FDB20_FUSPC
ID FDB20_FUSPC Reviewed; 456 AA.
AC K3VD64;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Acyl-CoA transferase FPSE_08120 {ECO:0000303|PubMed:25727347};
DE EC=2.8.3.- {ECO:0000305|PubMed:26828593};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster protein FPSE_08120 {ECO:0000303|PubMed:25727347};
DE Short=FDB cluster protein FPSE_08120 {ECO:0000303|PubMed:25727347};
DE Flags: Precursor;
GN ORFNames=FPSE_08120;
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: Acyl-CoA transferase; 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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
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 CoA-transferase III family. {ECO:0000305}.
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DR EMBL; AFNW01000283; EKJ71674.1; -; Genomic_DNA.
DR RefSeq; XP_009259513.1; XM_009261238.1.
DR STRING; 101028.EKJ71674; -.
DR EnsemblFungi; EKJ71674; EKJ71674; FPSE_08120.
DR GeneID; 20366738; -.
DR KEGG; fpu:FPSE_08120; -.
DR eggNOG; KOG3957; Eukaryota.
DR HOGENOM; CLU_033975_0_1_1; -.
DR InParanoid; K3VD64; -.
DR Proteomes; UP000007978; Chromosome 2.
DR Proteomes; UP000007978; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Mitochondrion; Transferase; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..456
FT /note="Acyl-CoA transferase FPSE_08120"
FT /id="PRO_0000454612"
SQ SEQUENCE 456 AA; 49273 MW; EF9095974E12E5D5 CRC64;
MARLLFSGQR LRPSFLRSYI RANPSSTPSA TRAAINYRYN SNNAALQSAS SSQGALTGIK
IIDLSRVLAG PFCTQILADY GAEVTKVEAV GKGDDTRHWI MAGEKASWNE SSGPISNYFA
AVNRNKRSIT VNFKKAEGRQ LILDLIKDAD VVVENFKPGT MERLGLGYDV LKELNPRIIY
AGLSGYGRTG PYRTRGGYDP IAAAEAGLLH VTGEKNGPPV RAGIGLVDMS TGLFLHGAIL
SALIARARDG TGQRVDASLF ETQLSLLTNV GLAWLNLGIE AERWGCQHPS IAPYDAFKTR
DRYLVCGATN DNQYAALCCL LGVEHLVTDP RFITNPLRVQ HREELAALLG PIFASKTIDE
WIALFEPSGL PFGPINNMEA TFAHPQTAAR DMVIDVPMDA ACAGSIKVIG PAVKFGDSKT
GLRTGPPRLG QHTVEILEEI GMDAEAIAKY KEDGII
