ID   A0A1V2L5A7_CYBFA        Unreviewed;       174 AA.
AC   A0A1V2L5A7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=UDP-glucose 4-epimerase {ECO:0000313|EMBL:ONH66446.1};
GN   ORFNames=BON22_3702 {ECO:0000313|EMBL:ONH66446.1};
OS   Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH66446.1, ECO:0000313|Proteomes:UP000189513};
RN   [1] {ECO:0000313|Proteomes:UP000189513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX   PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA   van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT   "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT   and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT   Zimbabwe.";
RL   Genome Announc. 5:E00064-E00064(2017).
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. {ECO:0000256|ARBA:ARBA00037676}.
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   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldose epimerase
CC       family. {ECO:0000256|ARBA:ARBA00038238}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC       epimerase/dehydratase family. {ECO:0000256|ARBA:ARBA00037955}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ONH66446.1}.
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DR   EMBL; MPUK01000007; ONH66446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2L5A7; -.
DR   STRING; 36022.A0A1V2L5A7; -.
DR   VEuPathDB; FungiDB:BON22_3702; -.
DR   OrthoDB; 5489993at2759; -.
DR   Proteomes; UP000189513; Unassembled WGS sequence.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43725; UDP-GLUCOSE 4-EPIMERASE; 1.
DR   PANTHER; PTHR43725:SF51; UDP-GLUCOSE 4-EPIMERASE; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023144};
KW   Galactose metabolism {ECO:0000256|ARBA:ARBA00023144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189513}.
FT   DOMAIN          83..173
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
SQ   SEQUENCE   174 AA;  18906 MW;  EB048027D2D012FB CRC64;
     MTITSYTLVT GGLGYIASHT IPLLDCPVII IDNVSNSSLS QLEGIKSLTS HPVVFEKLDL
     TDKSALNHFF SRFHDGKSQI NQTLIFASSA AVYGSAPPGV KEDIDCVPTT PYGVTKLKVE
     HILEQYSLSK GIDIAMLRYF NPIGVHPSGK LGEQSNNLMP IVLKSLREGK TMTL
//