| IED ID | IndEnz0015000116 |
| Enzyme Type ID | laccase000116 |
| Protein Name |
Conidial pigment polyketide synthase alb1 EC 2.3.1.- Conidial pigment biosynthesis protein alb1 Naphthopyrone synthase |
| Gene Name | alb1 pksP AFUA_2G17600 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MEDLHRLYLFGDQTISCDEGLRNLLQAKNHTIVASFIERCFHALRQEITRLPPSQRTLFPRFTSIADLLAQHRESGTNPALGSALTCIYQLGCFIDYHGDRGHPYPSSDDGLLGSCTGMLSCTAVSSCKNVGELLPLAVEIVRLTIHLGLCVMRVREMVDSTESSSGSWSILVSEINEADATSLIGNFVKKRGIPPSSQPYISAVGSKGLTISAPPEILDNFIEEGLPKEYKHFKAPGVSGPYHAPHLYNDREIRNILSFCSEDVILRHTPRVPLVSSNTGKLVQVKSMRDLLKVALEEILLRKICWDKVTESCLSIVQATNDKPWRILPIASNATQGLVTALQRMGNCQIEVDTGVGAPQMDPAAPNATGNASRSKIAIIGMSGRFPEADGIEAFWDLLYKGLDVHKKVPPERWDVDAHVDLTGTKRNTSKVPYGCWINEPGLFDARFFNMSPREALQADPAQRLALLSAYEALEMAGFVPNSSPSTQRDRVGIFMGMTSDDYREINSGQDIDTYFIPGGNRAFTPGRINYYFKFSGPSVSVDTACSSSLAAIHLACNAIWRNDCDTAISGGVNLLTNPDNHAGLDRGHFLSRTGNCNTFDDGADGYCRADGVGTIVLKRLEDAEADNDPILGVINAAYTNHSAEAVSITRPHVGAQAFIFNKLLNDTNTNPHEIGYVEMHGTGTQAGDAVEMQSVLDVFAPDYRRGPANSLYLGSAKSNIGHGESASGVTSLVKVLLMLKQNMIPPHCGIKTKINHNFPTDLAQRNVHIAFKPTPWNRPVSGKRKMFINNFSAAGGNTALLMEDAPLREITGQDPRNVHVVSVTARSQTALKRNINALIKYINTHAPSSPANERRFLASLAYTTTARRMHHPFRVTAVGSSVKDIREVLRQRADQDVTTPVPATAPKTGFVFTGQGAQYTGMGKQLYEDCATFRSTIHRLDCIAQSQGFPSILPLIDGSMPVEELSPVVTQLGTTCLQMALVDYWKGLGVTPAFVLGHSLGDYAALNSAGVLSTSDTIYLCGRRAQLLTQQCQMGTHAMLAVKAAVSEIQHLLDPDVHAVACINGPTETVISGLSGRIDELAQQCSSQNLKSTKLKVPFAFHSAQVDPILESFEESAQGVIFHEPAVPFVSALNGEVITESNYSVLGPTYMVKHCREAVNFLGALEATRHAKLMDDATLWVEVGSHPICSGMIKSTFGPQATTVPSLRRDDDPWKILSNSLSTLHLAGVELNWKEFHQDFSSAHEVLELPRYGWDLKNYWIPYTNNFCLTKGGPVTAEVSAPKSTFLTTAAQKIVECREDGNTATLVVENNIAEPELNRVIQGHKVNGVALTPSSLYADIAQTLVDHLITKYKPEYQGLGLDVCDMTVPKPLIAKSGDQFFRVSAVMSWAEQKASVQVWSVNGDGKKMAEHAHCTVKLFNCAERETEWKRNSYLIKRSVSLLQDKAQTGEAHRMQRGMVYKLFAALVDYDENFKAIQEVILDSNEHEATARVKFQAPPGNFHRNPFWIDSFGHLSGFIMNASDATDSKNQVFVNHGWDSMRCLKKFSGDATYQTYVKMQPWKDSIWAGDVYVFEGDDIIAVYGGVKFQALARKILDTVLPPIGGSKTVGAPAPAPARPIGEKKAPPPIKVTGPPKPNPSNARAASPVVARALEILAAEVGLSEAEMTDSLNFADYGVDSLLSLTVTGRYREELNLDLESSVFMDYPTIKDFKAYLAEKGFCDSSSPEPSSEPESKFSFNSDASSEASSGLTTPGITSPVKHEAPKGGQNKVWKSICSIIAEEIGVSVGDIDPSDNLPEMGMDSLLSLTVLGRIRETLGMDLPAEFFLENPTLDAVQAALDLKPKMVPAATPVSEPIRLLETIDNTKPKTSRHPPATSILLQGNPHTATKKLFMFPDGSGSASSYATIPALSPDVCVYGLNCPYMKTPQNLTCSLDELTEPYLAEIRRRQPKGPYSFGGWSAGGICAFDAARQLILEEGEEVERLLLLDSPFPIGLEKLPPRLYKFFNSIGLFGDGKRAPPDWLLPHFLAFIDSLDAYKAVPLPFNDSKWAKKMPKTYLIWAKDGVCGKPGDPRPEPAEDGSEDPREMQWLLNDRTDLGPNKWDTLVGPQNIGGIHVMEDANHFTMTTGQKAKELSQFMATAMSS |
| Enzyme Length | 2146 |
| Uniprot Accession Number | Q4WZA8 |
| Absorption | |
| Active Site | ACT_SITE 547; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 547; /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 | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O + YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:133763; Evidence={ECO:0000269|PubMed:11040426};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653; Evidence={ECO:0000269|PubMed:11040426}; |
| 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 and a structural component of the conidial wall (PubMed:9620950, PubMed:10515939, PubMed:18539819, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:9620950, PubMed:11040426). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939, PubMed:11350964). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin plays also a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:9620950, PubMed:9832321, PubMed:12464010,PubMed:16110796, PubMed:20145078, PubMed:21501368, PubMed:21747802, PubMed:21573171, PubMed:24818666, PubMed:24836942, PubMed:25810442, PubMed:26972005). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622). {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:11040426, ECO:0000269|PubMed:11350964, ECO:0000269|PubMed:12464010, ECO:0000269|PubMed:16110796, ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:19703288, ECO:0000269|PubMed:20145078, ECO:0000269|PubMed:21501368, ECO:0000269|PubMed:21573171, ECO:0000269|PubMed:21747802, ECO:0000269|PubMed:24818666, ECO:0000269|PubMed:24836942, ECO:0000269|PubMed:25684622, ECO:0000269|PubMed:25810442, ECO:0000269|PubMed:26972005, ECO:0000269|PubMed:9620950, ECO:0000269|PubMed:9832321}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:10515939}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (2); Domain (2); Modified residue (2); Region (7) |
| Keywords | Endosome;Multifunctional enzyme;Phosphopantetheine;Phosphoprotein;Reference proteome;Repeat;Transferase;Virulence |
| Interact With | |
| Induction | INDUCTION: Expression is up-regulated by laeA during mycelial growth in a liquid medium but laeA is not involved in alb1 regulation during conidial morphogenesis (PubMed:17630330). Expression is, at least in part, controlled by the cAMP/PKA signal transduction pathway (PubMed:16110796). {ECO:0000269|PubMed:16110796, ECO:0000269|PubMed:17630330}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:26972005}. |
| Modified Residue | MOD_RES 1681; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258; MOD_RES 1805; /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 | 234,494 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62652; RHEA:62653 |
| Cross Reference Brenda |