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FDB34_GIBM7
ID   FDB34_GIBM7             Reviewed;         546 AA.
AC   W7MSI0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Carboxylic ester hydrolase FVEG_12634 {ECO:0000303|PubMed:19302487};
DE            EC=3.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10039};
DE   AltName: Full=Fusarium detoxification of benzoxazolinone cluster 2 protein FVEG_12634 {ECO:0000303|PubMed:19302487};
DE            Short=FDB2 cluster protein FVEG_12634 {ECO:0000303|PubMed:19302487};
GN   ORFNames=FVEG_12634;
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: Carboxylic ester hydrolase; part of the Fusarium
CC       detoxification of benzoxazolinone cluster 2 (FDB2) involved in the
CC       degradation of benzoxazolinones produced by the host plant
CC       (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2
CC       benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-
CC       3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due
CC       to their inherent instability once released, spontaneously degrade to
CC       the more stable corresponding benzoxazolinones, 6-methoxy-2-
CC       benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively
CC       (PubMed:11876429). The first step in the detoxification of
CC       benzoxazolinones involves the hydrolysis of the cyclic ester bond of
CC       benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to
CC       aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to
CC       convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-
CC       2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2
CC       cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols
CC       via N-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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
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 type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; DS022261; EWG54413.1; -; Genomic_DNA.
DR   RefSeq; XP_018760604.1; XM_018901982.1.
DR   STRING; 334819.W7MSI0; -.
DR   ESTHER; gibm7-w7msi0; Fungal_carboxylesterase_lipase.
DR   GeneID; 30070062; -.
DR   KEGG; fvr:FVEG_12634; -.
DR   VEuPathDB; FungiDB:FVEG_12634; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   OrthoDB; 754103at2759; -.
DR   Proteomes; UP000009096; Chromosome 3.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:RHEA.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Carboxylic ester hydrolase FVEG_12634"
FT                   /id="PRO_0000454624"
FT   REGION          72..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        214
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
SQ   SEQUENCE   546 AA;  62089 MW;  08859A3C777DBE0E CRC64;
     MFDNYSRESY IFNAGSLGHI KGLTITSHGS PAVHYFGGLP YALPPVGQWR FRVPRRLPKD
     YRYGTATEPG KFTDGTKICP QPPSSNTPDP SVVSEDCLQL NIWVPAGPPP IHGWPVCFYI
     HGGFLQVGTS NTKPEDLVSL LNESAFRAIM VLPSYRLNVF GFLASKALAA EASSNGEATG
     NYGLWDQRLA LEWTHENIRL FGGDRSNITV AGYSAGAYST FQQLAHELFR VPEEKAIIRR
     VAMFSNSTGV MPKSLQDQQL QCDELLRRLG INLDLSYDEK LASLRAVPHD RLVQAQIGMR
     ISEFRVLADD AFYPLDLMDK INNGEFAKRM KIRGIRLMNG ECESEHIMYC RWRTPQESYS
     AVYQRLLADF SPEVTQKIME HYCGSSENLP VGYKNWEEFF GRVYANIQVH YLQRGFHNAL
     FTGGLEAGRD VFRYRFERRL DCVAEKIPSE WGVTHLTDIP VWLWGCGYTN GLDDQEKKWL
     KGWNEGFAVF VNGDEVNWGT KNPKDMRRWR RDGKTDVCED NSWEDGLKFW KLVNSGHRGT
     EGKAND
 
 
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