FDB95_GIBM7
ID FDB95_GIBM7 Reviewed; 530 AA.
AC W7MLD8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Amidase FVEG_08295 {ECO:0000303|PubMed:26808652};
DE EC=3.5.1.4 {ECO:0000305|PubMed:26808652};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster 1 protein FVEG_08295 {ECO:0000303|PubMed:26808652};
DE Short=FDB1 cluster protein FVEG_08295 {ECO:0000303|PubMed:26808652};
GN ORFNames=FVEG_08295;
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.
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, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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: Amidase; part of the Fusarium detoxification of
CC benzoxazolinone cluster 1 (FDB1) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC Evidence={ECO:0000305|PubMed:26808652};
CC -!- PATHWAY: Xenobiotic degradation. {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 BOA degradation.
CC {ECO:0000269|PubMed:26808652}.
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 amidase family. {ECO:0000305}.
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DR EMBL; DS022252; EWG48584.1; -; Genomic_DNA.
DR RefSeq; XP_018754775.1; XM_018897188.1.
DR STRING; 117187.FVEG_08295T0; -.
DR GeneID; 30066037; -.
DR KEGG; fvr:FVEG_08295; -.
DR VEuPathDB; FungiDB:FVEG_08295; -.
DR eggNOG; KOG1212; Eukaryota.
DR OrthoDB; 852596at2759; -.
DR Proteomes; UP000009096; Chromosome 10.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..530
FT /note="Amidase FVEG_08295"
FT /id="PRO_0000454599"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT ACT_SITE 238
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT BINDING 235..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P97612"
SQ SEQUENCE 530 AA; 58078 MW; 720FAAAE761CF41C CRC64;
MAEVNWQQLI NQKRATREAL IPEQWLLPAT ITSKVTPQST ASAFELLSEA GLLTEREIDI
TEKYTAVSLT AKIATGELSS YDVATAFCKR AAIVHQLTNS LTEIFFDKAL ERARWLDEYL
SKEGKTVGPL HGLPITLKDM IHVKGQYSTM GFVGHLRHPP ADENAVITDM LEAAGAVFYC
KTNVPQTLFV CESFNNVFGR TLNPYKLCLS PGGSSSGEAA QLGLCGSIMG VGSDIAGSVR
VPAIFTGVYG FRPTVNRLPW SKQAELALKG WQGVQPTLGP MARTAQDLTL FMKTIIQAEP
WRYDSTALAI PWHDAPRKDK LTIGVWSQDP QFPVFPPIAR TMASAVGRLR AAGHTIKIIE
APPTMKAMKI AMRWFALDQV NLPLKFVQDG AESPIADLDA MDPGKFLDPG YVADLSENIS
ISADIHDYRE EWAKIWREAG IDVLLCPASR GSAVPHGEFG PLMYTIPWNL LDFPSSVVPF
GKADKTLDSK DGYDSTVVDG APTGFQLVGW RFQDEQTLMA TEVIADTLKA
