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Database: UniProt
Entry: G9PAH5_HYPAI
LinkDB: G9PAH5_HYPAI
Original site: G9PAH5_HYPAI 
ID   G9PAH5_HYPAI            Unreviewed;       322 AA.
AC   G9PAH5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=NADP-dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF00248};
GN   ORFNames=TRIATDRAFT_259849 {ECO:0000313|EMBL:EHK40009.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK40009.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK40009.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC       {ECO:0000256|ARBA:ARBA00004722}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC       {ECO:0000256|ARBA:ARBA00007905}.
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:EHK40009.1}.
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DR   EMBL; ABDG02000028; EHK40009.1; -; Genomic_DNA.
DR   RefSeq; XP_013938171.1; XM_014082696.1.
DR   AlphaFoldDB; G9PAH5; -.
DR   STRING; 452589.G9PAH5; -.
DR   GeneID; 25779059; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   OMA; ECGEGVA; -.
DR   OrthoDB; 8274at2759; -.
DR   UniPathway; UPA00810; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
DR   GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:InterPro.
DR   GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd19115; AKR_AKR2D1; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044487; AKR2D.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR   PANTHER; PTHR11732:SF218; NADPH-DEPENDENT ALDOSE REDUCTASE GRE3; 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.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629}.
FT   DOMAIN          16..300
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        49
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            78
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   322 AA;  36536 MW;  4F8991EBA41EA094 CRC64;
     MAPTLKLNSG YEMPQVGFGL WKVDQATAAD TVYNAIKAGY RLFDGACDYG NEKECGEGVA
     RAIKEGLVKR EELFIVSKLW QTFHDEDKVE PITRKQLADW QIDYFDLFLI HFPAALEYVD
     PKVRYPPGWF YDGESEVRWS KTTLQQTWGA MEKLVEKKLA RSIGISNYQA QSVYDALIYA
     KIRPATLQIE HHPYLQQPDL VNLAQKEGIV VTAYSSFGPT GFMELDMPRA KSAAPLMEHA
     LIKEIAAKHK KTPAQVLLRW ATQRGLAVIP KTSRPEVLAQ NLDSTTFDLE SSDLEKIAEM
     DLNIRFNKPT NYFSADKLFL FG
//
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