| IED ID | IndEnz0007000140 |
| Enzyme Type ID | catalase000140 |
| Protein Name |
Catalase ifgD EC 1.11.-.- Isofumigaclavine biosynthesis cluster A protein D |
| Gene Name | ifgD PROQFM164_S05g000508 |
| 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 | MAPNYAKKCPVMGKAPSSGHSSIGPQDVHTLEVLSNFNREKIPERVVHALGAGAYGEFEVTHDISDICNIDMLLGVGKKTSLVTRFSTTGLERGSSEGVQDLKGMATKLFTSDGEWDWVFLNFPFFFIRDPVKFPDMIHSQRRDPQTNRLNPNNFWEFVTENHESIHMVLLQYSDFGRMFTWRTLSSYSGHAFKWVMPDGSFKYVHFFLSSDRGPNFKDGAGTIMDSSEPDFASRDLFEAIERGDHPSWTANVQVIDPKDAPHLGFNILDVTKHWNLGTYPQGVEKIPSRPFGKLTLNRNVKDYFSEVEQLAFSPSHLVPGIEASEDPILQARLFAYPDAQRYRLGRTLSKQASPRTSSTAEYQASLGKDFAEWVAQVSSDVWSQPHEDDYKFAREYYEILPEFRSQEFQDRMVERIVESVSQTRQDIRNKVYRTFALVSSELATRVQEGVEGAEIGQEKNVQARL |
| Enzyme Length | 466 |
| Uniprot Accession Number | W6QJS4 |
| Absorption | |
| Active Site | ACT_SITE 48; /evidence=ECO:0000250|UniProtKB:P15202 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.11.-.- |
| Enzyme Function | FUNCTION: Catalase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids (PubMed:28620689). 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:0000305|PubMed:28620689}. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (1); Region (1) |
| Keywords | Alkaloid metabolism;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;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 | 53,038 |
| Kinetics | |
| Metal Binding | METAL 337; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:P15202 |
| Rhea ID | |
| Cross Reference Brenda |