MBL1_GIBM7
ID MBL1_GIBM7 Reviewed; 399 AA.
AC W7MLD5;
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=Gamma-lactamase MBL1 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000305|PubMed:26808652};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster 1 protein MBL1 {ECO:0000303|PubMed:26808652};
DE Short=FDB1 cluster protein MBL1 {ECO:0000303|PubMed:26808652};
DE AltName: Full=Metallo-beta-lactamase 1 {ECO:0000303|PubMed:26808652};
GN Name=MBL1 {ECO:0000303|PubMed:26808652}; ORFNames=FVEG_08291;
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: Gamma-lactamase; 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 and other enzymes encoded by the
CC 2 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 -!- PATHWAY: Xenobiotic degradation. {ECO:0000269|PubMed:12788712,
CC ECO:0000269|PubMed:26808652}.
CC -!- INDUCTION: Expression is induced in response to 2-benzoxasolinone (BOA)
CC exposure. {ECO:0000269|PubMed:26808652}.
CC -!- DISRUPTION PHENOTYPE: Impairs the ability to of metabolize 2-
CC benzoxazolinone (BOA) and thus growth BOA-amended media.
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) (PubMed:26808652).
CC The FDB2 cluster arose as a duplication of the FDB1 cluster with
CC rearrangement and expansion by incorporating additional genes
CC (Probable). {ECO:0000269|PubMed:26808652, ECO:0000305|PubMed:26808652}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; DS022252; EWG48579.1; -; Genomic_DNA.
DR RefSeq; XP_018754770.1; XM_018897183.1.
DR EnsemblFungi; FVEG_08291T0; FVEG_08291T0; FVEG_08291.
DR GeneID; 30066033; -.
DR KEGG; fvr:FVEG_08291; -.
DR VEuPathDB; FungiDB:FVEG_08291; -.
DR eggNOG; ENOG502S1A6; Eukaryota.
DR HOGENOM; CLU_030571_1_0_1; -.
DR OMA; FEAYDFY; -.
DR OrthoDB; 1139836at2759; -.
DR Proteomes; UP000009096; Chromosome 10.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..399
FT /note="Gamma-lactamase MBL1"
FT /id="PRO_0000454592"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
SQ SEQUENCE 399 AA; 44602 MW; 10A6FED93CDB00A9 CRC64;
MLTSPLRQDH LVPETLMADA SPIIRPETPP DLHIPDSQAT VKVSIIDTTS YMSNFPMWAF
LDPLMPGHEE MKGCDFSFII EHPKSGNKYD TLLFDLGVRK DWENLPTPFV QGIKAGGCKI
EVQKDVATIL KDNGRDLSEV GGIIWSHWHF DHVGDAQTFP GTTDVIVGPG FKKAHVPAWP
TDPESHIDEK AWQGRTLREI DFAAEEGKGL KIGQFDALDF YGDGSFYVLN TPGHTIGHLS
ALARTTVDPP TFIFMGGDIA HQGGEFRPTP YMPLPAEISP NPFNRILPRP ALTCPGEIFV
EIHRNKSRTE PFFDPTTAEG AWHHCAHEAK RSIDKLTEFD AYENIFPVIA HDNSLYGVID
VYPKPANDWF AKSWKDKTRW GWLNEFDPSF AGLAKASEP
