GALE_SALTY
ID GALE_SALTY Reviewed; 338 AA.
AC P22715;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=STM0776;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2198256; DOI=10.1128/jb.172.8.4392-4398.1990;
RA Houng H.S.H., Kopecko D.J., Baron L.S.;
RT "Molecular cloning and physical and functional characterization of the
RT Salmonella typhimurium and Salmonella typhi galactose utilization
RT operons.";
RL J. Bacteriol. 172:4392-4398(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; M33681; AAA27111.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19714.1; -; Genomic_DNA.
DR PIR; A37760; A37760.
DR RefSeq; NP_459755.1; NC_003197.2.
DR RefSeq; WP_001265465.1; NC_003197.2.
DR AlphaFoldDB; P22715; -.
DR SMR; P22715; -.
DR STRING; 99287.STM0776; -.
DR PaxDb; P22715; -.
DR EnsemblBacteria; AAL19714; AAL19714; STM0776.
DR GeneID; 1252296; -.
DR KEGG; stm:STM0776; -.
DR PATRIC; fig|99287.12.peg.809; -.
DR HOGENOM; CLU_007383_1_10_6; -.
DR OMA; GEHLICN; -.
DR PhylomeDB; P22715; -.
DR BioCyc; SENT99287:STM0776-MON; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000001014; 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..338
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183218"
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 BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 88
FT /note="E -> N (in Ref. 1; AAA27111)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="T -> A (in Ref. 1; AAA27111)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="Y -> T (in Ref. 1; AAA27111)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Missing (in Ref. 1; AAA27111)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="G -> A (in Ref. 1; AAA27111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37134 MW; 5F27201F0B3D5E65 CRC64;
MRVLVTGGSG YIGSHTCVQL LQNGHDVVIL DNLCNSKRSV LPVIERLGGK HPTFVEGDIR
NEALITEILH DHAIDTVIHF AGLKAVGESV ARPLEYYDNN VNGTLRLVSA MRAANVKNLI
FSSSATVYGD QPKIPYVESF PTGTPQSPYG KSKLMVEQIL TDLQKAQPEW SIALLRYFNP
VGAHPSGDMG EDPQGIPNNL MPYIAQVAVG RRESLAVFGN DYPTEDGTGV RDYIHVMDLA
DGHVVAMEKL ADKSGVHIYN LGAGVGSSVL DVVNAFSKAC GKPINYHFAP RRDGDLPAYW
ADASKADREL NWRVTRTLDE MAQDTWHWQS RHPQGYPD
