ID   FDB29_GIBM7             Reviewed;         569 AA.
AC   W7N463;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Acyl-CoA transferase FVEG_12629 {ECO:0000303|PubMed:19302487};
DE            EC=2.8.3.- {ECO:0000305|PubMed:19302487};
DE   AltName: Full=Fusarium detoxification of benzoxazolinone cluster 2 protein FVEG_12629 {ECO:0000303|PubMed:19302487};
DE            Short=FDB2 cluster protein FVEG_12629 {ECO:0000303|PubMed:19302487};
GN   ORFNames=FVEG_12629;
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: Acyl-CoA transferase; part of the Fusarium detoxification of
CC       benzoxazolinone cluster 2 (FDB2) involved in the degradation of
CC       benzoxazolinones produced by the host plant (PubMed:19302487,
CC       PubMed:26808652). 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 (PubMed:11876429). The
CC       first step in the detoxification of benzoxazolinones involves the
CC       hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1
CC       cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652,
CC       PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-
CC       AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP)
CC       (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-
CC       malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-
CC       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   -!- 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 CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; DS022261; EWG54409.1; -; Genomic_DNA.
DR   RefSeq; XP_018760600.1; XM_018901979.1.
DR   STRING; 117187.FVEG_12629T0; -.
DR   EnsemblFungi; FVEG_12629T0; FVEG_12629T0; FVEG_12629.
DR   GeneID; 30070059; -.
DR   KEGG; fvr:FVEG_12629; -.
DR   VEuPathDB; FungiDB:FVEG_12629; -.
DR   eggNOG; KOG3957; Eukaryota.
DR   HOGENOM; CLU_021588_1_1_1; -.
DR   OMA; TIMCGIR; -.
DR   OrthoDB; 776830at2759; -.
DR   Proteomes; UP000009096; Chromosome 3.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 2.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..569
FT                   /note="Acyl-CoA transferase FVEG_12629"
FT                   /id="PRO_0000454613"
SQ   SEQUENCE   569 AA;  62501 MW;  332E4127D07056B6 CRC64;
     MTTKTSNETY GAGTVVDSEF SPLPAECERI LRIFAARTPG FTKDEALLSG VNFHGDDLPC
     IPGPIKSQAV TAVLHAMVGI VGLEILHLRG VTTDNQIDID VNHAGLYPAT AALVDIDGVT
     GPEVIKLPTV PQWDKDRASN SPLVYRATAI YETADSGVWF QLHGSLDSWK VLALLGIGKD
     LDSEIRTNDA AYELIQERVR KYRAREIEQL VVEKGLSGSI VYSPEEWRQT EMGRSLSRHP
     LVNYKQKSHC ATLAPASFPV LEDKRPLAGI KVVELTRIIA GAAAGAALAS LGAEVIRVNS
     SKLKDYTPAQ PSSLMAGKKT IDLDLEDPAD HKKLMQLFEQ ADVILQGYRL GSLARRGFGL
     EAALELANKR GRGVVYVDEN CYGPDGYYAE RPGWQQVADA AAGSSYVMGQ SFGFPKGQGV
     LPSLPISDMS TGILTALTIM CGIRDRAKFG GSYHGHASLT AYNMATLDSE VRLYQREVVQ
     KISDKYEFPT WSSDVHVAPL YYSILDAWGK KSELIKDEKH YIHFSDSVFG SDLRVLGPVV
     RYDKEEYSPK WNSPPVPFCH HEFTMFSNQ