GALE_RAT
ID GALE_RAT Reviewed; 347 AA.
AC P18645;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE EC=5.1.3.2 {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=Galactowaldenase {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=UDP-N-acetylglucosamine 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE Short=UDP-GlcNAc 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE EC=5.1.3.7 {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=UDP-galactosamine 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE Short=UDP-GalNAc 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=UDP-galactose 4-epimerase {ECO:0000250|UniProtKB:Q14376};
GN Name=Gale;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=2205840; DOI=10.1093/nar/18.17.5289;
RA Zeschnigk M., Wilcken-Bergmann B., Starzinski-Powitz A.;
RT "cDNA from rat cells with reconstitutive galactose-epimerase activity in E.
RT coli.";
RL Nucleic Acids Res. 18:5289-5289(1990).
CC -!- FUNCTION: Catalyzes two distinct but analogous reactions: the
CC reversible epimerization of UDP-glucose to UDP-galactose and the
CC reversible epimerization of UDP-N-acetylglucosamine to UDP-N-
CC acetylgalactosamine. The reaction with UDP-Gal plays a critical role in
CC the Leloir pathway of galactose catabolism in which galactose is
CC converted to the glycolytic intermediate glucose 6-phosphate. It
CC contributes to the catabolism of dietary galactose and enables the
CC endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous
CC sources are limited. Both UDP-sugar interconversions are important in
CC the synthesis of glycoproteins and glycolipids.
CC {ECO:0000250|UniProtKB:Q14376}.
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; Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC galactosamine; Xref=Rhea:RHEA:20517, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:67138; EC=5.1.3.7;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q14376}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; X53949; CAA37897.1; -; mRNA.
DR PIR; S11223; S11223.
DR AlphaFoldDB; P18645; -.
DR SMR; P18645; -.
DR STRING; 10116.ENSRNOP00000013322; -.
DR PaxDb; P18645; -.
DR RGD; 621493; Gale.
DR eggNOG; KOG1371; Eukaryota.
DR InParanoid; P18645; -.
DR Reactome; R-RNO-70370; Galactose catabolism.
DR UniPathway; UPA00214; -.
DR PRO; PR:P18645; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; ISO:RGD.
DR GO; GO:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0019388; P:galactose catabolic process; ISO:RGD.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
DR GO; GO:0006012; P:galactose metabolic process; ISO:RGD.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD;
KW Reference proteome.
FT CHAIN 1..347
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183191"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 12..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 33..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 66..67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 132..134
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 184..186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 223..225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 299..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
SQ SEQUENCE 347 AA; 38225 MW; 625B81546E699143 CRC64;
MEEKVLVTGG AGYIGSHTVL ELLEAGYSPV VIDNFHNSIR GEDSMPESLR RVQELTGRSV
EFEEMDILDQ AALQHLFKKH NFKAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMR
AMGVKSLVFS SSATVYGKPV PASGRGPPHR GCTKPYGKSK FFIEEMIQDL CRADTAWNAV
LLRYFIPIGA HRSARIGEDP QGIPNNLMPY VSQVAIGRRE ALNVFGDDYA TEDGTGVRDY
IHVVDLAKGH IAALKKLKEQ CGCRIYNLGT GTGYSVLQMV QAMEKASGKK IPYKVVARRE
GDVAACYANP SLAHEELGWT AALGLDRMCE DLWRWQKQNP SGLGAHG
