AFLC_ASPPU
ID AFLC_ASPPU Reviewed; 2109 AA.
AC Q12053; A0A0F0I481; Q6UEH2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Norsolorinic acid synthase {ECO:0000303|PubMed:17086560};
DE Short=NSAS {ECO:0000303|PubMed:17086560};
DE EC=2.3.1.221 {ECO:0000269|PubMed:17086560, ECO:0000269|PubMed:18403714};
DE AltName: Full=Aflatoxin biosynthesis polyketide synthase {ECO:0000305};
DE AltName: Full=Aflatoxin biosynthesis protein C {ECO:0000303|PubMed:15006741};
DE AltName: Full=Polyketide synthase A {ECO:0000303|PubMed:18403714};
GN Name=aflC {ECO:0000303|PubMed:15006741};
GN Synonyms=pksA {ECO:0000303|PubMed:18403714},
GN pksL1 {ECO:0000303|PubMed:7592391}; ORFNames=P875_00052995;
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISRUPTION PHENOTYPE, FUNCTION,
RP AND INDUCTION.
RC STRAIN=ATCC 26691 / NRRL 2999 / CBS 921.70;
RX PubMed=7592391; DOI=10.1128/jb.177.21.6246-6254.1995;
RA Feng G.H., Leonard T.J.;
RT "Characterization of the polyketide synthase gene (pksL1) required for
RT aflatoxin biosynthesis in Aspergillus parasiticus.";
RL J. Bacteriol. 177:6246-6254(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15094053; DOI=10.1016/s0014-5793(04)00327-8;
RA Yu J., Bhatnagar D., Cleveland T.E.;
RT "Completed sequence of aflatoxin pathway gene cluster in Aspergillus
RT parasiticus.";
RL FEBS Lett. 564:126-130(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=1339261; DOI=10.1128/aem.58.11.3527-3537.1992;
RA Skory C.D., Chang P.K., Cary J., Linz J.E.;
RT "Isolation and characterization of a gene from Aspergillus parasiticus
RT associated with the conversion of versicolorin A to sterigmatocystin in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 58:3527-3537(1992).
RN [5]
RP FUNCTION.
RX PubMed=8434913; DOI=10.1128/aem.59.2.479-484.1993;
RA Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
RA Ullah A.H.J.;
RT "Purification of a 40-kilodalton methyltransferase active in the aflatoxin
RT biosynthetic pathway.";
RL Appl. Environ. Microbiol. 59:479-484(1993).
RN [6]
RP FUNCTION.
RX PubMed=8368836; DOI=10.1128/aem.59.8.2486-2492.1993;
RA Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic
RT acid to averufin.";
RL Appl. Environ. Microbiol. 59:2486-2492(1993).
RN [7]
RP FUNCTION.
RX PubMed=8368837; DOI=10.1128/aem.59.8.2493-2500.1993;
RA Yabe K., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: cyclase reaction in the
RT conversion of versiconal to versicolorin B and racemization of versiconal
RT hemiacetal acetate.";
RL Appl. Environ. Microbiol. 59:2493-2500(1993).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7565588; DOI=10.1007/bf02191593;
RA Chang P.K., Cary J.W., Yu J., Bhatnagar D., Cleveland T.E.;
RT "The Aspergillus parasiticus polyketide synthase gene pksA, a homolog of
RT Aspergillus nidulans wA, is required for aflatoxin B1 biosynthesis.";
RL Mol. Gen. Genet. 248:270-277(1995).
RN [9]
RP FUNCTION.
RX PubMed=10543813; DOI=10.1128/aem.65.11.4987-4994.1999;
RA Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
RT "Cloning and characterization of the O-methyltransferase I gene (dmtA) from
RT Aspergillus parasiticus associated with the conversions of
RT demethylsterigmatocystin to sterigmatocystin and
RT dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in aflatoxin
RT biosynthesis.";
RL Appl. Environ. Microbiol. 65:4987-4994(1999).
RN [10]
RP FUNCTION.
