FDB38_GIBM7
ID FDB38_GIBM7 Reviewed; 327 AA.
AC W7N2Q9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Aldo-keto reductase FVEG_12638 {ECO:0000303|PubMed:19302487};
DE EC=1.1.1.- {ECO:0000305|PubMed:26808652};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster 2 protein FVEG_12638 {ECO:0000303|PubMed:19302487};
DE Short=FDB2 cluster protein FVEG_12638 {ECO:0000303|PubMed:19302487};
GN ORFNames=FVEG_12638;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2]
RP FUNCTION.
RX PubMed=11876429; DOI=10.1094/mpmi.2002.15.2.91;
RA Glenn A.E., Gold S.E., Bacon C.W.;
RT "Fdb1 and Fdb2, Fusarium verticillioides loci necessary for detoxification
RT of preformed antimicrobials from corn.";
RL Mol. Plant Microbe Interact. 15:91-101(2002).
RN [3]
RP FUNCTION.
RX PubMed=12788712; DOI=10.1128/aem.69.6.3165-3169.2003;
RA Glenn A.E., Meredith F.I., Morrison W.H. III, Bacon C.W.;
RT "Identification of intermediate and branch metabolites resulting from
RT biotransformation of 2-benzoxazolinone by Fusarium verticillioides.";
RL Appl. Environ. Microbiol. 69:3165-3169(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19302487; DOI=10.1111/j.1365-2672.2009.04246.x;
RA Glenn A.E., Bacon C.W.;
RT "FDB2 encodes a member of the arylamine N-acetyltransferase family and is
RT necessary for biotransformation of benzoxazolinones by Fusarium
RT verticillioides.";
RL J. Appl. Microbiol. 107:657-671(2009).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=26808652; DOI=10.1371/journal.pone.0147486;
RA Glenn A.E., Davis C.B., Gao M., Gold S.E., Mitchell T.R., Proctor R.H.,
RA Stewart J.E., Snook M.E.;
RT "Two horizontally transferred xenobiotic resistance gene clusters
RT associated with detoxification of benzoxazolinones by Fusarium species.";
RL PLoS ONE 11:e0147486-e0147486(2016).
CC -!- FUNCTION: Aldo-keto reductase; part of the Fusarium detoxification of
CC benzoxazolinone cluster 2 (FDB2) involved in the degradation of
CC benzoxazolinones produced by the host plant (PubMed:19302487,
CC PubMed:26808652). 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 (PubMed:11876429). The
CC first step in the detoxification of benzoxazolinones involves the
CC hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1
CC cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652,
CC PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-
CC AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP)
CC (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-
CC malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-
CC malonylation to non-toxic malonamic acids (PubMed:19302487,
CC PubMed:12788712). FDB2/NAT1 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:19302487, PubMed:12788712). The
CC duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant
CC function for hydrolyzing the lactone moiety in the BOA molecule
CC (Probable). The roles of the amidases an other enzymes encoded by the 2
CC FDB clusters have not been identified so far (Probable).
CC {ECO:0000269|PubMed:11876429, ECO:0000269|PubMed:12788712,
CC ECO:0000269|PubMed:19302487, ECO:0000269|PubMed:26808652,
CC ECO:0000305|PubMed:26808652}.
CC -!- INDUCTION: Expression is induced in response to 2-benzoxasolinone (BOA)
CC exposure. {ECO:0000269|PubMed:26808652}.
CC -!- DISRUPTION PHENOTYPE: Does not affect tolerance to 2-benzoxazolinone
CC (BOA). {ECO:0000269|PubMed:19302487}.
CC -!- MISCELLANEOUS: Fusarium verticillioides possesses 2 unlinked loci, FDB1
CC and FDB2, necessary for detoxification of antimicrobial compounds
CC produced by maize, including 2-benzoxazolinone (BOA) (Probable). The
CC FDB2 cluster arose as a duplication of the FDB1 cluster with
CC rearrangement and expansion by incorporating additional genes
CC (Probable). {ECO:0000305|PubMed:26808652}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; DS022261; EWG54420.1; -; Genomic_DNA.
DR RefSeq; XP_018760611.1; XM_018901988.1.
DR EnsemblFungi; FVEG_12638T0; FVEG_12638T0; FVEG_12638.
DR GeneID; 30070066; -.
DR KEGG; fvr:FVEG_12638; -.
DR VEuPathDB; FungiDB:FVEG_12638; -.
DR eggNOG; KOG1575; Eukaryota.
DR HOGENOM; CLU_023205_2_1_1; -.
DR OMA; CGIAAFE; -.
DR OrthoDB; 1136766at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
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; Reference proteome.
FT CHAIN 1..327
FT /note="Aldo-keto reductase FVEG_12638"
FT /id="PRO_0000454615"
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; 36914 MW; 8CE54807E9FB48B8 CRC64;
MVKSMRFRDL EVPTPGFGAM GISFALGNDL SYEEAEPVLL KALEQGCTFW DTAVSYGPGK
NEKILGDFIR KYNCRDKLFI ASKCGIAAFE DGSVTNSAEH IKTYIEGTIE RLGFTPDLYY
IHRMDPNTPL EESIPALDSL RKQGKTKYIG LSECSAETLR KANSIARIDA VQAEYSAFET
IHETDGLIDT ARELDIEFIA YGPLGHGWLV EDFPYQTPED FAPEDYRRQI PKWQGENFYA
NKRIADGFRE LAKRKKCTLP QVALAWVAAQ GLISIPGTTK PERLVENFTS RDIELTEEEI
KDMRKLVDVL KPQGDRYNEV AMRSIGK
