GALE_DICDI
ID GALE_DICDI Reviewed; 344 AA.
AC Q553X7; Q86I53;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000303|PubMed:4252223};
DE EC=5.1.3.2 {ECO:0000303|PubMed:4252223};
DE AltName: Full=Galactowaldenase {ECO:0000303|PubMed:4252223};
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:0000303|PubMed:4252223};
GN Name=galE; ORFNames=DDB_G0275295;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP CHARACTERIZATION, DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NC-4;
RX PubMed=4252223; DOI=10.1016/s0021-9258(19)77214-7;
RA Telser A., Sussman M.;
RT "Uridine diphosphate galactose-4-epimerase, a developmentally regulated
RT enzyme in the cellular slime mold Dictyostelium discoideum.";
RL J. Biol. Chem. 246:2252-2257(1971).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:4252223};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q14376}.
CC -!- DEVELOPMENTAL STAGE: Expressed in prestalk cells, between 16 and 21
CC hours. Expression peaks at 18.5 hours. {ECO:0000269|PubMed:4252223}.
CC -!- MISCELLANEOUS: After the expression has peaked the enzyme is released
CC to the surrounding media.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69928.1; -; Genomic_DNA.
DR RefSeq; XP_643834.1; XM_638742.1.
DR AlphaFoldDB; Q553X7; -.
DR SMR; Q553X7; -.
DR STRING; 44689.DDB0231575; -.
DR PaxDb; Q553X7; -.
DR EnsemblProtists; EAL69928; EAL69928; DDB_G0275295.
DR GeneID; 8619881; -.
DR KEGG; ddi:DDB_G0275295; -.
DR dictyBase; DDB_G0275295; galE.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q553X7; -.
DR OMA; GEHLICN; -.
DR PhylomeDB; Q553X7; -.
DR Reactome; R-DDI-70370; Galactose catabolism.
DR UniPathway; UPA00214; -.
DR PRO; PR:Q553X7; -.
DR Proteomes; UP000002195; Chromosome 2.
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:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD;
KW Reference proteome.
FT CHAIN 1..344
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000328225"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 15..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 36..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 63..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 129..131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 181..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 220..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
SQ SEQUENCE 344 AA; 37850 MW; 803C8CF3A2603ED0 CRC64;
MEPIDDRIMV TGGAGYIGSH TVIELIEAGY TPVIVDNLSN SSLEAIKRVE SITGKEIEFH
HVDIMNEKAL DEIFETGNIR SVIHFAGLKA VGESNKLPLK YYNNNIAGTL TLLNLMDKHR
VKKLVFSSSA TVYGDPHTVP ITEDFPLSAT NPYGRTKLYV EGILQDLCAS DPEWNCIMLR
YFNPVGAHPS GLIGEDPKDI PNNLMPYVTQ TAIGKRPILS IFGNDYNTPD GTGVRDFIHV
VDLAKGHISA LSSLHSKKQG CVAYNLGTGR GYSVLEMVGA LKQASHKEIP YQIVSRRKGD
VASSFADPSK ALKELGWKAT HNQDDMCRDA WKWQSLNPNG YSDS
