| IED ID | IndEnz0010001283 |
| Enzyme Type ID | esterase001283 |
| Protein Name |
Esterase inpF EC 3.1.2.- Fellutamide B biosynthesis cluster protein F Inp cluster protein F |
| Gene Name | inpF ANIA_03494 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MRILFFHGHTQTGPVFERKTVRLREHIQRAYPGSTFFFPTGPIAYKVSDRLDYLSEIQRERSDNFKDPDLIETHAWFRLFEDDPPRGLLESLDIAAEILRVEGPFDGVICFSQGSVVGSMMASLLEGPRRRQRFDEYAASFPGAVRYPKSYKNINHPPLKFGITYGAYMGTSPVFNAFYSEPLIETPFLHFMGEFDPVVPSEMVAAVDKAQIGGSRRRKVMHPGAHAIPVGDRYHEAVVDFIRSACETSPTYFDLPSDEVPLLSYNDTPEQTPFQTPLLTPSLSSAVSTTSIPSSEATILATRRLDQWEKSRSPRSNIRPRSTRRTVFSGRRSTSSSAESSAASQHSDHFEATRTPTSSTSTVQMIEPTVNKEPNLAVRVVEDDTIVSGSEYEGEGWQELLLSDLLNEMLRRHGRPGRFYFVPDGEGGRLENGMRLN |
| Enzyme Length | 437 |
| Uniprot Accession Number | Q5B7I6 |
| Absorption | |
| Active Site | ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P38777; ACT_SITE 196; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P38777; ACT_SITE 226; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P38777 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.2.- |
| Enzyme Function | FUNCTION: Esterase; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor (PubMed:20952652, PubMed:27294372). In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu (PubMed:27294372). Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides (PubMed:27294372). The MFS efflux transporter inpD may contribute to fellutamide resistance as well (PubMed:27294372). {ECO:0000269|PubMed:27294372, ECO:0000305|PubMed:20952652}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:27294372}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Region (1) |
| Keywords | Hydrolase;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 | 49,125 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |