT   lipopolysaccharide.";
RL   Mol. Microbiol. 8:891-901(1993).
CC   -!- FUNCTION: Involved in the metabolism of galactose. Plays an essential
CC       role in the incorporation of galactose into meningococcal
CC       lipopolysaccharide surface molecules, which are important for
CC       pathogenesis. Catalyzes the conversion of UDP-galactose (UDP-Gal) to
CC       UDP-glucose (UDP-Glc) through a mechanism involving the transient
CC       reduction of NAD. {ECO:0000269|PubMed:8355614}.
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; Z21508; CAA79721.1; -; Genomic_DNA.
DR   PIR; S34984; S34984.
DR   RefSeq; WP_003694383.1; NZ_WHPL01000002.1.
DR   AlphaFoldDB; Q05026; -.
DR   SMR; Q05026; -.
DR   PRIDE; Q05026; -.
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..338
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183211"
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         292..295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  36885 MW;  C6A905035A083984 CRC64;
     MTVLITGGTG FIGSHTAVSL VQSGYDAVIL DNLCNSSAAV LPRLRQITGR NIPFYQGDIR
     DCQILRQIFS EHEIESVIHF AGLKAVGESV AEPTKYYGNN VYGSLVLAEE MARAGVLKIV
     FSSSATVYGD AEKVPYTEDM RPGDTANPYG ASKAMVERML TDIQKADPRW SVILLRYFNP
     IGAHESGLIG EQPNGVPNNL LPYICQVASG RLPQLSVFGG DYPTPDGTGM RDYIHVMDLA
     EGHIAAMKAK GGVAGVHLFN LGSGRAYSVL EIIRAFEAAS GLHIPYRIQP RRAGDLACSY
     ADPSHTKQQT GWETKRGLQQ MMEDSWRWVS RNPGRYGD