ID   GAL10_PACTA             Reviewed;         689 AA.
AC   P40801;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Bifunctional protein GAL10;
DE   Includes:
DE     RecName: Full=UDP-glucose 4-epimerase;
DE              EC=5.1.3.2;
DE     AltName: Full=Galactowaldenase;
DE   Includes:
DE     RecName: Full=Aldose 1-epimerase;
DE              EC=5.1.3.3;
DE     AltName: Full=Galactose mutarotase;
GN   Name=GAL10;
OS   Pachysolen tannophilus (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX   NCBI_TaxID=4918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 32691 / BCRC 20329 / CBS 4044 / DSM 70352 / NBRC 1007 / NRRL
RC   Y-2460;
RX   PubMed=8125329; DOI=10.1016/0378-1119(94)90742-0;
RA   Skrzypek M., Maleszka R.;
RT   "A gene homologous to that encoding UDP galactose-4-epimerase is inducible
RT   by xylose in the yeast Pachysolen tannophilus.";
RL   Gene 140:127-129(1994).
CC   -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC       active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC       lactose (By similarity). {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC         ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10126};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- INDUCTION: By xylose.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC       epimerase/dehydratase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldose epimerase
CC       family. {ECO:0000305}.
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DR   EMBL; X68593; CAA48580.1; -; Genomic_DNA.
DR   PIR; S29621; S29621.
DR   AlphaFoldDB; P40801; -.
DR   SMR; P40801; -.
DR   BRENDA; 5.1.3.2; 4482.
DR   UniPathway; UPA00214; -.
DR   UniPathway; UPA00242; -.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
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   Pfam; PF01263; Aldose_epim; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   TIGRFAMs; TIGR01179; galE; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Galactose metabolism; Isomerase;
KW   Multifunctional enzyme; NAD.
FT   CHAIN           1..689
FT                   /note="Bifunctional protein GAL10"
FT                   /id="PRO_0000197440"
FT   REGION          1..345
FT                   /note="Galactowaldenase"
FT   REGION          346..689
FT                   /note="Mutarotase"
FT   ACT_SITE        534
FT                   /note="For mutarotase activity"
FT                   /evidence="ECO:0000255"
FT   BINDING         3..34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   689 AA;  76671 MW;  80C8A08262D3ED36 CRC64;
     MSYILVTGGA GYIGSHTVVE LVNNGYNVVV VDNLVNSSYD VIVRIEVLTR KQIPFFKIDL
     NDHDALDQVF KLYPIQAVLH FAALKAVGES TKFPLNYYSN NVGGAISLLK VMEENNVKNI
     VFSSSATVYG DATRFENMIP IPEHCPTGPT NPYGETKITI ENIIRDVYAN DKSWKCAILR
     YFNPIGAHPS GLIGEDPLGI PNNLLPFLAQ VAIGRREKLS VFGSDYNSKD GTPIRDYIHV
     IDLAKGHIAA LNYLFNHKDN GLCREWNLGT GNGSTVFEVF NAFCEAVGKK LPFEVVGRRD
     GDVLNLTANP KRANTELKWK AQLSINDACK DLWNWTTKNP FGFQINNYSW TKFDSESLTN
     YDRLNTVRTF NGKFEVSISN HGATIVAAKL NGIKLNLGFD NLKGYLREDN PFFGATIGRV
     ANRISKGDLL INGTHYQVGL NELHRTSLHG GTYGYNKRTF LGPIVKTNEK EKETTMEFVL
     IDLDGTEGYP GDVETKVIYT VRDTGVGGEL GIEYEAKLLE ESGRDSTAVS LTNHSYWNIG
     NQPSIEGTHI KLVSNKHLES NPLDSTPTGK IVTSTDLDSQ NSAKLGPDGP VFDYCFVTKQ
     QDKLDTRNDE LRVVATATHP KTRIAFTTLT TEPAFQFYTG DGVDVAGVFT KRSGFCLEAS
     RYIYNPKWFI PLNKGEVYGS YTIYRFENF