| IED ID | IndEnz0010000374 |
| Enzyme Type ID | esterase000374 |
| Protein Name |
Probable esterase afoC EC 3.1.2.- Asperfuranone biosynthesis protein B |
| Gene Name | afoC AN1032 |
| 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 | MPALDIASAPAAVYQQQLHLPRILCLHGGGTNARIFTAQCRALRRQLTDSYRLVFADAPFLSSAGPDVTSVYGEWGPFRSWVPVPAGVDISAWAAAGAASRIDIDVEAIDECIAAAIAQDDRAGATGDWVGLLGFSQGARVAASLLYRQQKQQRMGLTSWSRGRDRKRGATSSTNYRFAVLFAGRGPLLDLGFGSGSLAGSSAASSSASASVSGSESAGEEEEDGHLLSIPTIHVHGLRDPGLEMHRDLVRSCRPSSVRIVEWEGAHRMPITTKDVGAVVAELRHLAISRKYESLRC |
| Enzyme Length | 297 |
| Uniprot Accession Number | Q5BEJ8 |
| Absorption | |
| Active Site | ACT_SITE 136; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P38777; ACT_SITE 240; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P38777; ACT_SITE 267; /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: Probable esterase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437). The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM) (PubMed:19199437). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation (PubMed:19199437). AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 (PubMed:19199437). After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination (PubMed:19199437). AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone (PubMed:19199437). Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood (PubMed:19199437). Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency (PubMed:19199437). {ECO:0000269|PubMed:19199437}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Region (1) |
| Keywords | Hydrolase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Expression is regulated by the asperfuranone cluster transcription factor afoA (PubMed:19199437). {ECO:0000269|PubMed:19199437}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,685 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |