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; |