ID   A0A2G5HY19_CERBT        Unreviewed;       326 AA.
AC   A0A2G5HY19;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glycerol 2-dehydrogenase (NADP(+)) {ECO:0000313|EMBL:PIA97428.1};
GN   ORFNames=CB0940_06349 {ECO:0000313|EMBL:PIA97428.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA97428.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA97428.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA97428.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIA97428.1}.
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DR   EMBL; LKMD01000102; PIA97428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HY19; -.
DR   OrthoDB; 5305445at2759; -.
DR   Proteomes; UP000230605; Chromosome 2.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43827; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR   PANTHER; PTHR43827:SF3; ALDO-KETO REDUCTASE; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PE   4: Predicted;
FT   DOMAIN          18..295
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        53
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            83
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   326 AA;  36734 MW;  6125DB46EC355EA7 CRC64;
     MSNGKTFTLN NGVSIPAVGF GTFANEGSKG ETYKAVTHAL NVGYRHLDCA WFYQNEDEVG
     DAVVDFLKSN PSVHRSDIFI CTKVWNHLHE PEEVKWSLQS SLKKLKVDYL DLFLVHWPIA
     AEKDENYNPK LNEKGQYVIK EELTNNPRPT WRAMEEIYES GKARAIGVSN WTVPGLKDML
     SWAKVKPAVN QIEIHPFLPN EELVNFCFEN NILPQAYSPL GSQNQVPTTG EKVNTNKTLN
     EIAEKGGNTL AQVLIAWGIR RGYVVLPKSS TPSRIESNFK SIDLSDEDFE AVNAVAKGRH
     TRFVNMKGDF GYDVWPEDSQ IADVQK
//