ALB1_ASPFU
ID ALB1_ASPFU Reviewed; 2146 AA.
AC Q4WZA8;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Conidial pigment polyketide synthase alb1 {ECO:0000303|PubMed:9620950};
DE EC=2.3.1.- {ECO:0000269|PubMed:11040426};
DE AltName: Full=Conidial pigment biosynthesis protein alb1 {ECO:0000305};
DE AltName: Full=Naphthopyrone synthase {ECO:0000303|PubMed:11040426};
GN Name=alb1 {ECO:0000303|PubMed:9620950};
GN Synonyms=pksP {ECO:0000303|PubMed:9832321}; ORFNames=AFUA_2G17600;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9620950; DOI=10.1128/jb.180.12.3031-3038.1998;
RA Tsai H.F., Chang Y.C., Washburn R.G., Wheeler M.H., Kwon-Chung K.J.;
RT "The developmentally regulated alb1 gene of Aspergillus fumigatus: its role
RT in modulation of conidial morphology and virulence.";
RL J. Bacteriol. 180:3031-3038(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9832321; DOI=10.1007/s004300050077;
RA Langfelder K., Jahn B., Gehringer H., Schmidt A., Wanner G., Brakhage A.A.;
RT "Identification of a polyketide synthase gene (pksP) of Aspergillus
RT fumigatus involved in conidial pigment biosynthesis and virulence.";
RL Med. Microbiol. Immunol. 187:79-89(1998).
RN [4]
RP FUNCTION.
RX PubMed=10515939; DOI=10.1128/jb.181.20.6469-6477.1999;
RA Tsai H.F., Wheeler M.H., Chang Y.C., Kwon-Chung K.J.;
RT "A developmentally regulated gene cluster involved in conidial pigment
RT biosynthesis in Aspergillus fumigatus.";
RL J. Bacteriol. 181:6469-6477(1999).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11040426; DOI=10.1111/j.1574-6968.2000.tb09356.x;
RA Watanabe A., Fujii I., Tsai H., Chang Y.C., Kwon-Chung K.J., Ebizuka Y.;
RT "Aspergillus fumigatus alb1 encodes naphthopyrone synthase when expressed
RT in Aspergillus oryzae.";
RL FEMS Microbiol. Lett. 192:39-44(2000).
RN [6]
RP FUNCTION.
RX PubMed=11350964; DOI=10.1074/jbc.m101998200;
RA Tsai H.F., Fujii I., Watanabe A., Wheeler M.H., Chang Y.C., Yasuoka Y.,
RA Ebizuka Y., Kwon-Chung K.J.;
RT "Pentaketide melanin biosynthesis in Aspergillus fumigatus requires chain-
RT length shortening of a heptaketide precursor.";
RL J. Biol. Chem. 276:29292-29298(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12464010; DOI=10.1046/j.1462-5822.2002.00228.x;
RA Jahn B., Langfelder K., Schneider U., Schindel C., Brakhage A.A.;
RT "PKSP-dependent reduction of phagolysosome fusion and intracellular kill of
RT Aspergillus fumigatus conidia by human monocyte-derived macrophages.";
RL Cell. Microbiol. 4:793-803(2002).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=15321679; DOI=10.1111/j.1574-6968.2004.tb09713.x;
RA Mouyna I., Henry C., Doering T.L., Latge J.P.;
RT "Gene silencing with RNA interference in the human pathogenic fungus
RT Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 237:317-324(2004).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=15812003; DOI=10.1128/aem.71.4.1798-1802.2005;
RA Sugui J.A., Chang Y.C., Kwon-Chung K.J.;
RT "Agrobacterium tumefaciens-mediated transformation of Aspergillus
RT fumigatus: an efficient tool for insertional mutagenesis and targeted gene
RT disruption.";
RL Appl. Environ. Microbiol. 71:1798-1802(2005).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=16110796; DOI=10.1080/13693780400028967;
RA Brakhage A.A., Liebmann B.;
RT "Aspergillus fumigatus conidial pigment and cAMP signal transduction:
RT significance for virulence.";
RL Med. Mycol. 43:S75-S82(2005).
RN [11]
RP INDUCTION.
RX PubMed=17630330; DOI=10.1128/ec.00140-07;
RA Sugui J.A., Pardo J., Chang Y.C., Muellbacher A., Zarember K.A.,
RA Galvez E.M., Brinster L., Zerfas P., Gallin J.I., Simon M.M.,
RA Kwon-Chung K.J.;
RT "Role of laeA in the regulation of alb1, gliP, conidial morphology, and
RT virulence in Aspergillus fumigatus.";
RL Eukaryot. Cell 6:1552-1561(2007).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=17343676; DOI=10.1111/j.1574-6968.2007.00680.x;
RA Khalaj V., Eslami H., Azizi M., Rovira-Graells N., Bromley M.;
RT "Efficient downregulation of alb1 gene using an AMA1-based episomal
RT expression of RNAi construct in Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 270:250-254(2007).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=18539819; DOI=10.1128/aem.00470-08;
RA Grosse C., Heinekamp T., Kniemeyer O., Gehrke A., Brakhage A.A.;
RT "Protein kinase A regulates growth, sporulation, and pigment formation in
RT Aspergillus fumigatus.";
RL Appl. Environ. Microbiol. 74:4923-4933(2008).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19703288; DOI=10.1186/1471-2180-9-177;
RA Pihet M., Vandeputte P., Tronchin G., Renier G., Saulnier P.,
RA Georgeault S., Mallet R., Chabasse D., Symoens F., Bouchara J.P.;
RT "Melanin is an essential component for the integrity of the cell wall of
RT Aspergillus fumigatus conidia.";
RL BMC Microbiol. 9:177-177(2009).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19156203; DOI=10.1371/journal.pone.0004224;
RA Jackson J.C., Higgins L.A., Lin X.;
RT "Conidiation color mutants of Aspergillus fumigatus are highly pathogenic
RT to the heterologous insect host Galleria mellonella.";
RL PLoS ONE 4:E4224-E4224(2009).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20145078; DOI=10.1128/aac.01504-09;
RA Ben-Ami R., Lewis R.E., Leventakos K., Latge J.P., Kontoyiannis D.P.;
RT "Cutaneous model of invasive aspergillosis.";
RL Antimicrob. Agents Chemother. 54:1848-1854(2010).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21501368; DOI=10.1111/j.1462-5822.2011.01605.x;
RA Volling K., Thywissen A., Brakhage A.A., Saluz H.P.;
RT "Phagocytosis of melanized Aspergillus conidia by macrophages exerts
RT cytoprotective effects by sustained PI3K/Akt signalling.";
RL Cell. Microbiol. 13:1130-1148(2011).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21747802; DOI=10.3389/fmicb.2011.00096;
RA Thywissen A., Heinekamp T., Dahse H.M., Schmaler-Ripcke J., Nietzsche S.,
RA Zipfel P.F., Brakhage A.A.;
RT "Conidial dihydroxynaphthalene melanin of the human pathogenic fungus
RT Aspergillus fumigatus interferes with the host endocytosis pathway.";
RL Front. Microbiol. 2:96-96(2011).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21573171; DOI=10.1371/journal.pone.0019591;
RA Mech F., Thywissen A., Guthke R., Brakhage A.A., Figge M.T.;
RT "Automated image analysis of the host-pathogen interaction between
RT phagocytes and Aspergillus fumigatus.";
RL PLoS ONE 6:E19591-E19591(2011).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24818666; DOI=10.1128/iai.01726-14;
RA Bayry J., Beaussart A., Dufrene Y.F., Sharma M., Bansal K., Kniemeyer O.,
RA Aimanianda V., Brakhage A.A., Kaveri S.V., Kwon-Chung K.J., Latge J.P.,
RA Beauvais A.;
RT "Surface structure characterization of Aspergillus fumigatus conidia
RT mutated in the melanin synthesis pathway and their human cellular immune
RT response.";
RL Infect. Immun. 82:3141-3153(2014).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24836942; DOI=10.1016/j.ijmm.2014.04.009;
RA Amin S., Thywissen A., Heinekamp T., Saluz H.P., Brakhage A.A.;
RT "Melanin dependent survival of Apergillus fumigatus conidia in lung
RT epithelial cells.";
RL Int. J. Med. Microbiol. 304:626-636(2014).
RN [22]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25684622; DOI=10.1111/1462-2920.12808;
RA Hillmann F., Novohradska S., Mattern D.J., Forberger T., Heinekamp T.,
RA Westermann M., Winckler T., Brakhage A.A.;
RT "Virulence determinants of the human pathogenic fungus Aspergillus
RT fumigatus protect against soil amoeba predation.";
RL Environ. Microbiol. 17:2858-2869(2015).
