FDB1_FUSPC
ID FDB1_FUSPC Reviewed; 413 AA.
AC K3VFR8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Gamma-lactamase FDB1 {ECO:0000303|PubMed:26296598};
DE EC=3.1.1.- {ECO:0000305|PubMed:26296598};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster protein 1 {ECO:0000303|PubMed:26296598};
DE Short=FDB cluster protein 1 {ECO:0000303|PubMed:26296598};
GN Name=FDB1 {ECO:0000303|PubMed:26296598}; ORFNames=FPSE_08124;
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096;
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
RN [2]
RP FUNCTION, INDUCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=26296598; DOI=10.1016/j.fgb.2015.08.005;
RA Kettle A.J., Carere J., Batley J., Benfield A.H., Manners J.M., Kazan K.,
RA Gardiner D.M.;
RT "A gamma-lactamase from cereal infecting Fusarium spp. catalyses the first
RT step in the degradation of the benzoxazolinone class of phytoalexins.";
RL Fungal Genet. Biol. 83:1-9(2015).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=25727347; DOI=10.1111/mpp.12250;
RA Kettle A.J., Batley J., Benfield A.H., Manners J.M., Kazan K.,
RA Gardiner D.M.;
RT "Degradation of the benzoxazolinone class of phytoalexins is important for
RT virulence of Fusarium pseudograminearum towards wheat.";
RL Mol. Plant Pathol. 16:946-962(2015).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=26828593; DOI=10.1016/j.fgb.2016.01.015;
RA Kettle A.J., Carere J., Batley J., Manners J.M., Kazan K., Gardiner D.M.;
RT "The Fdb3 transcription factor of the Fusarium Detoxification of
RT Benzoxazolinone gene cluster is required for MBOA but not BOA degradation
RT in Fusarium pseudograminearum.";
RL Fungal Genet. Biol. 88:44-53(2016).
CC -!- FUNCTION: Gamma-lactamase; part of the Fusarium detoxification of
CC benzoxazolinone cluster involved in the degradation of benzoxazolinones
CC produced by the host plant (PubMed:26296598, PubMed:25727347,
CC PubMed:26828593). 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 (By similarity). The
CC first step in the detoxification of benzoxazolinones involves the
CC hydrolysis of the cyclic ester bond of benzoxazolinones by the gamma-
CC lactamase FDB1 to aminophenols (PubMed:26296598). FDB1 is able to
CC convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-
CC 2-aminophenol (2-AMP) (PubMed:26296598, PubMed:25727347). The N-
CC malonyltransferase FDB2 then metabolizes aminophenols via N-
CC malonylation to non-toxic malonamic acids (PubMed:26296598). FDB2
CC converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP
CC into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA)
CC (PubMed:26296598). The cluster contains also 2 transcription factors
CC (FDB3 and FPSE_08121), an aldo-keto reductase (FPSE_08125) that
CC possibly associates with a ketone component of BOA and MBOA
CC degradation, an esterase (FPSE_08126), an acyl-CoA transferase
CC (FPSE_08120), a solute carrier protein (FPSE_08119) and a transmembrane
CC transporter (FPSE_08127) proposed to shuttle metabolites of
CC benzoxazolinone degradation (Probable). {ECO:0000250|UniProtKB:W7MLD5,
CC ECO:0000269|PubMed:25727347, ECO:0000269|PubMed:26296598,
CC ECO:0000269|PubMed:26828593, ECO:0000305|PubMed:26828593}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for 2-benzoxasolinone (BOA) {ECO:0000269|PubMed:26296598};
CC -!- PATHWAY: Xenobiotic degradation. {ECO:0000269|PubMed:26296598}.
CC -!- INDUCTION: Expression is induced in response to 2-benzoxasolinone (BOA)
CC exposure (PubMed:26296598, PubMed:25727347). Expression is also induced
CC in response to 6-methoxy-2-benzoxazolinone (MBOA) and 2-aminophenol (2-
CC AP) treatment (PubMed:26828593). {ECO:0000269|PubMed:25727347,
CC ECO:0000269|PubMed:26296598, ECO:0000269|PubMed:26828593}.
CC -!- DISRUPTION PHENOTYPE: Reduces the tolerance to benzoxazolinones but not
CC to aminophenols. {ECO:0000269|PubMed:26296598}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AFNW01000283; EKJ71678.1; -; Genomic_DNA.
DR RefSeq; XP_009259517.1; XM_009261242.1.
DR EnsemblFungi; EKJ71678; EKJ71678; FPSE_08124.
DR GeneID; 20366742; -.
DR KEGG; fpu:FPSE_08124; -.
DR eggNOG; ENOG502S1A6; Eukaryota.
DR HOGENOM; CLU_030571_1_0_1; -.
DR InParanoid; K3VFR8; -.
DR BRENDA; 3.5.2.B2; 14501.
DR Proteomes; UP000007978; Chromosome 2.
DR Proteomes; UP000007978; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..413
FT /note="Gamma-lactamase FDB1"
FT /id="PRO_0000454591"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
SQ SEQUENCE 413 AA; 45704 MW; 3C295AF49CEC5A2A CRC64;
MSSIRLPPPV VIPESQSTVD VYIIDTTSYM SMVPASSFVE PLVSGFETLN AGSYAFLIEH
TSSKPSKHDT MVFDLGVRKD WEHLPDTFVA AVKEEGWSID VQTDVASILR DNGQDLKSVG
AIIWSHWHFD HVGDPQTFPS STDLIVGPGF KQGVMPGWPT AKDSHVNETA WQGRKLIEID
FSGEAALDIG RFQAYDFYGD GSFYLLNSPG HAVGHMSALA RTTADPPSFM LLGGDIAHHC
GEFRPSPYTP LPNMITPNPL SNTLLACPGR LFLSIHPWKD PERPFFDPTV GPGWHDEGVL
AKDSIDKLIE ADAYDNIFPV VAHDMTLVGT VDLYPNKANN WMSRGWKEDT RWGFCGDFTP
LDEEMVARNG QVEVLEGHHE VRDSAQDPKV TSIVHMESTD VDKKAKLHDP SFV
