GALE_CORGL
ID GALE_CORGL Reviewed; 329 AA.
AC Q45291;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=Cgl1921, cg2104;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=8921853; DOI=10.1016/0378-1119(96)00283-1;
RA Oguiza J.A., Marcos A.T., Malumbres M., Martin J.F.;
RT "The galE gene encoding the UDP-galactose 4-epimerase of Brevibacterium
RT lactofermentum is coupled transcriptionally to the dmdR gene.";
RL Gene 177:103-107(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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 (Probable).
CC {ECO:0000305|PubMed:8921853}.
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; Z49823; CAA89986.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99314.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20262.1; -; Genomic_DNA.
DR PIR; JC5168; JC5168.
DR RefSeq; NP_601127.1; NC_003450.3.
DR RefSeq; WP_011014754.1; NC_006958.1.
DR AlphaFoldDB; Q45291; -.
DR SMR; Q45291; -.
DR STRING; 196627.cg2104; -.
DR KEGG; cgb:cg2104; -.
DR KEGG; cgl:Cgl1921; -.
DR PATRIC; fig|196627.13.peg.1859; -.
DR eggNOG; COG1087; Bacteria.
DR HOGENOM; CLU_007383_1_10_11; -.
DR OMA; GEHLICN; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000582; 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..329
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183202"
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 16
FT /note="A -> R (in Ref. 1; CAA89986)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="S -> L (in Ref. 1; CAA89986)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="T -> I (in Ref. 1; CAA89986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 35263 MW; 3411E25C83DBC553 CRC64;
MKLLVTGGAG YVGSVAAAVL LEHGHDVTII DNFSTGNREA VPADARLIEG DVNDVVEEVL
SEGGFEGVVH FAARSLVGES VEKPNEYWHD NVVTALTLLD AMRAHGVNNL VFSSTAATYG
EPDVVPITED MPTQPTNAYG ATKLSIDYAI TSYAAAFGLA ATSLRYFNVA GAYGNIGENR
EVETHLIPLV LQVATGHREK TFMFGDDWPT PDGTAVRDYI HILDLAKAHV LALESNEAGK
HRIFNLGSGD GYSVKQVVEM CREVTGHPIP AEVAPRRAGD PATLIASSEK AKQELGWTPE
HTDLRTIVED AWAFTSALGD RSHAAKKKA
