| IED ID | IndEnz0010000444 |
| Enzyme Type ID | esterase000444 |
| Protein Name |
NADP-dependent oxidoreductase RED1 EC 1.-.-.- T-toxin biosynthesis protein RED1 |
| Gene Name | RED1 COCC4DRAFT_45938 |
| Organism | Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern corn leaf blight fungus) (Bipolaris maydis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Pleosporaceae Bipolaris Cochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris maydis) Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern corn leaf blight fungus) (Bipolaris maydis) |
| Enzyme Sequence | MYQNKSLIFKNPPIGWPKPDVDFGVECRPIDINGDIPLGGVILKNCYVSLDPYQRGRMRAPTVDSYSPPFTIGDPMEGHVISRVIRSASTKLQPGDFVSGVGPIQEFSVLSAGVVDGFTRIENPYNLNLEIFLGPLGMPGLTAYSSFYEIGKPKKGETIFISAASGAVGQLVGQLAKREGLYVIGSVGDDEKVEFITKGLGFDVGFNYKKEVIGEALMRVAPEGIDIYFDNVGGQTLESALYAMRPRGRIVVSGMISQYNLQPSELYGVKNLFMVITNRITIQGFIVTDSDMGPKYSAEHLKNVSQWIYDGSLKPKIHVDTGMDHACQSFINMLKGRKIGKAVLQIADLNGD |
| Enzyme Length | 352 |
| Uniprot Accession Number | N4WR35 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 192; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9EQZ5; BINDING 208; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9EQZ5; BINDING 231; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9EQZ5 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: NADP-dependent oxidoreductase; part of the Tox1B locus, one of the 2 loci that mediate the biosynthesis of T-toxin, a family of linear polyketides 37 to 45 carbons in length, of which the major component is 41 carbons, and which leads to high virulence to maize (PubMed:8953776, PubMed:20192833). One of the PKSs (PKS1 or PKS2) could synthesize a precursor, used subsequently by the other PKS as starter unit, to add additional carbons (PubMed:16529376). Variability in the length of the final carbon backbone C35-47 could be achieved by varying the number of condensation cycles, or use of different starter or extender units or might be due to decarboxylation of the penultimate product, catalyzed by DEC1 (PubMed:12236595). Additional proteins are required for the biosynthesis of T-toxin, including oxidoreductases RED1, RED2, RED3, LAM1 and OXI1, as well as esterase TOX9 (PubMed:20192833). {ECO:0000269|PubMed:12236595, ECO:0000269|PubMed:16529376, ECO:0000269|PubMed:20192833, ECO:0000269|PubMed:8953776}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20192833}. |
| nucleotide Binding | NP_BIND 166..169; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9EQZ5; NP_BIND 285..287; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9EQZ5 |
| Features | Binding site (3); Chain (1); Nucleotide binding (2); Sequence conflict (1) |
| Keywords | NADP;Oxidoreductase |
| 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 | 38,473 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |