FDB87_GIBM7
ID FDB87_GIBM7 Reviewed; 303 AA.
AC W7MC44;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=NmrA-like family domain-containing oxidoreductase FVEG_08287 {ECO:0000303|PubMed:26808652};
DE EC=1.-.-.- {ECO:0000305|PubMed:26808652};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster 1 protein FVEG_08287 {ECO:0000303|PubMed:26808652};
DE Short=FDB1 cluster protein FVEG_08287 {ECO:0000303|PubMed:26808652};
GN ORFNames=FVEG_08287;
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.
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: NmrA-like family domain-containing oxidoreductase; part of
CC the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1)
CC involved in the degradation of benzoxazolinones produced by the host
CC plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce
CC the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-
CC benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one
CC (DIBOA) that, due to their inherent instability once released,
CC spontaneously degrade to the more stable corresponding
CC benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-
CC benzoxazolinone (BOA), respectively (PubMed:11876429). The first step
CC in the detoxification of benzoxazolinones involves the hydrolysis of
CC the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-
CC lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1
CC is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into
CC 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The
CC FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes
CC aminophenols via N-malonylation to non-toxic malonamic acids
CC (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-
CC hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-
CC methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487,
CC PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2
CC may provide redundant function for hydrolyzing the lactone moiety in
CC the BOA molecule (Probable). The roles of the amidases an other enzymes
CC encoded by the 2 FDB clusters have not been identified so far
CC (Probable). {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 -!- 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 NmrA-type oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; DS022252; EWG48576.1; -; Genomic_DNA.
DR RefSeq; XP_018754767.1; XM_018897181.1.
DR EnsemblFungi; FVEG_08287T0; FVEG_08287T0; FVEG_08287.
DR GeneID; 30066031; -.
DR KEGG; fvr:FVEG_08287; -.
DR VEuPathDB; FungiDB:FVEG_08287; -.
DR eggNOG; ENOG502QPPB; Eukaryota.
DR HOGENOM; CLU_059949_0_0_1; -.
DR OMA; AQDKTEW; -.
DR OrthoDB; 1106256at2759; -.
DR Proteomes; UP000009096; Chromosome 10.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05259; PCBER_SDR_a; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR InterPro; IPR045312; PCBER-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..303
FT /note="NmrA-like family domain-containing oxidoreductase
FT FVEG_08287"
FT /id="PRO_0000454621"
FT BINDING 8..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 8..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 36..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 56..57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 77..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 159..162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
SQ SEQUENCE 303 AA; 33580 MW; 4CCDDABD97A3C2BA CRC64;
MSDNILVLGA GELGTAILEA LAKHPSRANA KLSVLLRPSS INSTAPEKKK QIEHLQGLGI
TPQPGDVESS TSELAAIFRN YDTIISCNGM GRPFGTQTKL ADAVFEAGVK RYFPWQFGMD
YDAIGTGSDQ DRFDEQINIR KKLRAQNKTE WTIVSTGLFM SFLFLTDFGV INLEQKVTRG
LGTWDTKITV TVPRDIGRVT ADIVFDPRGI ANEVVHIAGD TLSYKEIADL VDERFGEGTF
RRELWDMETL KKQLAEGRPV AEYKATFAVG KGVAWDREGT VNMARGIQMT GLREYLKDVN
LVK