RX PubMed=10584035; DOI=10.1128/aem.65.12.5639-5641.1999;
RA Zhou R., Linz J.E.;
RT "Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
RT Aspergillus parasiticus.";
RL Appl. Environ. Microbiol. 65:5639-5641(1999).
RN [11]
RP FUNCTION.
RX PubMed=11055914; DOI=10.1128/aem.66.11.4715-4719.2000;
RA Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G., Bhatnagar D.,
RA Cleveland T.E.;
RT "adhA in Aspergillus parasiticus is involved in conversion of 5'-
RT hydroxyaverantin to averufin.";
RL Appl. Environ. Microbiol. 66:4715-4719(2000).
RN [12]
RP FUNCTION.
RX PubMed=16256699; DOI=10.1006/bioo.2001.1216;
RA Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
RA Townsend C.A.;
RT "Hexanoate synthase, a specialized type I fatty acid synthase in aflatoxin
RT B1 biosynthesis.";
RL Bioorg. Chem. 29:293-307(2001).
RN [13]
RP FUNCTION.
RX PubMed=11996570; DOI=10.1021/ja012185v;
RA Udwary D.W., Casillas L.K., Townsend C.A.;
RT "Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
RT cytochrome P-450 in the final step of aflatoxin biosynthesis.";
RL J. Am. Chem. Soc. 124:5294-5303(2002).
RN [14]
RP REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
RX PubMed=15006741; DOI=10.1128/aem.70.3.1253-1262.2004;
RA Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D., Cleveland T.E.,
RA Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
RT "Clustered pathway genes in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 70:1253-1262(2004).
RN [15]
RP FUNCTION.
RX PubMed=15528514; DOI=10.1128/aem.70.11.6518-6524.2004;
RA Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
RT "Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
RT formation.";
RL Appl. Environ. Microbiol. 70:6518-6524(2004).
RN [16]
RP FUNCTION.
RX PubMed=15932995; DOI=10.1128/aem.71.6.2999-3006.2005;
RA Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K., Nakajima H.;
RT "Aspergillus parasiticus cyclase catalyzes two dehydration steps in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 71:2999-3006(2005).
RN [17]
RP FUNCTION.
RX PubMed=16332900; DOI=10.1128/aem.71.12.8963-8965.2005;
RA Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
RT "An aflatoxin biosynthesis cluster gene encodes a novel oxidase required
RT for conversion of versicolorin a to sterigmatocystin.";
RL Appl. Environ. Microbiol. 71:8963-8965(2005).
RN [18]
RP FUNCTION.
RX PubMed=15771506; DOI=10.1021/ja0455188;
RA Henry K.M., Townsend C.A.;
RT "Ordering the reductive and cytochrome P450 oxidative steps in
RT demethylsterigmatocystin formation yields general insights into the
RT biosynthesis of aflatoxin and related fungal metabolites.";
RL J. Am. Chem. Soc. 127:3724-3733(2005).
RN [19]
RP FUNCTION.
RX PubMed=16461654; DOI=10.1128/aem.72.2.1096-1101.2006;
RA Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
RT "The aflatoxin biosynthesis cluster gene, aflX, encodes an oxidoreductase
RT involved in conversion of versicolorin A to demethylsterigmatocystin.";
RL Appl. Environ. Microbiol. 72:1096-1101(2006).
RN [20]
RP FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=17086560; DOI=10.1002/cbic.200600341;
RA Ma Y., Smith L.H., Cox R.J., Beltran-Alvarez P., Arthur C.J.,
RA Simpson F.R.S.T.J.;
RT "Catalytic relationships between type I and type II iterative polyketide
RT synthases: The Aspergillus parasiticus norsolorinic acid synthase.";
RL ChemBioChem 7:1951-1958(2006).
RN [21]
RP FUNCTION.
RX PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
RA Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y., Adachi Y.,
RA Nakajima H., Yabe K.;
RT "Involvement of the nadA gene in formation of G-group aflatoxins in
RT Aspergillus parasiticus.";
RL Fungal Genet. Biol. 45:1081-1093(2008).
RN [22]
RP DOMAIN, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18403714; DOI=10.1126/science.1154711;
RA Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L., Kelleher N.L.,
RA Townsend C.A.;
RT "Deconstruction of iterative multidomain polyketide synthase function.";
RL Science 320:243-246(2008).
