Detail Information for IndEnz0007000546
IED ID IndEnz0007000546
Enzyme Type ID catalase000546
Protein Name Chanoclavine-I aldehyde reductase fgaOx3
EC 1.3.1.100
Isofumigaclavine biosynthesis protein fgaOx3
Old yellow enzyme homolog fgaOx3
OYE fgaOx3
Gene Name fgaOx3 PROQFM164_S03g000127
Organism Penicillium roqueforti (strain FM164)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium roqueforti Penicillium roqueforti (strain FM164)
Enzyme Sequence MTKLFTPLHVGRMELANRIAMAPMTRYRASDNHVPLPIMKDYYAQRASVPGTLLITEATTISARAGGYANAPGIYNDAQIAAWKEVTDAVHAKGSYIYVQLWAVGRPANPQLLQAEGGYDLVSSSATAVSADAPTPRALSETEIYAWIADYAQAARNAVAAGFDGVEIHAANGYLIDQFTQDICNTRTDAWGGSVQGRARFALEVSRAVVEAVGADRTGIRFSPWSTFQGMRMKDPKPQFEYLAVQTAKLGLAYVHLVESRIAGGADVDATDRLDFFLRAYGKASPVIFAGGYDAESAVRAVDVEYADYDAIVGIGRPFISNPDLPFRVQNGIPFVPYDRATFYVPKDPKGYTDYAFSAEFQKAIEAAA
Enzyme Length 369
Uniprot Accession Number W6Q9S9
Absorption
Active Site ACT_SITE 174; /note=Proton donor; /evidence=ECO:0000269|PubMed:28902217
Activity Regulation
Binding Site BINDING 58; /note=FMN; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 100; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 169; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 169; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q02899; BINDING 172; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q02899; BINDING 292; /note=FMN; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q4WZ70; BINDING 317; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q02899; BINDING 344; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q02899
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=dihydrochanoclavine-I aldehyde + NADP(+) = chanoclavine-I aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:35947, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65032, ChEBI:CHEBI:71487; EC=1.3.1.100; Evidence={ECO:0000269|PubMed:28902217};
DNA Binding
EC Number 1.3.1.100
Enzyme Function FUNCTION: Chanoclavine-I aldehyde reductase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids (PubMed:28902217). The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:28620689). The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan (PubMed:28620689). The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:28902217). The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:28620689, PubMed:28902217). The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689). Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A (PubMed:28620689). Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689, PubMed:28902217). The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions (PubMed:28902217). {ECO:0000269|PubMed:28620689, ECO:0000269|PubMed:28902217}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis. {ECO:0000269|PubMed:28902217}.
nucleotide Binding NP_BIND 23..25; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70; NP_BIND 316..317; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q4WZ70
Features Active site (1); Binding site (8); Chain (1); Mutagenesis (1); Nucleotide binding (2)
Keywords Alkaloid metabolism;FMN;Flavoprotein;NADP;Oxidoreductase;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 40,053
Kinetics
Metal Binding
Rhea ID RHEA:35947
Cross Reference Brenda