| IED ID | IndEnz0016000123 |
| Enzyme Type ID | tyrosinase000123 |
| Protein Name |
Aspulvinone E synthetase melA EC 2.3.1.- Nonribosomal peptide synthetase melA |
| Gene Name | melA |
| Organism | Aspergillus terreus |
| 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 |
| Enzyme Sequence | MQPSLIPSLLETAAARNGDGRVILYSQGNREDPRSITYRDLLETASKASVAVHNHQNYTPGAAVLLHFNNHLDNIVWFWAVLLAGCIPAITPAFSNNPVQRVANLEHLSSTLITDWCLTSQALLAEFAGQDAIEPVSVETLGWEKASPASNTASVKAKPTDTALLLFTSGSTGKSKAVCLSHFQIVSAIAGKLSVVPLPEQSSFLNWVGLDHVAAIIEIHLQALYADLDQVHVPGSDVISDPIWFLDLMATHRVSRTFAPNFFLARIRDALVQNARSASPRQWDLSGLRYVASGGEANTTKTCDDLSQLLKSFGAPLNVIVPGFGMTETCAGAIFNTNCPDYDKKHGLEYTSVGSCMPGIFMRVTNQQGDPLPPGEMGSLELAGPVVFRQYLNNPAATQESFTMDGWFKTGDCGTLDENGYLVLGGRAKETIIINGVKYSPHEIETAVEEHNIKGLSRSFTCCFSSLSPGAETEEIVLVYLPTYAPEDIPARAATADAISKVVLMSTGSRPHIIPLEQALLPKSTLGKLSRSKIKAAYERGEYRTHDSINRSLIARHRQATRASPKNDFEKGLLEIFLRSFKISEDEFDVQTPIFDVGIDSIELINLKRDIEQHLGFADATIPIIILLENTTVRELAAALDNLYRPKEYNPVVTLQAHGDKNPLWLVHPGAGEVLIFINLAKFITDRPVYALRARGFDEGEKPFDSIEDAVTSYYNGVKSKQPHGPYALAGYCYGSMLAFEVAKKLEENGDEVRFVGSFNLPPHIKMRMRELDWKECLLHLAYFLDLITQKRSRELAVELDGLDQDTILQAIIDEADKERYAQLSLSRPFLSRWADVAYELHRIAGDYDPDGRVASMDVFFSIPLAIAAASKSEWRNVHLSQWDDFTRSHVRFHDVPGEHYSMIGPEHVFAFQKILRSALAERGM |
| Enzyme Length | 925 |
| Uniprot Accession Number | A0A336U965 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of Asp-melanin, a pigment that confers resistance against UV light and hampers phagocytosis by soil amoeba (PubMed:23841722, PubMed:27133313, PubMed:29270299). The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:27133313, PubMed:29270299). The tyrosinase tyrP then performs hydroxylations of both aromatic moieties of aspulvinone E (PubMed:27133313). The product of tyrP is highly unstable, and, due to the high reactivity of methides and ortho-diquinones, the polymeric Asp-melanin forms spontaneously (PubMed:27133313). {ECO:0000269|PubMed:23841722, ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Modified residue (1); Region (2) |
| Keywords | Cytoplasm;Phosphopantetheine;Phosphoprotein;Transferase |
| Interact With | |
| Induction | INDUCTION: Expression is induced during conidiation. {ECO:0000269|PubMed:27133313}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29270299}. |
| Modified Residue | MOD_RES 601; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 102,287 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |