GALE_CORDI
ID GALE_CORDI Reviewed; 328 AA.
AC P33119;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=DIP1415;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C7(-);
RX PubMed=2116013; DOI=10.1073/pnas.87.15.5968;
RA Boyd J.M., Oza M.N., Murphy J.R.;
RT "Molecular cloning and DNA sequence analysis of a diphtheria tox iron-
RT dependent regulatory element (dtxR) from Corynebacterium diphtheriae.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5968-5972(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
RN [3]
RP IDENTIFICATION.
RA Apweiler R.;
RL Unpublished observations (APR-1995).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 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; M80338; AAA23300.1; -; Genomic_DNA.
DR EMBL; M34239; AAA23297.1; -; Genomic_DNA.
DR EMBL; BX248358; CAE49946.1; -; Genomic_DNA.
DR RefSeq; WP_010935053.1; NC_002935.2.
DR AlphaFoldDB; P33119; -.
DR SMR; P33119; -.
DR STRING; 257309.DIP1415; -.
DR EnsemblBacteria; CAE49946; CAE49946; DIP1415.
DR KEGG; cdi:DIP1415; -.
DR HOGENOM; CLU_007383_1_10_11; -.
DR OMA; GEHLICN; -.
DR OrthoDB; 1597849at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000002198; Chromosome.
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; 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..328
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183201"
FT ACT_SITE 139
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 51..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 71..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277..280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 57
FT /note="D -> E (in Ref. 1; AAA23300/AAA23297)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="L -> P (in Ref. 1; AAA23300/AAA23297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 35433 MW; 6E6D1C50E1D4A33F CRC64;
MKLLVTGGAG YVGSVCSTVL LEQGHEVTIV DNLTTGNRDA VPLGATFVEG DIKDVADNVL
SSDSFDAVLH FAARSLVGES VEKPDEYWQH NMVTTLALLD AMKRNNVRNI VFSSTAATYG
EPETVPITED APTHPTNPYG ATKLSIDYAI TSYAHAYGFA ATSLRYFNVA GAYGLVGENR
EIETHLIPLV LQVALGHRDK IFMFGDDWPT EDGTPIRDYI HIRDLADAHI LALQSNVEGS
HRIFNLGSGE GYSVKQVIDT CREVTGHLIP AEVAPRRAGD PAVLIASSAK AQSELGWKPQ
RTDLHTIVSD AWAFTSQLGD KAHSASRG
