GALE_HAEIN
ID GALE_HAEIN Reviewed; 338 AA.
AC P24325;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 144.
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=HI_0351;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=RM 7004 / Serotype B;
RX PubMed=1956282; DOI=10.1111/j.1365-2958.1991.tb01874.x;
RA Maskell D.J., Szabo M.J., Butler P.D., Williams A.E., Moxon E.R.;
RT "Molecular analysis of a complex locus from Haemophilus influenzae involved
RT in phase-variable lipopolysaccharide biosynthesis.";
RL Mol. Microbiol. 5:1013-1022(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 controlling
CC the internal galactose concentration, it may be linked to the
CC biosynthesis of lipopolysaccharide surface molecules, which are
CC important for the pathogenesis of H.influenzae.
CC {ECO:0000269|PubMed:1956282}.
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; X57315; CAA40568.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22012.1; -; Genomic_DNA.
DR PIR; A64063; A64063.
DR RefSeq; NP_438515.1; NC_000907.1.
DR RefSeq; WP_005694325.1; NC_000907.1.
DR AlphaFoldDB; P24325; -.
DR SMR; P24325; -.
DR STRING; 71421.HI_0351; -.
DR EnsemblBacteria; AAC22012; AAC22012; HI_0351.
DR KEGG; hin:HI_0351; -.
DR PATRIC; fig|71421.8.peg.370; -.
DR eggNOG; COG1087; Bacteria.
DR HOGENOM; CLU_007383_1_10_6; -.
DR OMA; KVMTGQY; -.
DR PhylomeDB; P24325; -.
DR BioCyc; HINF71421:G1GJ1-367-MON; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000579; 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; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF01370; Epimerase; 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_0000183205"
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"
FT VARIANT 285
FT /note="A -> P (in strain: RM 7004)"
FT VARIANT 333
FT /note="P -> S (in strain: RM 7004)"
SQ SEQUENCE 338 AA; 37165 MW; 449934B0E21C8A56 CRC64;
MAILVTGGAG YIGSHTVVEL LNVGKEVVVL DNLCNSSPKS LERVKQITGK EAKFYEGDIL
DRALLQKIFA ENEINSVIHF AGLKAVGESV QKPTEYYMNN VAGTLVLIQE MKKAGVWNFV
FSSSATVYGD PKIIPITEDC EVGGTTNPYG TSKYMVEQIL RDTAKAEPKF SMTILRYFNP
VGAHESGLIG EDPNGIPNNL LPYISQVAIG KLAQLSVFGS DYDTHDGTGV RDYIHVVDLA
VGHLKALQRH ENDAGLHIYN LGTGHGYSVL DMVKAFEKAN NITIAYKLVE RRSGDIATCY
SDPSLAAKEL GWVAERGLEK MMQDTWNWQK NNPKGYRD
