FDB2_FUSPC
ID FDB2_FUSPC Reviewed; 343 AA.
AC K3VCL0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 23-FEB-2022, entry version 25.
DE RecName: Full=N-malonyltransferase FDB2 {ECO:0000303|PubMed:25727347};
DE EC=2.3.1.- {ECO:0000269|PubMed:25727347};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster protein 2 {ECO:0000303|PubMed:25727347};
DE Short=FDB cluster protein 2 {ECO:0000303|PubMed:25727347};
GN Name=FDB2 {ECO:0000303|PubMed:25727347}; ORFNames=FPSE_08123;
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, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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, AND INDUCTION.
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: N-malonyltransferase; 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 BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-
CC 2-aminophenol (2-AMP) (PubMed:26296598, PubMed:25727347). The N-
CC malonyltransferase FDB2 then metabolizes aminophenols via N-
CC malonylation to non-toxic malonamic acids (PubMed:26296598). FDB2
CC converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP
CC into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA)
CC (PubMed:26296598). The cluster contains also 2 transcription factors
CC (FDB3 and FPSE_08121), an aldo-keto reductase (FPSE_08125) that
CC possibly associates with a ketone component of BOA and MBOA
CC 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 -!- PATHWAY: Xenobiotic degradation. {ECO:0000269|PubMed:25727347}.
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: Significantly reduced growth on medium amended
CC with BOA or 6-methoxy-2-benzoxazolinone (MBOA) and no growth on 2-
CC aminophenol (2-AP) (PubMed:25727347). Leads to the accumulation of 2-
CC amino-3H-phenoxazin-3-one (2-APO), a compound resulting from
CC spontaneous oxidation of 2-AP, when grown on BOA-amended medium
CC (PubMed:25727347). Results also in reduced virulence (PubMed:25727347).
CC {ECO:0000269|PubMed:25727347}.
CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AFNW01000283; EKJ71677.1; -; Genomic_DNA.
DR RefSeq; XP_009259516.1; XM_009261241.1.
DR EnsemblFungi; EKJ71677; EKJ71677; FPSE_08123.
DR GeneID; 20366741; -.
DR KEGG; fpu:FPSE_08123; -.
DR eggNOG; ENOG502RD0D; Eukaryota.
DR HOGENOM; CLU_049918_2_0_1; -.
DR InParanoid; K3VCL0; -.
DR PHI-base; PHI:4601; -.
DR Proteomes; UP000007978; Chromosome 2.
DR Proteomes; UP000007978; Unassembled WGS sequence.
DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001447; Arylamine_N-AcTrfase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR11786; PTHR11786; 1.
DR Pfam; PF00797; Acetyltransf_2; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Transferase.
FT CHAIN 1..343
FT /note="N-malonyltransferase FDB2"
FT /id="PRO_0000454594"
FT ACT_SITE 107
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WJI5"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WJI5"
FT ACT_SITE 170
FT /evidence="ECO:0000250|UniProtKB:P9WJI5"
SQ SEQUENCE 343 AA; 39832 MW; 264C7FED603541C9 CRC64;
MSCLPEPTVL TQLWVDNPPR YSQAQLQDYL KVIKLPQRFL NSAVLKDSSL AHTKEHGLPL
LKAITRYHAC NVPFENLELH YSAHKTITLD PVELFEKIVT RRRGGRCMEN NTFLGTVFRS
FGYEVRDCGG RVARAMSPYP DVRKNQAYTY DGWNHMLNLV YLEDEWYVVD VGMGSMGPNL
PFPLRHGFET MSIAPRKIRL QRRPIAESHA SNPTKGTELW CYDVCLKPTK DGTEVWIPTY
AFTETEFLPQ DYEVMSWFTS TNPRSFFTRY VTCTKMIQDE EKEEIIGNLT LFKDTIRETI
GNQRKVVREC KTEEERIQAL VEIFDVNLTD EEKNGLPEER RLA