RN [23]
RP INDUCTION.
RX PubMed=23113196;
RA Jahanshiri Z., Shams-Ghahfarokhi M., Allameh A., Razzaghi-Abyaneh M.;
RT "Effect of curcumin on Aspergillus parasiticus growth and expression of
RT major genes involved in the early and late stages of aflatoxin
RT biosynthesis.";
RL Iran. J. Public Health 41:72-79(2012).
RN [24]
RP STRUCTURE BY NMR OF 1705-1791 IN COMPLEX WITH PHOSPHOPANTETHEINE, AND
RP PHOSPHOPANTETHEINYLATION AT SER-1746.
RX PubMed=20136099; DOI=10.1021/bi902176v;
RA Wattana-amorn P., Williams C., Ploskon E., Cox R.J., Simpson T.J.,
RA Crosby J., Crump M.P.;
RT "Solution structure of an acyl carrier protein domain from a fungal type I
RT polyketide synthase.";
RL Biochemistry 49:2186-2193(2010).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1305-1660, DOMAIN, AND MUTAGENESIS
RP OF HIS-1345; GLY-1491; ASP-1543; THR-1546; GLN-1547 AND ASN-1554.
RX PubMed=19847268; DOI=10.1038/nature08475;
RA Crawford J.M., Korman T.P., Labonte J.W., Vagstad A.L., Hill E.A.,
RA Kamari-Bidkorpeh O., Tsai S.C., Townsend C.A.;
RT "Structural basis for biosynthetic programming of fungal aromatic
RT polyketide cyclization.";
RL Nature 461:1139-1143(2009).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1845-2109, DOMAIN, ACTIVE SITE,
RP AND MUTAGENESIS OF SER-1937; ASP-1964; ASP-2070 AND HIS-2088.
RX PubMed=20332208; DOI=10.1073/pnas.0913531107;
RA Korman T.P., Crawford J.M., Labonte J.W., Newman A.G., Wong J.,
RA Townsend C.A., Tsai S.C.;
RT "Structure and function of an iterative polyketide synthase thioesterase
RT domain catalyzing Claisen cyclization in aflatoxin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6246-6251(2010).
CC -!- FUNCTION: Norsolorinic acid synthase; part of the gene cluster that
CC mediates the biosynthesis of aflatoxins, a group of polyketide-derived
CC furanocoumarins, and part of the most toxic and carcinogenic compounds
CC among the known mycotoxins (PubMed:7592391, PubMed:15094053,
CC PubMed:7565588, PubMed:15006741). The four major aflatoxins produced by
CC A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin
CC G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). The first step of
CC the pathway is the conversion of acetate to norsolorinic acid (NOR) and
CC requires the fatty acid synthase subunits aflA and aflB, as well as the
CC PKS aflC (PubMed:15006741). AflC combines a hexanoyl starter unit and 7
CC malonyl-CoA extender units to synthesize the precursor NOR
CC (PubMed:17086560, PubMed:18403714). The hexanoyl starter unit is
CC provided to the acyl-carrier protein (ACP) domain by the fungal fatty
CC acid synthase aflA/aflB (PubMed:16256699). The second step is the
CC conversion of NOR to averantin (AVN) and requires the norsolorinic acid
CC ketoreductase aflD, which catalyzes the dehydration of norsolorinic
CC acid to form (1'S)-averantin (PubMed:10584035). The norsolorinic acid
CC reductases aflE and aflF may also play a role in the conversion of NOR
CC to AVN (PubMed:15006741). The cytochrome P450 monooxygenase aflG then
CC catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN)
CC (PubMed:8368836). The next step is performed by the 5'-hydroxyaverantin
CC dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which
CC is further converted to averufin (AVF) by aflK that plays a dual role
CC in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion
CC of 5'-oxoaverantin, as well as a versicolorin B synthase in a later
CC step in the pathway (PubMed:15006741, PubMed:11055914,
CC PubMed:15932995). The averufin oxidase aflI catalyzes the conversion of
CC AVF to versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is
CC then the substrate for the versiconal hemiacetal acetate esterase aflJ
CC to yield versiconal (VAL) (PubMed:15006741). Versicolorin B synthase
CC aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran
CC ring of aflatoxin which is required for DNA-binding, thus giving to
CC aflatoxin its activity as a mutagen (PubMed:15006741, PubMed:8368837,
CC PubMed:15932995). Then, the activity of the versicolorin B desaturase
CC aflL leads to versicolorin A (VERA) (PubMed:15006741, PubMed:8368837).
CC A branch point starts from VERB since it can also be converted to
CC dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA
CC being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins
CC B2 and G2 (PubMed:15006741). Next, the versicolorin reductase aflM and
CC the cytochrome P450 monooxygenase aflN are involved in conversion of
CC VERA to demethylsterigmatocystin (DMST) (PubMed:15006741,
CC PubMed:1339261, PubMed:15771506). AflX and aflY seem also involved in
CC this step, through probable aflX-mediated epoxide ring-opening step
CC following versicolorin A oxidation and aflY-mediated Baeyer-Villiger
CC oxidation required for the formation of the xanthone ring
CC (PubMed:16332900, PubMed:16461654). The methyltransferase aflO then
CC leads to the modification of DMST to sterigmatocystin (ST), and of
CC DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both ST and
CC DHST are then substrates of the O-methyltransferase aflP to yield O-
CC methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin
CC (DHOMST), respectively (PubMed:8434913). Finally OMST is converted to
CC aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the
CC action of several enzymes including O-methylsterigmatocystin
CC oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also
CC the NADH-dependent flavin oxidoreductase nadA which is specifically
CC required for the synthesis of AFG1 (PubMed:15006741, PubMed:11996570,
CC PubMed:15528514, PubMed:18486503). {ECO:0000269|PubMed:10543813,
CC ECO:0000269|PubMed:10584035, ECO:0000269|PubMed:11055914,
CC ECO:0000269|PubMed:11996570, ECO:0000269|PubMed:1339261,
CC ECO:0000269|PubMed:15006741, ECO:0000269|PubMed:15528514,
CC ECO:0000269|PubMed:15771506, ECO:0000269|PubMed:15932995,
CC ECO:0000269|PubMed:16256699, ECO:0000269|PubMed:16332900,
CC ECO:0000269|PubMed:16461654, ECO:0000269|PubMed:17086560,
CC ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
CC ECO:0000269|PubMed:7565588, ECO:0000269|PubMed:7592391,
CC ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
CC ECO:0000269|PubMed:8434913, ECO:0000305|PubMed:15006741,
CC ECO:0000305|PubMed:15094053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6 H(+) + hexanoyl-[ACP] + 7 malonyl-CoA = 7 CO2 + 7 CoA + 2
CC H2O + holo-[ACP] + noranthrone; Xref=Rhea:RHEA:35179, Rhea:RHEA-
CC COMP:9632, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:77904, ChEBI:CHEBI:78459;
CC EC=2.3.1.221; Evidence={ECO:0000269|PubMed:18403714};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000269|PubMed:20136099};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000269|PubMed:20136099};
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC {ECO:0000269|PubMed:15094053, ECO:0000305|PubMed:15006741}.
CC -!- INTERACTION:
CC Q12053; Q12053: aflC; NbExp=4; IntAct=EBI-15811477, EBI-15811477;
CC -!- INDUCTION: Actively expressed at 27 degrees Celsius but not at all at a
CC temperature higher than 35 degrees Celsius (PubMed:7592391). Expression
CC is repressed by curcumin (PubMed:23113196).
CC {ECO:0000269|PubMed:23113196, ECO:0000269|PubMed:7592391}.
