AMD2_GIBM7
ID AMD2_GIBM7 Reviewed; 512 AA.
AC W7MTI6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Amidase 2 {ECO:0000303|PubMed:26808652};
DE EC=3.5.1.4 {ECO:0000305|PubMed:26808652};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster 2 protein AMD2 {ECO:0000303|PubMed:26808652};
DE Short=FDB2 cluster protein AMD2 {ECO:0000303|PubMed:26808652};
GN Name=AMD2 {ECO:0000303|PubMed:26808652}; ORFNames=FVEG_17313;
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, 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 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 -!- 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 not induced in response to 2-benzoxazolinone
CC (BOA) exposure. {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; DS022261; EWG54411.1; -; Genomic_DNA.
DR RefSeq; XP_018760602.1; XM_018906570.1.
DR STRING; 117187.FVEG_12632T0; -.
DR GeneID; 30074189; -.
DR KEGG; fvr:FVEG_17313; -.
DR VEuPathDB; FungiDB:FVEG_17313; -.
DR eggNOG; KOG1212; Eukaryota.
DR OrthoDB; 852596at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..512
FT /note="Amidase 2"
FT /id="PRO_0000454598"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT ACT_SITE 221
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P97612"
FT BINDING 218..221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P97612"
SQ SEQUENCE 512 AA; 56633 MW; 5EFD34493C75B145 CRC64;
MTTSKDTTKV HKPWTEVVTE KRALRDARID KHLKSDIKFP SDGISFETVD IDVLTSLLRD
RKVSAVEVIH AHSRACEAQK QTNCLTEICF DDALEQATQL DEFQQEHGQL MGPLHGVPVT
VKDQFNIRGL DSTLGYVAKA FSPAESDAPL VQTLKKLGAV IIAKTNLPQS IMWCETNNPL
WGLTTHPEDP KLTPGGSSGG EAAMLLMGAS IIGWGTDIGG SIRIPCHMNG LWGLKPSSGR
LSYRGVEVTL EGQQHIPSAV GPMARSLSCL KLVTKLAIEA EPWAIDPQLP PVPWRDGIFQ
ATSTRPLSVF RDLVTKLEAA GHEVIEWDSS LNSSIIDIMD GYYSADGGED IRSAVSAGGE
PFIPQIQAFV NRGEPISVFE YWQLNKRKIA IQEAYHDMWD NKRSPTSRPV DVLLVPTMPH
TAVPHGSCRW TGYTKIFNLL DYTALTFPAG KAPRGENDGS FWEHVPRNEV DAWNQRLYDP
VTMGGRHVGL QIVGRRFEEE KVPIVLKPKC IF
