ID   PRD1_MAGO7              Reviewed;         328 AA.
AC   G4MZI3; Q3MSM6;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=NAD(P)H-dependent pentose reductase;
DE            Short=PRD;
DE            EC=1.1.1.-;
GN   Name=PRD1; Synonyms=ARD1; ORFNames=MGG_01404;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   INDUCTION.
RC   STRAIN=P1.2;
RX   PubMed=23499935; DOI=10.1016/j.febslet.2013.03.003;
RA   Klaubauf S., Ribot C., Melayah D., Lagorce A., Lebrun M.H., de Vries R.P.;
RT   "The pentose catabolic pathway of the rice-blast fungus Magnaporthe oryzae
RT   involves a novel pentose reductase restricted to few fungal species.";
RL   FEBS Lett. 587:1346-1352(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Pentose reductase with a broad substrate affinity involved in
CC       pentose catabolism. Has highest reductase activities with L-arabinose
CC       and D-xylose as substrates, and displays much lower activities with D-
CC       ribose, D-galactose and D-glucose. Has highest dehydrogenase activity
CC       with L-arabitol as substrate, followed by xylitol and D-sorbitol. May
CC       be responsible for the first step of the L-arabinose catabolic pathway.
CC       {ECO:0000269|PubMed:23499935}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=19.7 mM for L-arabinose {ECO:0000269|PubMed:23499935};
CC         KM=19.9 mM for D-xylose {ECO:0000269|PubMed:23499935};
CC         Vmax=0.36 umol/min/mg enzyme for L-arabinose
CC         {ECO:0000269|PubMed:23499935};
CC         Vmax=0.244 umol/min/mg enzyme for D-xylose
CC         {ECO:0000269|PubMed:23499935};
CC   -!- INDUCTION: Overexpressed during growth on both D-xylose or L-arabinose
CC       compared to D-glucose. Significantly expressed during late stages of
CC       infection of barley leaves. {ECO:0000269|PubMed:23499935}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ890448; CAI67592.1; -; mRNA.
DR   EMBL; CM001232; EHA54542.1; -; Genomic_DNA.
DR   RefSeq; XP_003714349.1; XM_003714301.1.
DR   AlphaFoldDB; G4MZI3; -.
DR   SMR; G4MZI3; -.
DR   STRING; 318829.MGG_01404T0; -.
DR   EnsemblFungi; MGG_01404T0; MGG_01404T0; MGG_01404.
DR   GeneID; 2679231; -.
DR   KEGG; mgr:MGG_01404; -.
DR   VEuPathDB; FungiDB:MGG_01404; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; G4MZI3; -.
DR   OMA; TYNTGER; -.
DR   OrthoDB; 1016440at2759; -.
DR   SABIO-RK; G4MZI3; -.
DR   Proteomes; UP000009058; Chromosome 2.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
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.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="NAD(P)H-dependent pentose reductase"
FT                   /id="PRO_0000425414"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         223..232
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         279..289
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   328 AA;  37106 MW;  56D010239B43981D CRC64;
     MAKTSIKLNS GYEMPLVGFG IWKVPVDKTA QAVYDAIKLG YRQIDGAYDY TNSKEAGEGV
     RRAIEEGIVK REDLFITSKL WNNYHKHEHA IEMAKHEVDT WGIGYLDLFL IHFPISLEYI
     SHSKMPYPCF WPDREKSRST PLQYTPVAET WAALESLVKT DSNPDGILRS IGVANFRAQL
     LTDLWGSAKI KPAVNQIEHH PYLVQPQLLA FLKDHGIAIT AYSSFGPQSF VELDHPRVSK
     VEPLFTHPTI KAIADKHGRT GAQVLLRWAT QRDIVVIPKS NNVDRLKQNL DCVSFDLSDD
     EVKQISDLDC GVRFNDPADL SPPIYIFD