Detail Information for IndEnz0015000140
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