RN [23]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25810442; DOI=10.1093/infdis/jiv191;
RA Rambach G., Blum G., Latge J.P., Fontaine T., Heinekamp T., Hagleitner M.,
RA Jeckstroem H., Weigel G., Wuertinger P., Pfaller K., Krappmann S.,
RA Loeffler J., Lass-Floerl C., Speth C.;
RT "Identification of Aspergillus fumigatus surface components that mediate
RT interaction of conidia and hyphae with human platelets.";
RL J. Infect. Dis. 212:1140-1149(2015).
RN [24]
RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26972005; DOI=10.1016/j.celrep.2016.02.059;
RA Upadhyay S., Xu X., Lowry D., Jackson J.C., Roberson R.W., Lin X.;
RT "Subcellular compartmentalization and trafficking of the biosynthetic
RT machinery for fungal melanin.";
RL Cell Rep. 14:2511-2518(2016).
RN [25]
RP DISRUPTION PHENOTYPE.
RX PubMed=26701308; DOI=10.1016/j.fgb.2015.12.007;
RA Zhang C., Meng X., Wei X., Lu L.;
RT "Highly efficient CRISPR mutagenesis by microhomology-mediated end joining
RT in Aspergillus fumigatus.";
RL Fungal Genet. Biol. 86:47-57(2016).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a
CC bluish-green pigment and a structural component of the conidial wall
CC (PubMed:9620950, PubMed:10515939, PubMed:18539819, PubMed:19156203).
CC The first step of the pathway is the production of the heptaketide
CC naphtopyrone YWA1 by the polyketide synthase alb1 though condensation
CC of acetyl-CoA with malonyl-CoA (PubMed:9620950, PubMed:11040426). The
CC naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-
CC tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase
CC ayg1 though chain-length shortening (PubMed:10515939, PubMed:11350964).
CC 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to
CC yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then
CC reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also
CC substrate of the hydroxynaphthalene reductase arp2 to yield vermelone
CC (PubMed:10515939). Vermelone is further converted by the multicopper
CC oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2
CC transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin
CC biosynthesis appears to be initiated in endosomes where early enzymes
CC (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to
CC melanin deposition on the cell surface where late enzymes (abr1 and
CC abr2) localize (PubMed:26972005). DHN-melanin is an important
CC structural component of the outer cell wall and is required for the
CC presence of conidial surface hydrophobins (PubMed:19703288). DHN-
CC melanin also plays a crucial role in fungal virulence, including a
CC protective role against the host's immune defenses (PubMed:9620950,
CC PubMed:9832321, PubMed:12464010,PubMed:16110796, PubMed:20145078,
CC PubMed:21501368, PubMed:21747802, PubMed:21573171, PubMed:24818666,
CC PubMed:24836942, PubMed:25810442, PubMed:26972005). DHN-melanin
CC protects also conidia against amoeba predation (PubMed:25684622).
CC {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:11040426,
CC ECO:0000269|PubMed:11350964, ECO:0000269|PubMed:12464010,
CC ECO:0000269|PubMed:16110796, ECO:0000269|PubMed:19156203,
CC ECO:0000269|PubMed:19703288, ECO:0000269|PubMed:20145078,
CC ECO:0000269|PubMed:21501368, ECO:0000269|PubMed:21573171,
CC ECO:0000269|PubMed:21747802, ECO:0000269|PubMed:24818666,
CC ECO:0000269|PubMed:24836942, ECO:0000269|PubMed:25684622,
CC ECO:0000269|PubMed:25810442, ECO:0000269|PubMed:26972005,
CC ECO:0000269|PubMed:9620950, ECO:0000269|PubMed:9832321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O +
CC YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:133763;
CC Evidence={ECO:0000269|PubMed:11040426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC Evidence={ECO:0000269|PubMed:11040426};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000269|PubMed:10515939}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:26972005}.
CC -!- INDUCTION: Expression is up-regulated by laeA during mycelial growth in
CC a liquid medium but laeA is not involved in alb1 regulation during
CC conidial morphogenesis (PubMed:17630330). Expression is, at least in
CC part, controlled by the cAMP/PKA signal transduction pathway
CC (PubMed:16110796). {ECO:0000269|PubMed:16110796,
CC ECO:0000269|PubMed:17630330}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DOMAIN: The C-terminal region is involved in Claisen-type cyclization
CC of the second ring of naphthopyrone. {ECO:0000250|UniProtKB:Q03149}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of melanin and leads to an
CC albino phenotype (PubMed:9620950, PubMed:15321679, PubMed:15812003,
CC PubMed:17343676, PubMed:19156203, PubMed:26701308). Blocks the
CC synthesis of the intermediate 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-
CC THN) (PubMed:9620950). Results in an altered conidial surface with
CC masked surface rodlet layer, leaky cell wall allowing the deposition of
CC proteins on the cell surface and exposing the otherwise-masked cell
CC wall polysaccharides at the surface (PubMed:19703288, PubMed:24818666,
CC PubMed:26972005). Results also in a dramatic reduction of virulence in
CC a mice models of infections (pulmonary and cutanous) with efficient
CC complement component C3 binding on conidial surfaces and increased
CC neutrophil-mediated phagocytosis (PubMed:9620950, PubMed:9832321,
CC PubMed:12464010, PubMed:20145078, PubMed:21501368, PubMed:21747802,
CC PubMed:21573171, PubMed:24836942). Decreases also the protection of
CC conidia against amoeba predation (PubMed:25684622). Decreases
CC significantly the ability of conidia to activate platelets and to
CC induce platelet aggregation (PubMed:25810442). Causes enhanced insect
CC mortality compared to the parent strain in a wax moth Galleria
CC mellonella infection model, probably through exacerbated immune
CC response of the wax moth (PubMed:19156203).
CC {ECO:0000269|PubMed:12464010, ECO:0000269|PubMed:15321679,
CC ECO:0000269|PubMed:15812003, ECO:0000269|PubMed:17343676,
CC ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:20145078,
CC ECO:0000269|PubMed:21501368, ECO:0000269|PubMed:21573171,
CC ECO:0000269|PubMed:21747802, ECO:0000269|PubMed:24818666,
CC ECO:0000269|PubMed:24836942, ECO:0000269|PubMed:25684622,
CC ECO:0000269|PubMed:25810442, ECO:0000269|PubMed:26701308,
CC ECO:0000269|PubMed:26972005, ECO:0000269|PubMed:9620950,
CC ECO:0000269|PubMed:9832321}.
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DR EMBL; AAHF01000001; EAL94057.1; -; Genomic_DNA.
DR RefSeq; XP_756095.1; XM_751002.1.
DR AlphaFoldDB; Q4WZA8; -.
DR SMR; Q4WZA8; -.
DR STRING; 746128.CADAFUBP00003263; -.
DR ESTHER; aspfu-PKSP; Thioesterase.
DR EnsemblFungi; EAL94057; EAL94057; AFUA_2G17600.
DR GeneID; 3513291; -.
DR KEGG; afm:AFUA_2G17600; -.
DR VEuPathDB; FungiDB:Afu2g17600; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR InParanoid; Q4WZA8; -.
DR OMA; VCVYGLN; -.
DR OrthoDB; 68112at2759; -.
DR UniPathway; UPA00785; -.
DR PHI-base; PHI:6891; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:InterPro.
DR GO; GO:0001848; F:complement binding; IDA:AspGD.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0042243; P:asexual spore wall assembly; IMP:AspGD.
DR GO; GO:0052034; P:effector-mediated suppression of host pattern-triggered immunity; TAS:PHI-base.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:AspGD.
DR GO; GO:0046148; P:pigment biosynthetic process; IMP:AspGD.
DR GO; GO:0075136; P:response to host; IEP:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Endosome; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Virulence.
