| IED ID | IndEnz0015000122 |
| Enzyme Type ID | laccase000122 |
| Protein Name |
Conidial pigment polyketide synthase PfmaE EC 2.3.1.- Conidial pigment biosynthesis cluster protein E |
| Gene Name | PfmaE PFICI_07101 |
| 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 | MAEQMSYLLFGDQSLDTHGFLADFYRQGNPSILAKTFLQRAGDSLRDEIDRLPRCQRDRIPQFRTLQQLNERYHQQTIKFPGIDSALLCITQLAHYIDRSEKEHQDVTAAENTYLSGLCTGLFAATAIASSPSLSSLLPIAVQVSLMAYRVGSHVASLAERLSPSDERSESWTYVVPGAKETDAKPILAEFHETEGISPAAQAYVSAVSASNIAISGPPATLKSLFSKDLFESRPTAIPVYGPYHAPHLHAAANLDKILRLDDEAVTAAFDGSKPRSHIVSCVTGQSFPETDTKSLLKAVVHEILNEPLLFHKALKGSLNSAKEFKGSRVLVIPYGPTQAASTLANLLKAQTKLEVVLRTPPQVSRESNGASIGNHGSSGKCKLAIVGMAGRFPDAASHEKLWELLEKGIDAHRVVPADRFPVETHVDPTGKAINTSHTPYGCWIENPGLFDPRFFNMSPREAFQTDPMQRMALTTAYEALEMSGYVPNRTPSTRLDRIGTFYGQTSDDWREINAAQEVDTYYITGGVRAFGPGRINYHFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFAGLSRGQFLSKKGNCNTFDNDADGYCRADACASVIVKRLDDALADKDNILAVVLGTSTNHSADAISITHPHGPTQSVLSRAILDEAGVDPLDVDYVEMHGTGTQAGDGTEMVSVTDVFAPANRHRASDRPLYLGAIKSNVGHGEAASGITALSKVLLMMKKNSIPPHVGIKGEINKTFPKDLGARGVNIAFHKTPFQRKDGKPRRIFVNNFSAAGGNTGLLLEDGPRYKTAEADPRSVHVVTVTAKSKSAMIRNAEGLVQWMEQNPSTPVSDVAYTTTARKIQHYWRMNVAAGSLPEAIQAIKERLKSTFVPVSPEQPKVAFMFTGQGSHYAGLGKELYAHYAIFRDAIDEYDQLAGIHGFPSFLPLIDGSEPDVQNLSPVVVQLGLCSFEMALARLWQSWGIQPGAVLGHSLGEYAALHVAGVLSASDTIYLVGARAQLLVNKCTAGTHAMLAVQGSVETVKEALGARAESTNVACINGPRETVLSGASSEVAEIAEQLGGAGFKCTQLKVPFAFHSAQVEPILDDFESLARSVRFETPKVPVISPLLGKLVDNEPINPAYLRNHAREAVNFLGGLVSAQQSGMIDEKTVWLEVGPHPVCANMVKAAFGATTIAVPTLRRNEATYKTLSSSLCTLHSAGLNLDWNEFHRDFDASVRLLDLPSYAFDYKNYWLQYTGDWSLTKNRGALPASTKAIEAPKPKLSTTTVQKVVREEVKGDIAILETESEMTRDDLRLVCSGHMVNGTALTPSSLYGDMAITACEYAYKLLRPDAKNIGCNVSHMEVPKTLIFNGKAKSQVLRMSVKANAAEGFADLSWTSGEGAQKTEHANCKVFFGDNEEWLGEFERVNYLIKSRIDALRAAEQRGDASKIGRGLAYKLFAALVDYDRRYRGMESVILDSETCEATAKVVFQTSPEDGTFHTAPYWIDSVCHISGFILNGSDAIDSREQVFISHGWGSMRFAERLSAEKTYQTYIRMQNVKGSKMMSGDAYIFDGDKLIGIAGDVRFQAIPRKVLNVVLPPQGAAAAGSAPARAPAAAAKPAAKAAPKEKKQVTSANLPAVNKSLTKNSVVAQVMEIIAKETGVSHDELADNIAFSDLGVDSLMGLTISGRLREELELNVDSHAFNDHATVGAFKAFLAQFESADAAMVEENAHSSASSDSADMETESNFTTPSDDSEKDEVKGDAPAADGNVSELQDIVRSTISAEMGVEVEEVIAAPDLAALGMDSLMSLSILGILREKTGLNIPSDLLGHNPSLKDIEKALGIEDKPKRAAPKSAKQEPAKPEPKVQGEAKAHTNPVDNYPHRKATSVLLQGNHRTAKKQLFMIPDGSGSATSYTEISEVGSDVAVWGLFSPFMKTPDEYNCGVYGMATKFIQEMKRRQPEGPYAVAGWSAGGVIAYEIVNQLTKANEEVSNLLIIDAPCPITIEPLPAGLHAWFASIGLLGEGDDAEAKKIPEWLLPHFAASVTALSNYDAEPIPADKCPKVTVIWCEDGVCKLPTDPRPDPYPTGHALFLLDNRSDFGPNRWDEYLDSKKMTFHHMPGNHFSMMHGPLAKQLGGFMRDGMKS |
| Enzyme Length | 2155 |
| Uniprot Accession Number | W3X7U2 |
| Absorption | |
| Active Site | ACT_SITE 553; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 553; /note=For beta-ketoacyl synthase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 1001; /note=For acyl/malonyl transferase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: Non-reducing polyketide synthase; 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 | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:28517364}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (3); Domain (2); Modified residue (2); Region (7) |
| Keywords | Melanin biosynthesis;Multifunctional enzyme;Phosphopantetheine;Phosphoprotein;Reference proteome;Repeat;Transferase |
| Interact With | |
| Induction | INDUCTION: Expression is positively regulazed by the cluster-specific transcription factor pfmaF. {ECO:0000269|PubMed:28517364, ECO:0000269|PubMed:31116900}. |
| Subcellular Location | |
| Modified Residue | MOD_RES 1690; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258; MOD_RES 1816; /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 | 233,253 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |