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Database: UniProt
Entry: B6K552_SCHJY
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ID   B6K552_SCHJY            Unreviewed;       690 AA.
AC   B6K552;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|ARBA:ARBA00013189};
DE            EC=5.1.3.2 {ECO:0000256|ARBA:ARBA00013189};
GN   ORFNames=SJAG_03818 {ECO:0000313|EMBL:EEB08656.1};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08656.1, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB08656.1, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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:0000256|ARBA:ARBA00000083};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000256|ARBA:ARBA00007637}.
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DR   EMBL; KE651167; EEB08656.1; -; Genomic_DNA.
DR   RefSeq; XP_002174949.1; XM_002174913.2.
DR   AlphaFoldDB; B6K552; -.
DR   STRING; 402676.B6K552; -.
DR   EnsemblFungi; EEB08656; EEB08656; SJAG_03818.
DR   GeneID; 7050460; -.
DR   JaponicusDB; SJAG_03818; -.
DR   VEuPathDB; FungiDB:SJAG_03818; -.
DR   eggNOG; KOG1371; Eukaryota.
DR   HOGENOM; CLU_007383_22_1_1; -.
DR   OMA; KGLYREW; -.
DR   OrthoDB; 5489993at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IBA:GO_Central.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd09019; galactose_mutarotase_like; 1.
DR   CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR047215; Galactose_mutarotase-like.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005886; UDP_G4E.
DR   NCBIfam; TIGR01179; galE; 1.
DR   PANTHER; PTHR43725; UDP-GLUCOSE 4-EPIMERASE; 1.
DR   PANTHER; PTHR43725:SF51; UDP-GLUCOSE 4-EPIMERASE; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001744}.
FT   DOMAIN          8..337
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   690 AA;  76295 MW;  E81C2186CC8015E5 CRC64;
     MAIDKYILVT GGAGYIGSHT VVELIQRGFK VVVIDSLVNS SYDAIVRAEY IVRSPIPFFK
     IDLHDKAALN KVFDDYAIEG VIHFAAFKAV GESAQKPLEY YENNVGGAVA LLEVMSTHGV
     KTIVYSSSAT VYGDVSRFKD HNYLPINEKC PTDPVSPYGK TKYAIENIIA DLHSSDNSWR
     GAVLRYFNPI GAHPSGLLGE DPLGVPNNLL PYLAQVAVGR RDKLNVFGND YDSRDGTPIR
     DYIHVVDLAQ GHVAALEYLK TLEQGQGLYR VWNLGTGKGS TVLEIHAAFS AVVGRELPYN
     VVGRRAGDVL NLTADPTRAN TELGWKAKLT VEDACRDLWK WTMENPYGFQ VKNFKWSLFN
     DPGAEVNFAS RLNTFTFGDF SVTIANYGAT IQNIAFKGRT VVTSMDKLSL YQSDDNPAFG
     ATVGRYANRI RNGTFSIDGV TYHTDKNWRG HTIHGGSRGF GRQFWLGPVA KSDETHGTLE
     FLIYDKDGSN GFPADVIATA KFTVDEKSLR LEIEARIPES SPKDVTAVNM TNHVYFNLSS
     GETIDGTIIK TCTDTILESD PDYLLPTGRV IQYKQKLSES VDLQPSNPID NCFVAKVDGF
     KLDTRGDEMQ TIVEAHHPST GFKLTAATTD PAFQIYTGDF VDIGPYKARA GFCVEAQRYL
     EAINNEHWNK QVILRKGEVY GSDTIYTFSV
//
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