CC -!- DOMAIN: The domain architecture includes starter unit:ACP transacylase
CC (SAT), beta-ketoacyl synthase (KS), malonyl-CoA:ACP transacylase (MAT),
CC product template (PT), acyl-carrier domain (ACP), and
CC thioesterase/Claisen cyclase (TE/CLC) domains (PubMed:17086560). The
CC SAT domain receives a C6-fatty acid starter unit and transfers it onto
CC the ACP for chain elongation. The KS accepts the hexanoyl-ACP unit and
CC subsequent malonate extender units are loaded onto the ACP from the MAT
CC domain for chain extension to generate the linear poly-beta-keto ACP-
CC bound intermediate. The linear intermediate is then cyclized and
CC aromatized in the PT domain. The resulting bicyclic intermediate is
CC ultimately transferred from the ACP to the TE/CLC domain and undergoes
CC Claisen-type C-C bond cyclization to release the product norsolorinic
CC acid anthrone (noranthrone), which spontaneously oxidizes in vitro to
CC norsolorinic acid (PubMed:17086560, PubMed:18403714, PubMed:19847268,
CC PubMed:20332208). {ECO:0000269|PubMed:17086560,
CC ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:19847268,
CC ECO:0000269|PubMed:20332208}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of norsolorinic acid, as
CC well as of the four major forms of aflatoxin: AFB1, AFB2, AFG1 and AFG2
CC (PubMed:7592391, PubMed:7565588). {ECO:0000269|PubMed:7565588,
CC ECO:0000269|PubMed:7592391}.
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DR EMBL; L42766; AAC41675.1; -; mRNA.
DR EMBL; L42765; AAC41674.1; -; Genomic_DNA.
DR EMBL; AY371490; AAS66004.1; -; Genomic_DNA.
DR EMBL; JZEE01000728; KJK60793.1; -; Genomic_DNA.
DR PIR; T17490; T17490.
DR PDB; 2KR5; NMR; -; A=1705-1791.
DR PDB; 3HRQ; X-ray; 1.80 A; A/B=1305-1660.
DR PDB; 3HRR; X-ray; 1.90 A; A/B=1305-1660.
DR PDB; 3ILS; X-ray; 1.70 A; A=1845-2109.
DR PDB; 5KBZ; X-ray; 1.80 A; A/B=1305-1660.
DR PDBsum; 2KR5; -.
DR PDBsum; 3HRQ; -.
DR PDBsum; 3HRR; -.
DR PDBsum; 3ILS; -.
DR PDBsum; 5KBZ; -.
DR AlphaFoldDB; Q12053; -.
DR BMRB; Q12053; -.
DR SMR; Q12053; -.
DR DIP; DIP-59286N; -.
DR STRING; 1403190.Q12053; -.
DR ESTHER; aspor-PKSL1; Thioesterase.
DR EnsemblFungi; KJK60793; KJK60793; P875_00052995.
DR BioCyc; MetaCyc:MON-17895; -.
DR BRENDA; 2.3.1.221; 523.
DR UniPathway; UPA00287; -.
DR EvolutionaryTrace; Q12053; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0102973; F:norsolorinate anthrone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
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; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
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; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2109
FT /note="Norsolorinic acid synthase"
FT /id="PRO_0000180303"
FT DOMAIN 1709..1788
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:17086560"
FT REGION 1..374
FT /note="Starter unit:ACP transacylase (SAT) domain"
FT /evidence="ECO:0000255"
FT REGION 363..819
FT /note="Ketoacyl synthase (KS)domain"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17086560"
FT REGION 895..1216
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17086560"
FT REGION 1206..1713
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1281..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1867..2102
FT /note="Thioesterase/Claisen cyclase (TE/CLC) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1669..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 543
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 993
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1937
FT /note="For thioesterase activity"
