| IED ID | IndEnz0016000162 |
| Enzyme Type ID | tyrosinase000162 |
| Protein Name |
FAD-dependent monooxygenase terD EC 1.-.-.- Terrein biosynthesis cluster protein terD |
| Gene Name | terD ATEG_00142 |
| Organism | Aspergillus terreus (strain NIH 2624 / FGSC A1156) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus terreus Aspergillus terreus (strain NIH 2624 / FGSC A1156) |
| Enzyme Sequence | MSSKFDVVICGSGTAGLAAATWLAQYGVDCKILESRSGPLDVGQADGIQVRSVEIFESFGMAEELLREAYHNIEVAFWGSNPTSSGMGIVRKRSAHATTPGLSHMPRVILNQARFNEMWLEAMRRRNGQEVDYGHKVTKVTVDEEKATDPDAYPVTIVAQKDGQEQVFEAKYCLASDGAHSAVRKSLGFNMVGETSDSVWGVMDVFPRTNFPDIRKQCIIQSDAGSIITIPREGGSMVRVYVELAAGTNAKEVTLEQIQNASRQVFHPYALDVADVWWWSAYPIGQRIADHFSKANRVFLTGDACHTHSPKAGQGMNVSLQDGYNIGWKLASVLKGHAGPELLETYVLERQKVADVLINWDKVWAKQMCSIAKEDGGVVDANGKIDFSEVFVKAEAFTAGLTVTYGDSIITQAGDSNQQAATNLKVGMRLPAAQVVRFCDAKVMKTVNALPSDGRWRIMIFPGDIRQPSASTRLAQLGTYLFSNHGPIRKYLPPGADIDSLIEVIVILSGERLEIQQDQIPDAFWPTTGKYRMRDLHKIYIDDETYHNGHGHAYDFYGIDPERGAVAIVRPDQYISKVLDMKNHEGISAFFEKFLQKKGQANGSLNSHDEWTLA |
| Enzyme Length | 614 |
| Uniprot Accession Number | Q0D1P2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 44; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6SSJ6; BINDING 137; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q6SSJ6; BINDING 282; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6SSJ6; BINDING 303; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6SSJ6; BINDING 319; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6SSJ6 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of terrein, a fungal metabolite with ecological, antimicrobial, antiproliferative, and antioxidative activities (PubMed:24816227). The first step in the pathway is performed by the polyketide synthase terA that produces 4-hydroxy-6-methylpyranon (4-HMP), orsellinic acid (OA), and 2,3-dehydro-6-hydroxymellein (2,3-dehydro-6-HM) by condensing acetyl-CoA with two, three, or four malonyl-CoA units, respectively (PubMed:24816227). 4-HMP and OA are not pathway intermediates, but are rather shunt or side products (PubMed:24816227). 2,3-dehydro-6-HM is further converted to 6-hydroxymellein (6-HM) by the 6-hydroxymellein synthase terB (PubMed:24816227). The monooxygenases terC and terD, the multicopper oxidase terE and the Kelch-like protein terF are then involved in the transformation of 6-HM to terrein (PubMed:24816227). Even if they are co-regulated with the other terrein cluster genes, terH and terI seem to be dispensable for terrein production; whereas one or both of the 2 transporters terG and terJ are probably required for efficient secretion of metabolites (PubMed:24816227). {ECO:0000269|PubMed:24816227}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:24816227}. |
| nucleotide Binding | NP_BIND 6..35; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6SSJ6; NP_BIND 239..241; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6SSJ6 |
| Features | Binding site (5); Chain (1); Glycosylation (3); Nucleotide binding (2); Signal peptide (1) |
| Keywords | FAD;Flavoprotein;Glycoprotein;Monooxygenase;Oxidoreductase;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is under the control of the terrein cluster-specific transcription factor terR (PubMed:25852654). {ECO:0000269|PubMed:25852654}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 67,859 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |