GALE_NEIMB
ID GALE_NEIMB Reviewed; 339 AA.
AC P56985; Q59617; Q59624;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=NMB0064;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=MC58;
RX PubMed=7934827; DOI=10.1111/j.1365-2958.1993.tb01962.x;
RA Jennings M.P., van der Ley P., Wilks K.E., Maskell D.J., Poolman J.T.,
RA Moxon E.R.;
RT "Cloning and molecular analysis of the galE gene of Neisseria meningitidis
RT and its role in lipopolysaccharide biosynthesis.";
RL Mol. Microbiol. 10:361-369(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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:7934827}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L20495; AAA65535.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF40532.1; -; Genomic_DNA.
DR PIR; S39638; S39638.
DR RefSeq; NP_273128.1; NC_003112.2.
DR RefSeq; WP_002249104.1; NC_003112.2.
DR AlphaFoldDB; P56985; -.
DR SMR; P56985; -.
DR STRING; 122586.NMB0064; -.
DR PaxDb; P56985; -.
DR EnsemblBacteria; AAF40532; AAF40532; NMB0064.
DR KEGG; nme:NMB0064; -.
DR PATRIC; fig|122586.8.peg.100; -.
DR HOGENOM; CLU_007383_1_10_4; -.
DR OMA; GEHLICN; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IBA:GO_Central.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
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..339
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183213"
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; 37062 MW; 7D702C44F07DA99B CRC64;
MKKILVTGGT GFIGSHTVVS LLKSGHQVVI LDNLCNSSIN ILPRLKTITG QEIPFYQGDI
RDREILRRIF AENRIDSVIH FAGLKAVGES VAEPMKYYDN NVSGSLVLAE EMARAGVFSI
VFSSSATVYG DPGKVPYTED MPPGDTTSPY GASKSMVERI LTDIQKADPR WSMILLRYFN
PIGAHESGLI GEQPNGIPNN LLPYICQVAA GKLPQLAVFG DDYPTPDGTG MRDYIHVMDL
AEGHVAAMQA KSNVAGTHLL NLGSGRASSV LEIIRAFEAA SGLTIPYEVK PRRAGDLACF
YADPSYTKAQ IGWQTQRDLT QMMEDSWRWV SNNPNGYDD