FT /evidence="ECO:0000269|PubMed:20332208"
FT MOD_RES 1746
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:20136099"
FT MUTAGEN 1345
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19847268"
FT MUTAGEN 1491
FT /note="G->L: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19847268"
FT MUTAGEN 1543
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19847268"
FT MUTAGEN 1546
FT /note="T->A: 40% decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:19847268"
FT MUTAGEN 1547
FT /note="Q->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19847268"
FT MUTAGEN 1554
FT /note="N->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19847268"
FT MUTAGEN 1937
FT /note="S->A: Abolishes hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:20332208"
FT MUTAGEN 1964
FT /note="D->N: Abolishes hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:20332208"
FT MUTAGEN 2070
FT /note="D->N: Slight reduction in hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:20332208"
FT MUTAGEN 2088
FT /note="H->F: Abolishes hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:20332208"
FT STRAND 1314..1321
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1324..1332
FT /evidence="ECO:0007829|PDB:3HRQ"
FT TURN 1336..1338
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1339..1342
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1345..1347
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1350..1352
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1355..1372
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1386..1394
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1407..1415
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1421..1423
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1426..1434
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1442..1452
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1455..1462
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1464..1479
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1483..1487
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1488..1495
FT /evidence="ECO:0007829|PDB:3HRQ"
FT TURN 1496..1498
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1503..1505
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1508..1514
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1515..1517
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1519..1525
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1526..1528
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1539..1554
FT /evidence="ECO:0007829|PDB:3HRQ"
FT TURN 1561..1563
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1564..1576
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1585..1591
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1600..1609
FT /evidence="ECO:0007829|PDB:3HRQ"
FT STRAND 1612..1626
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1627..1635
FT /evidence="ECO:0007829|PDB:3HRQ"
FT HELIX 1712..1726
FT /evidence="ECO:0007829|PDB:2KR5"
FT HELIX 1730..1732
FT /evidence="ECO:0007829|PDB:2KR5"
FT HELIX 1739..1742
FT /evidence="ECO:0007829|PDB:2KR5"
FT HELIX 1746..1758
FT /evidence="ECO:0007829|PDB:2KR5"
FT TURN 1770..1772
FT /evidence="ECO:0007829|PDB:2KR5"
FT HELIX 1777..1785
FT /evidence="ECO:0007829|PDB:2KR5"
FT STRAND 1853..1859
FT /evidence="ECO:0007829|PDB:3ILS"
FT TURN 1861..1863
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 1864..1871
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 1878..1881
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 1888..1897
FT /evidence="ECO:0007829|PDB:3ILS"
FT TURN 1899..1902
