IED ID | IndEnz0015000140 |
Enzyme Type ID | laccase000140 |
Protein Name |
5-oxoprolinase PfmaA EC 3.5.2.9 Conidial pigment biosynthesis cluster protein A |
Gene Name | PfmaA PFICI_07097 |
Organism | Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Xylariomycetidae Xylariales Sporocadaceae Pestalotiopsis Pestalotiopsis fici Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) |
Enzyme Sequence | MTADIRVSIDRGGTFCDVIAHVEGREPIIFKLLSVDPANYQDAPTEGIRRVLEIVEGKKIPVGEKLDGTRIASCRLGTTVATNALLEGKYEKFALVTTKGFEDVCVIGDQSRPKLFDLKVKKAEALHDTVIGVDERVTIEDYDLNPYPLDKSASLNDPDLVRTPSGEIIRILARVNEETVREQLLALRDAGYNSVAISFMHSYIFPDHEDQVAKIAREVGFTYVTTSAETRPVLKYLNRSTSCCSEACLYPVIRRYIENFESGFRVLPRRVDFMCSDGGLKQSQKFRGNEALLSGPAGGVVGIATSCYDVEQKIPIIGFDMGGTSTDVSRFDGKYDYLSETVIADRTISMPMLNISTVAAGGGSILFARSGLLVVGPESAGAHPGPACYRKGGPLTVTDANLFLGRLVVSSFPSIFGENADQPLDQDVVTAKFQEITADFNSQTSQNLTAEEVALGFLDVANEAMSRPIRNTTEARGFAPEKHNLVSFGGAGGQHACAIASKLGIKRVLIHKWSSLLSAHGISQADLQYESFEPLSLDFGMDLNGFIKERLSLLREKVAAGLLAQGAQESTLRFDESLVMKYFGTDTTITVTTPDDLDYGAAFEALHLREFAFKLNRKIVIDSVNVRGTGSAVTLATEEPPLKALARVKSVATTAQTTEEQKVYINGSWRKVPIYRLDQLSKGCAVSGPAMIIDKTQTIFVEPRFNAYILPDHVILEESNVEDTVTRQAVSAEEINPLLLSVFAHRFMSIAEQMGNTLQRTSVSSSIKERLDFSCAIFSREGKLVANAPHIPIHLGSMQMAIRYQHEAWKGKLKPGDALVTNHPLSGGTHLPDLTVVSPVFVNGDVAFYVASRGHHTDIGGKGIAAMMPESKELWEEGISIKTMKIVSGGEFLEDEIRAAFDKAGSFPGCSPTRRIADNLSDLKAQIASNQRGIILLGNLCEEFTLPVVCTYMEGIQANAEFAVRRFLKQLAKKHPEPLTAIDYFDDGTPIKIKIIIDPETGGAVYDFSGTGPQQWGNYNCPISITHSAIIYTLRCLVDVDIPLNEGCLTPIDIRVPYGSMLNPSPAVAICGSTLASQRVIDTILRAFRRCAASQGCASSFSWGMGGRDPETGKVLPGWNYGESLGGGVGALPGYHGESAINVHSTNTRNTDPEVVEKRTAVLVTKYAVRKGSGGRGQWRGGDGVTREIQARIPLKFSILSDRRVYRPYGMEGGEAGHRGQNYVFKFNQEGTGFEQINLGGKAVVVLNPGEKMQINTPGGGAWGKPEGDADGYREEDQAGDGI |
Enzyme Length | 1283 |
Uniprot Accession Number | W3X7R6 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9; Evidence={ECO:0000305|PubMed:28517364}; |
DNA Binding | |
EC Number | 3.5.2.9 |
Enzyme Function | FUNCTION: 5-oxoprolinase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment forming a dark layer in the conidial wall that protects the conidia from UV radiations (PubMed:28517364). The first step of the pathway is the production of the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN is not stable and easily oxidizes into the stable form flaviolin (PubMed:28517364). T4HN is also substrate of the hydroxynaphthalene reductase PfmaG to yield scytalone (PubMed:28517364). The scytalone dehydratase PfmaJ then reduces scytalone to 1,3,8-THN (PubMed:31116900). 1,3,8-THN is then substrate of the hydroxynaphthalene reductase PfmaI to yield vermelone (Probable). Vermelone is further converted by the multicopper oxidase PfmaD to 1,8-DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the proline iminopeptidase PfmaB within the cluster have not been elucidated yet (Probable). {ECO:0000269|PubMed:28517364, ECO:0000269|PubMed:31116900, ECO:0000305|PubMed:28517364, ECO:0000305|PubMed:31116900}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (1); Region (1) |
Keywords | ATP-binding;Hydrolase;Melanin biosynthesis;Nucleotide-binding;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 | 139,396 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:10348 |
Cross Reference Brenda |