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GLD2_HYPJE
ID   GLD2_HYPJE              Reviewed;         318 AA.
AC   Q0GYU4;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Glycerol 2-dehydrogenase (NADP(+));
DE            EC=1.1.1.156;
GN   Name=gld2;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16930134; DOI=10.1111/j.1742-4658.2006.05423.x;
RA   Liepins J., Kuorelahti S., Penttila M., Richard P.;
RT   "Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-
RT   glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina.";
RL   FEBS J. 273:4229-4235(2006).
CC   -!- FUNCTION: Glycerol oxidoreductase probably involved in glycerol
CC       synthesis. {ECO:0000269|PubMed:16930134}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol + NADP(+) = dihydroxyacetone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:12753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.156; Evidence={ECO:0000269|PubMed:16930134};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1 mM for dihydroxyacetone (in the reductive reaction)
CC         {ECO:0000269|PubMed:16930134};
CC         KM=50 mM for NADPH (in the reductive reaction)
CC         {ECO:0000269|PubMed:16930134};
CC         KM=350 mM for glycerol (in the oxidative reaction)
CC         {ECO:0000269|PubMed:16930134};
CC         KM=110 mM for NADP (in the oxidative reaction)
CC         {ECO:0000269|PubMed:16930134};
CC         KM=96 mM for D-glyceraldehyde {ECO:0000269|PubMed:16930134};
CC         KM=8 mM for L-glyceraldehyde {ECO:0000269|PubMed:16930134};
CC         KM=13 mM for diacetyl {ECO:0000269|PubMed:16930134};
CC         KM=30 mM for glyoxal {ECO:0000269|PubMed:16930134};
CC         KM=37500 mM for methylglyoxal {ECO:0000269|PubMed:16930134};
CC         KM=113 mM for acetoin {ECO:0000269|PubMed:16930134};
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; DQ422038; ABD83953.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0GYU4; -.
DR   SMR; Q0GYU4; -.
DR   PRIDE; Q0GYU4; -.
DR   VEuPathDB; FungiDB:TrQ_007971; -.
DR   OMA; HCRFVNM; -.
DR   BRENDA; 1.1.1.156; 6451.
DR   SABIO-RK; Q0GYU4; -.
DR   GO; GO:0047953; F:glycerol 2-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.100; -; 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   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Glycerol metabolism; NADP; Oxidoreductase.
FT   CHAIN           1..318
FT                   /note="Glycerol 2-dehydrogenase (NADP(+))"
FT                   /id="PRO_0000424285"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..277
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  35721 MW;  F781CFBE5A3FBA42 CRC64;
     MASKTYTLNT GAKIPAVGFG TFANEGAKGE TYAAVTKALD VGYRHLDCAW FYHNEDEVGD
     AVRDFLARRP DVKREDLFIC TKVWNHLHEP EDVKWSAKNS CENLKVDYID LFLVHWPIAA
     EKNSDRSVKL GPDGKYVINQ ALTENPEPTW RAMEELVESG LVKAIGVSNW TIPGLKKLLQ
     IAKIKPAVNQ IEIHPFLPNE ELVAFCFENG ILPEAYSPLG SQNQVPSTGE RVRDNPTLKA
     VAERSGYSLA QILLAWGLKR GYVVLPKSST PSRIESNFNI PELSDEDFEA IQQVAKGRHT
     RFVNMKDTFG YNVWPEEE
 
 
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