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 1904..1906
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 1911..1925
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 1931..1936
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 1938..1952
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 1957..1964
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 1976..1984
FT /evidence="ECO:0007829|PDB:3ILS"
FT TURN 1985..1990
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 1991..1994
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 1996..1998
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 2006..2016
FT /evidence="ECO:0007829|PDB:3ILS"
FT TURN 2017..2019
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 2032..2040
FT /evidence="ECO:0007829|PDB:3ILS"
FT TURN 2045..2047
FT /evidence="ECO:0007829|PDB:3ILS"
FT TURN 2056..2058
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 2069..2072
FT /evidence="ECO:0007829|PDB:3ILS"
FT STRAND 2078..2087
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 2090..2092
FT /evidence="ECO:0007829|PDB:3ILS"
FT TURN 2094..2097
FT /evidence="ECO:0007829|PDB:3ILS"
FT HELIX 2098..2107
FT /evidence="ECO:0007829|PDB:3ILS"
SQ SEQUENCE 2109 AA; 230716 MW; CB701372A16D8551 CRC64;
MAQSRQLFLF GDQTADFVPK LRSLLSVQDS PILAAFLDQS HYVVRAQMLQ SMNTVDHKLA
RTADLRQMVQ KYVDGKLTPA FRTALVCLCQ LGCFIREYEE SGNMYPQPSD SYVLGFCMGS
LAAVAVSCSR SLSELLPIAV QTVLIAFRLG LCALEMRDRV DGCSDDRGDP WSTIVWGLDP
QQARDQIEVF CRTTNVPQTR RPWISCISKN AITLSGSPST LRAFCAMPQM AQHRTAPIPI
CLPAHNGALF TQADITTILD TTPTTPWEQL PGQIPYISHV TGNVVQTSNY RDLIEVALSE
TLLEQVRLDL VETGLPRLLQ SRQVKSVTIV PFLTRMNETM SNILPDSFIS TETRTDTGRA
IPASGRPGAG KCKLAIVSMS GRFPESPTTE SFWDLLYKGL DVCKEVPRRR WDINTHVDPS
GKARNKGATK WGCWLDFSGD FDPRFFGISP KEAPQMDPAQ RMALMSTYEA MERAGLVPDT
TPSTQRDRIG VFHGVTSNDW METNTAQNID TYFITGGNRG FIPGRINFCF EFAGPSYTND
TACSSSLAAI HLACNSLWRG DCDTAVAGGT NMIYTPDGHT GLDKGFFLSR TGNCKPYDDK
ADGYCRAEGV GTVFIKRLED ALADNDPILG VILDAKTNHS AMSESMTRPH VGAQIDNMTA
ALNTTGLHPN DFSYIEMHGT GTQVGDAVEM ESVLSVFAPS ETARKADQPL FVGSAKANVG
HGEGVSGVTS LIKVLMMMQH DTIPPHCGIK PGSKINRNFP DLGARNVHIA FEPKPWPRTH
TPRRVLINNF SAAGGNTALI VEDAPERHWP TEKDPRSSHI VALSAHVGAS MKTNLERLHQ
YLLKNPHTDL AQLSYTTTAR RWHYLHRVSV TGASVEEVTR KLEMAIQNGD GVSRPKSKPK
ILFAFTGQGS QYATMGKQVY DAYPSFREDL EKFDRLAQSH GFPSFLHVCT SPKGDVEEMA
PVVVQLAITC LQMALTNLMT SFGIRPDVTV GHSLGEFAAL YAAGVLSASD VVYLVGQRAE
LLQERCQRGT HAMLAVKATP EALSQWIQDH DCEVACINGP EDTVLSGTTK NVAEVQRAMT
DNGIKCTLLK LPFAFHSAQV QPILDDFEAL AQGATFAKPQ LLILSPLLRT EIHEQGVVTP
SYVAQHCRHT VDMAQALRSA REKGLIDDKT LVIELGPKPL ISGMVKMTLG DKISTLPTLA
PNKAIWPSLQ KILTSVYTGG WDINWKKYHA PFASSQKVVD LPSYGWDLKD YYIPYQGDWC
LHRHQQDCKC AAPGHEIKTA DYQVPPESTP HRPSKLDPSK EAFPEIKTTT TLHRVVEETT
KPLGATLVVE TDISRKDVNG LARGHLVDGI PLCTPSFYAD IAMQVGQYSM QRLRAGHPGA
GAIDGLVDVS DMVVDKALVP HGKGPQLLRT TLTMEWPPKA AATTRSAKVK FATYFADGKL
DTEHASCTVR FTSDAQLKSL RRSVSEYKTH IRQLHDGHAK GQFMRYNRKT GYKLMSSMAR
FNPDYMLLDY LVLNEAENEA ASGVDFSLGS SEGTFAAHPA HVDAITQVAG FAMNANDNVD
IEKQVYVNHG WDSFQIYQPL DNSKSYQVYT KMGQAKENDL VHGDVVVLDG EQIVAFFRGL
TLRSVPRGAL RVVLQTTVKK ADRQLGFKTM PSPPPPTTTM PISPYKPANT QVSSQAIPAE
ATHSHTPPQP KHSPVPETAG SAPAAKGVGV SNEKLDAVMR VVSEESGIAL EELTDDSNFA
DMGIDSLSSM VIGSRFREDL GLDLGPEFSL FIDCTTVRAL KDFMLGSGDA GSGSNVEDPP
PSATPGINPE TDWSSSASDS IFASEDHGHS SESGADTGSP PALDLKPYCR PSTSVVLQGL
PMVARKTLFM LPDGGGSAFS YASLPRLKSD TAVVGLNCPY ARDPENMNCT HGAMIESFCN
EIRRRQPRGP YHLGGWSSGG AFAYVVAEAL VNQGEEVHSL IIIDAPIPQA MEQLPRAFYE
HCNSIGLFAT QPGASPDGST EPPSYLIPHF TAVVDVMLDY KLAPLHARRM PKVGIVWAAD
TVMDERDAPK MKGMHFMIQK RTEFGPDGWD TIMPGASFDI VRADGANHFT LMQKEHVSII
SDLIDRVMA
