| IED ID | IndEnz0010000411 |
| Enzyme Type ID | esterase000411 |
| Protein Name |
NADH-cytochrome b5 reductase-like protein alnC EC 1.6.2.- Asperlin biosynthesis cluster protein C |
| Gene Name | alnC ANIA_11198 |
| 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 | MASPASITLAEVARHSSPNDLWIVIEGNVYDVAEYREDHPGGDEILRQFAGKDATTEFQDAGHSNDAYVKLKTLLVGSLQSKTLPENQPEESSRIVSIAVSDRGKIPTKRQARNGNDTSKYGQLPSLVLAGGLALLFFTLKQHPWQSIQGYLSQAQVSRVQSSGWVGFLGGFLTATTLNTAAATFVGLTAKKTLLLRHRELEEYPRVKQHYLPLPPKKPGISGENTQQFLTLVDRQCIAPNVYKVRLQGDGLVIGLGQHLKVLAEIDGRKIQRSYTPVSPVGNSPKVDLIIKVYPKGQLGNYLLNLPLQSRVEIRGPFGRYSPSPTWKHIACIAGGTGIAPIYQVMRAWPGEITLLYGNETWEDILLREELEQLVLQSPRRIKVHHVLGQPKSDWKGLRGWITREMIQDLLPEPSSSTGFLVCGPDGMVRAIRGHFEAIDANGEEKANVFVF |
| Enzyme Length | 452 |
| Uniprot Accession Number | C8VJR5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.6.2.- |
| Enzyme Function | FUNCTION: NADH-cytochrome b5 reductase-like protein; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities (PubMed:30339758). The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with cleavage of the PKS product by the esterase alnB (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to asperlin via several steps involving the remaining enzymes from the cluster (PubMed:30339758). {ECO:0000269|PubMed:30339758}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}. |
| nucleotide Binding | NP_BIND 33..38; /note=FMN; /evidence=ECO:0000250|UniProtKB:P38038; NP_BIND 80..83; /note=FMN; /evidence=ECO:0000250|UniProtKB:P38038; NP_BIND 116..125; /note=FMN; /evidence=ECO:0000250|UniProtKB:P38038; NP_BIND 302..305; /note=FAD; /evidence=ECO:0000250|UniProtKB:P38038; NP_BIND 389..390; /note=NADP; /evidence=ECO:0000250|UniProtKB:P38038; NP_BIND 395..399; /note=NADP; /evidence=ECO:0000250|UniProtKB:P38038 |
| Features | Chain (1); Domain (2); Metal binding (2); Nucleotide binding (6); Transmembrane (2) |
| Keywords | FAD;FMN;Flavoprotein;Heme;Iron;Membrane;Metal-binding;NADP;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Expression is controlled by the asperlin biosynthesis cluster-specific transcription factor alnR. {ECO:0000269|PubMed:30339758}. |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,968 |
| Kinetics | |
| Metal Binding | METAL 39; /note=Iron (heme axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00279; METAL 63; /note=Iron (heme axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00279 |
| Rhea ID | |
| Cross Reference Brenda |