ID   FDB25_FUSPC             Reviewed;         327 AA.
AC   K3VD70;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Aldo-keto reductase FPSE_08125 {ECO:0000303|PubMed:25727347};
DE            EC=1.1.1.- {ECO:0000305|PubMed:26828593};
DE   AltName: Full=Fusarium detoxification of benzoxazolinone cluster protein FPSE_08125 {ECO:0000303|PubMed:25727347};
DE            Short=FDB cluster protein FPSE_08125 {ECO:0000303|PubMed:25727347};
GN   ORFNames=FPSE_08125;
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096;
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
RN   [2]
RP   FUNCTION.
RX   PubMed=26296598; DOI=10.1016/j.fgb.2015.08.005;
RA   Kettle A.J., Carere J., Batley J., Benfield A.H., Manners J.M., Kazan K.,
RA   Gardiner D.M.;
RT   "A gamma-lactamase from cereal infecting Fusarium spp. catalyses the first
RT   step in the degradation of the benzoxazolinone class of phytoalexins.";
RL   Fungal Genet. Biol. 83:1-9(2015).
RN   [3]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=25727347; DOI=10.1111/mpp.12250;
RA   Kettle A.J., Batley J., Benfield A.H., Manners J.M., Kazan K.,
RA   Gardiner D.M.;
RT   "Degradation of the benzoxazolinone class of phytoalexins is important for
RT   virulence of Fusarium pseudograminearum towards wheat.";
RL   Mol. Plant Pathol. 16:946-962(2015).
RN   [4]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26828593; DOI=10.1016/j.fgb.2016.01.015;
RA   Kettle A.J., Carere J., Batley J., Manners J.M., Kazan K., Gardiner D.M.;
RT   "The Fdb3 transcription factor of the Fusarium Detoxification of
RT   Benzoxazolinone gene cluster is required for MBOA but not BOA degradation
RT   in Fusarium pseudograminearum.";
RL   Fungal Genet. Biol. 88:44-53(2016).
CC   -!- FUNCTION: Aldo-keto reductase; part of the Fusarium detoxification of
CC       benzoxazolinone cluster involved in the degradation of benzoxazolinones
CC       produced by the host plant (PubMed:26296598, PubMed:25727347,
CC       PubMed:26828593). Maize, wheat, and rye produce the 2 benzoxazinone
CC       phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)
CC       and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their
CC       inherent instability once released, spontaneously degrade to the more
CC       stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone
CC       (MBOA) and 2-benzoxazolinone (BOA), respectively (By similarity). The
CC       first step in the detoxification of benzoxazolinones involves the
CC       hydrolysis of the cyclic ester bond of benzoxazolinones by the gamma-
CC       lactamase FDB1 to aminophenols (PubMed:26296598). FDB1 is able to
CC       convert 2-benzoxazolinone (BOA) into 2-aminophenol (2-AP), as well as
CC       6-methoxy-2-benzoxazolinone (MBOA) into 5-methoxy-2-aminophenol (2-AMP)
CC       (PubMed:26296598, PubMed:25727347). The N-malonyltransferase FDB2 then
CC       metabolizes aminophenols via N-malonylation to non-toxic malonamic
CC       acids (PubMed:26296598). FDB2 converts 2-AP into N-(2-hydroxyphenyl)
CC       malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl)
CC       malonamic acid (HMPMA) (PubMed:26296598). The cluster contains also 2
CC       transcription factors (FDB3 and FPSE_08121), an aldo-keto reductase
CC       (FPSE_08125) that possibly associates with a ketone component of BOA
CC       and MBOA degradation, an esterase (FPSE_08126), an acyl-CoA transferase
CC       (FPSE_08120), a solute carrier protein (FPSE_08119) and a transmembrane
CC       transporter (FPSE_08127) proposed to shuttle metabolites of
CC       benzoxazolinone degradation (Probable). {ECO:0000250|UniProtKB:W7MLD5,
CC       ECO:0000269|PubMed:25727347, ECO:0000269|PubMed:26296598,
CC       ECO:0000269|PubMed:26828593, ECO:0000305|PubMed:26828593}.
CC   -!- INDUCTION: Expression is induced in response to 2-benzoxasolinone (BOA)
CC       exposure (PubMed:25727347). Expression is also induced in response to
CC       6-methoxy-2-benzoxazolinone (MBOA) and 2-aminophenol (2-AP) treatment
CC       (PubMed:26828593). {ECO:0000269|PubMed:25727347,
CC       ECO:0000269|PubMed:26828593}.
CC   -!- DISRUPTION PHENOTYPE: Shows significantly reduced growth but does not
CC       affect tolerance to benzoxazolinone. {ECO:0000269|PubMed:26828593}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC       reductase 2 subfamily. {ECO:0000305}.
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DR   EMBL; AFNW01000283; EKJ71679.1; -; Genomic_DNA.
DR   RefSeq; XP_009259518.1; XM_009261243.1.
DR   STRING; 101028.EKJ71679; -.
DR   EnsemblFungi; EKJ71679; EKJ71679; FPSE_08125.
DR   GeneID; 20366743; -.
DR   KEGG; fpu:FPSE_08125; -.
DR   eggNOG; KOG1575; Eukaryota.
DR   HOGENOM; CLU_023205_2_1_1; -.
DR   InParanoid; K3VD70; -.
DR   Proteomes; UP000007978; Chromosome 2.
DR   Proteomes; UP000007978; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..327
FT                   /note="Aldo-keto reductase FPSE_08125"
FT                   /id="PRO_0000454614"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         51
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         152..153
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         202..212
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         286..294
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
SQ   SEQUENCE   327 AA;  36586 MW;  7F7884DB227675CE CRC64;
     MVKSLRFGDL DVPVPGFGAM GISFALGNDL SYEQAEPVLL EALKQGCTFW DTAVSYGPGK
     NEKLIGEFVK KHNCRDKLFI ASKCGVAAFE DGSITNSAEH IQAYIEGTIE RLGFTPDLYY
     IHRMDPNTPL EESIPAMDLL RKQGKTKYIG LSECSAETLR KANSIAKIDA VQAEYSAFET
     LHETDGLVDT ARELDISFIA YAPLGHGWLV ENFPYETPDD FAPDDYRRQI PKWQGDNFYA
     NKRIADKFKE LARKKNCTLP QIAIAWIAAQ GMIAIPGTTK PERLIENFAA REIEIAEEEN
     KEMRKLVDAL KPQGDRYSES AMKNIGK