Detail Information for IndEnz0010001305
IED ID IndEnz0010001305
Enzyme Type ID esterase001305
Protein Name Gamma-lactamase FDB1
EC 3.1.1.-
Fusarium detoxification of benzoxazolinone cluster protein 1
FDB cluster protein 1
Gene Name FDB1 FPSE_08124
Organism Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium sambucinum species complex Fusarium pseudograminearum (Wheat and barley crown-rot fungus) Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot fungus)
Enzyme Sequence MSSIRLPPPVVIPESQSTVDVYIIDTTSYMSMVPASSFVEPLVSGFETLNAGSYAFLIEHTSSKPSKHDTMVFDLGVRKDWEHLPDTFVAAVKEEGWSIDVQTDVASILRDNGQDLKSVGAIIWSHWHFDHVGDPQTFPSSTDLIVGPGFKQGVMPGWPTAKDSHVNETAWQGRKLIEIDFSGEAALDIGRFQAYDFYGDGSFYLLNSPGHAVGHMSALARTTADPPSFMLLGGDIAHHCGEFRPSPYTPLPNMITPNPLSNTLLACPGRLFLSIHPWKDPERPFFDPTVGPGWHDEGVLAKDSIDKLIEADAYDNIFPVVAHDMTLVGTVDLYPNKANNWMSRGWKEDTRWGFCGDFTPLDEEMVARNGQVEVLEGHHEVRDSAQDPKVTSIVHMESTDVDKKAKLHDPSFV
Enzyme Length 413
Uniprot Accession Number K3VFR8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.1.-
Enzyme Function FUNCTION: Gamma-lactamase; part of the Fusarium detoxification of benzoxazolinone cluster involved in the degradation of benzoxazolinones produced by the host plant (PubMed:26296598, PubMed:25727347, PubMed:26828593). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (By similarity). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the gamma-lactamase FDB1 to aminophenols (PubMed:26296598). FDB1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26296598, PubMed:25727347). The N-malonyltransferase FDB2 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:26296598). FDB2 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:26296598). The cluster contains also 2 transcription factors (FDB3 and FPSE_08121), an aldo-keto reductase (FPSE_08125) that possibly associates with a ketone component of BOA and MBOA degradation, an esterase (FPSE_08126), an acyl-CoA transferase (FPSE_08120), a solute carrier protein (FPSE_08119) and a transmembrane transporter (FPSE_08127) proposed to shuttle metabolites of benzoxazolinone degradation (Probable). {ECO:0000250|UniProtKB:W7MLD5, ECO:0000269|PubMed:25727347, ECO:0000269|PubMed:26296598, ECO:0000269|PubMed:26828593, ECO:0000305|PubMed:26828593}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Xenobiotic degradation. {ECO:0000269|PubMed:26296598}.
nucleotide Binding
Features Chain (1); Metal binding (8)
Keywords Hydrolase;Metal-binding;Zinc
Interact With
Induction INDUCTION: Expression is induced in response to 2-benzoxasolinone (BOA) exposure (PubMed:26296598, PubMed:25727347). Expression is also induced in response to 6-methoxy-2-benzoxazolinone (MBOA) and 2-aminophenol (2-AP) treatment (PubMed:26828593). {ECO:0000269|PubMed:25727347, ECO:0000269|PubMed:26296598, ECO:0000269|PubMed:26828593}.
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,704
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.19 mM for 2-benzoxasolinone (BOA) {ECO:0000269|PubMed:26296598};
Metal Binding METAL 126; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q7B8B9; METAL 128; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q7B8B9; METAL 130; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q7B8B9; METAL 131; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q7B8B9; METAL 211; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q7B8B9; METAL 235; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q7B8B9; METAL 235; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q7B8B9; METAL 323; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q7B8B9
Rhea ID
Cross Reference Brenda 3.5.2.B2;