ID   GALE_NEIMC              Reviewed;         339 AA.
AC   P56986; Q59617; Q59624;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
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 meningitidis serogroup C.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=135720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=FAM20 / Serogroup C;
RX   PubMed=7790063; DOI=10.1128/iai.63.7.2508-2515.1995;
RA   Lee F.K., Stephens D.S., Gibson B.W., Engstrom J.J., Zhou D.,
RA   Apicella M.A.;
RT   "Microheterogeneity of Neisseria lipooligosaccharide: analysis of a UDP-
RT   glucose 4-epimerase mutant of Neisseria meningitidis NMB.";
RL   Infect. Immun. 63:2508-2515(1995).
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:7790063}.
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; U19895; AAA86716.1; -; Genomic_DNA.
DR   AlphaFoldDB; P56986; -.
DR   SMR; P56986; -.
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..339
FT                   /note="UDP-glucose 4-epimerase"
FT                   /id="PRO_0000183214"
FT   ACT_SITE        150
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..13
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         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         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
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         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         293..296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  37030 MW;  7DC4E4ACBE046397 CRC64;
     MKKILVTGGT GFIGSHTVVS LLKSGHQVVI LDNLCNSSIN ILPRLKTITG QEIPFYQGDI
     RDREILRRIF AENRIDSVIH FAGLKAVGES VAEPMKYYDN NVSGSLVLAE EMARAGVFKI
     VFSSSATVYG DPGKVPYTED MQPGDTTSPY GTSKSMVERI LSDIQKADPR WSVILLRYFN
     PIGAHESGLI GEQPNGIPNN LLPYICQVAA GKLPQLAVFG GDYPTPDGTG MRDYIHVMDL
     AEGHVAAMQA KSNVAGTHLL NLGSGRASSV LEIIRAFEAA SGLTIPYEVK PRRAGDLACF
     YADPSYAKAQ IGWQTQRDLT QMMEDSWRWV SNNPNGYDD