FT CHAIN 1..2146
FT /note="Conidial pigment polyketide synthase alb1"
FT /id="PRO_0000436877"
FT DOMAIN 1647..1721
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1768..1845
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 8..244
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 375..748
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 911..1232
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1290..1602
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1611..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1724..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1892..2019
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT COMPBIAS 1620..1636
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 547
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1001
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1962
FT /note="For Claisen cyclase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1681
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1805
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2146 AA; 234494 MW; 19881353CAF0F022 CRC64;
MEDLHRLYLF GDQTISCDEG LRNLLQAKNH TIVASFIERC FHALRQEITR LPPSQRTLFP
RFTSIADLLA QHRESGTNPA LGSALTCIYQ LGCFIDYHGD RGHPYPSSDD GLLGSCTGML
SCTAVSSCKN VGELLPLAVE IVRLTIHLGL CVMRVREMVD STESSSGSWS ILVSEINEAD
ATSLIGNFVK KRGIPPSSQP YISAVGSKGL TISAPPEILD NFIEEGLPKE YKHFKAPGVS
GPYHAPHLYN DREIRNILSF CSEDVILRHT PRVPLVSSNT GKLVQVKSMR DLLKVALEEI
LLRKICWDKV TESCLSIVQA TNDKPWRILP IASNATQGLV TALQRMGNCQ IEVDTGVGAP
QMDPAAPNAT GNASRSKIAI IGMSGRFPEA DGIEAFWDLL YKGLDVHKKV PPERWDVDAH
VDLTGTKRNT SKVPYGCWIN EPGLFDARFF NMSPREALQA DPAQRLALLS AYEALEMAGF
VPNSSPSTQR DRVGIFMGMT SDDYREINSG QDIDTYFIPG GNRAFTPGRI NYYFKFSGPS
VSVDTACSSS LAAIHLACNA IWRNDCDTAI SGGVNLLTNP DNHAGLDRGH FLSRTGNCNT
FDDGADGYCR ADGVGTIVLK RLEDAEADND PILGVINAAY TNHSAEAVSI TRPHVGAQAF
IFNKLLNDTN TNPHEIGYVE MHGTGTQAGD AVEMQSVLDV FAPDYRRGPA NSLYLGSAKS
NIGHGESASG VTSLVKVLLM LKQNMIPPHC GIKTKINHNF PTDLAQRNVH IAFKPTPWNR
PVSGKRKMFI NNFSAAGGNT ALLMEDAPLR EITGQDPRNV HVVSVTARSQ TALKRNINAL
IKYINTHAPS SPANERRFLA SLAYTTTARR MHHPFRVTAV GSSVKDIREV LRQRADQDVT
TPVPATAPKT GFVFTGQGAQ YTGMGKQLYE DCATFRSTIH RLDCIAQSQG FPSILPLIDG
SMPVEELSPV VTQLGTTCLQ MALVDYWKGL GVTPAFVLGH SLGDYAALNS AGVLSTSDTI
YLCGRRAQLL TQQCQMGTHA MLAVKAAVSE IQHLLDPDVH AVACINGPTE TVISGLSGRI
DELAQQCSSQ NLKSTKLKVP FAFHSAQVDP ILESFEESAQ GVIFHEPAVP FVSALNGEVI
TESNYSVLGP TYMVKHCREA VNFLGALEAT RHAKLMDDAT LWVEVGSHPI CSGMIKSTFG
PQATTVPSLR RDDDPWKILS NSLSTLHLAG VELNWKEFHQ DFSSAHEVLE LPRYGWDLKN
YWIPYTNNFC LTKGGPVTAE VSAPKSTFLT TAAQKIVECR EDGNTATLVV ENNIAEPELN
RVIQGHKVNG VALTPSSLYA DIAQTLVDHL ITKYKPEYQG LGLDVCDMTV PKPLIAKSGD
QFFRVSAVMS WAEQKASVQV WSVNGDGKKM AEHAHCTVKL FNCAERETEW KRNSYLIKRS
VSLLQDKAQT GEAHRMQRGM VYKLFAALVD YDENFKAIQE VILDSNEHEA TARVKFQAPP
GNFHRNPFWI DSFGHLSGFI MNASDATDSK NQVFVNHGWD SMRCLKKFSG DATYQTYVKM
QPWKDSIWAG DVYVFEGDDI IAVYGGVKFQ ALARKILDTV LPPIGGSKTV GAPAPAPARP
IGEKKAPPPI KVTGPPKPNP SNARAASPVV ARALEILAAE VGLSEAEMTD SLNFADYGVD
SLLSLTVTGR YREELNLDLE SSVFMDYPTI KDFKAYLAEK GFCDSSSPEP SSEPESKFSF
NSDASSEASS GLTTPGITSP VKHEAPKGGQ NKVWKSICSI IAEEIGVSVG DIDPSDNLPE
MGMDSLLSLT VLGRIRETLG MDLPAEFFLE NPTLDAVQAA LDLKPKMVPA ATPVSEPIRL
LETIDNTKPK TSRHPPATSI LLQGNPHTAT KKLFMFPDGS GSASSYATIP ALSPDVCVYG
LNCPYMKTPQ NLTCSLDELT EPYLAEIRRR QPKGPYSFGG WSAGGICAFD AARQLILEEG
EEVERLLLLD SPFPIGLEKL PPRLYKFFNS IGLFGDGKRA PPDWLLPHFL AFIDSLDAYK
AVPLPFNDSK WAKKMPKTYL IWAKDGVCGK PGDPRPEPAE DGSEDPREMQ WLLNDRTDLG
PNKWDTLVGP QNIGGIHVME DANHFTMTTG QKAKELSQFM ATAMSS
