FDB26_FUSPC
ID FDB26_FUSPC Reviewed; 324 AA.
AC K3VZ29;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Esterase FPSE_08126 {ECO:0000303|PubMed:25727347};
DE EC=3.1.1.- {ECO:0000305|PubMed:26828593};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster protein FPSE_08126 {ECO:0000303|PubMed:25727347};
DE Short=FDB cluster protein FPSE_08126 {ECO:0000303|PubMed:25727347};
GN ORFNames=FPSE_08126;
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: Esterase; 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: Does not affect tolerance to benzoxazolinone.
CC {ECO:0000269|PubMed:26828593}.
CC -!- SIMILARITY: Belongs to the AB hydrolase 3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFNW01000283; EKJ71680.1; -; Genomic_DNA.
DR RefSeq; XP_009259519.1; XM_009261244.1.
DR STRING; 101028.EKJ71680; -.
DR EnsemblFungi; EKJ71680; EKJ71680; FPSE_08126.
DR GeneID; 20366744; -.
DR KEGG; fpu:FPSE_08126; -.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_6_0_1; -.
DR InParanoid; K3VZ29; -.
DR Proteomes; UP000007978; Chromosome 2.
DR Proteomes; UP000007978; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Hydrolase.
FT CHAIN 1..324
FT /note="Esterase FPSE_08126"
FT /id="PRO_0000454616"
FT ACT_SITE 156
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 255
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 285
FT /evidence="ECO:0000250|UniProtKB:O06350"
SQ SEQUENCE 324 AA; 36227 MW; EC2A10EBD4F781E4 CRC64;
MFDLDPINAA FYDQIKDLPC PHQMGGYQQA YDSLEQIQKH DAAPDIDTTT IQVGKRYGPT
TVTLFRLKTL VDKPLPMVFY THGGGWIMGS AKSFAVLMED LARRTQAVIV FPDYTRVPHQ
TFPYPLEQSY EVLDYMVRHS NQHQILHGTI ALAGDSVGGH MAIAMMQMSL ERKLPTQIGQ
LVLWAPVTIT YKKLGSYTTF SHAPFLTEDS MDWMIESFLP NKEDRQTALA SPLTHLSDEV
LAQFPPTIIF LSTVDPLLDE GVAFGHRLQK NGVDASIMKA EGQMHAFCAV KALRDGPTAR
AVIDLAALRL RRIFPQRDTP GHPS
