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Norsolorinic acid synthase (NSAS) (EC 2.3.1.221) (Aflatoxin biosynthesis polyketide synthase) (Aflatoxin biosynthesis protein C) (Polyketide synthase A)

 AFLC_ASPPU              Reviewed;        2109 AA.
Q12053; A0A0F0I481; Q6UEH2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 105.
RecName: Full=Norsolorinic acid synthase {ECO:0000303|PubMed:17086560};
Short=NSAS {ECO:0000303|PubMed:17086560};
EC=2.3.1.221 {ECO:0000269|PubMed:17086560, ECO:0000269|PubMed:18403714};
AltName: Full=Aflatoxin biosynthesis polyketide synthase {ECO:0000305};
AltName: Full=Aflatoxin biosynthesis protein C {ECO:0000303|PubMed:15006741};
AltName: Full=Polyketide synthase A {ECO:0000303|PubMed:18403714};
Name=aflC {ECO:0000303|PubMed:15006741};
Synonyms=pksA {ECO:0000303|PubMed:18403714},
pksL1 {ECO:0000303|PubMed:7592391}; ORFNames=P875_00052995;
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 /
SU-1).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=1403190;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISRUPTION PHENOTYPE,
FUNCTION, AND INDUCTION.
STRAIN=ATCC 26691 / NRRL 2999 / CBS 921.70;
PubMed=7592391; DOI=10.1128/jb.177.21.6246-6254.1995;
Feng G.H., Leonard T.J.;
"Characterization of the polyketide synthase gene (pksL1) required for
aflatoxin biosynthesis in Aspergillus parasiticus.";
J. Bacteriol. 177:6246-6254(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=15094053; DOI=10.1016/S0014-5793(04)00327-8;
Yu J., Bhatnagar D., Cleveland T.E.;
"Completed sequence of aflatoxin pathway gene cluster in Aspergillus
parasiticus.";
FEBS Lett. 564:126-130(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R.,
Ehrlich K.C., Bhatnagar D., Cleveland T.E., Bennett J.W.,
Nierman W.C.;
"Draft genome sequence of Aspergillus parasiticus SU-1.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=1339261;
Skory C.D., Chang P.K., Cary J., Linz J.E.;
"Isolation and characterization of a gene from Aspergillus parasiticus
associated with the conversion of versicolorin A to sterigmatocystin
in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 58:3527-3537(1992).
[5]
FUNCTION.
PubMed=8434913;
Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
Ullah A.H.J.;
"Purification of a 40-kilodalton methyltransferase active in the
aflatoxin biosynthetic pathway.";
Appl. Environ. Microbiol. 59:479-484(1993).
[6]
FUNCTION.
PubMed=8368836;
Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: conversion of
norsolorinic acid to averufin.";
Appl. Environ. Microbiol. 59:2486-2492(1993).
[7]
FUNCTION.
PubMed=8368837;
Yabe K., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: cyclase reaction in
the conversion of versiconal to versicolorin B and racemization of
versiconal hemiacetal acetate.";
Appl. Environ. Microbiol. 59:2493-2500(1993).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=7565588; DOI=10.1007/BF02191593;
Chang P.K., Cary J.W., Yu J., Bhatnagar D., Cleveland T.E.;
"The Aspergillus parasiticus polyketide synthase gene pksA, a homolog
of Aspergillus nidulans wA, is required for aflatoxin B1
biosynthesis.";
Mol. Gen. Genet. 248:270-277(1995).
[9]
FUNCTION.
PubMed=10543813;
Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
"Cloning and characterization of the O-methyltransferase I gene (dmtA)
from Aspergillus parasiticus associated with the conversions of
demethylsterigmatocystin to sterigmatocystin and
dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 65:4987-4994(1999).
[10]
FUNCTION.
PubMed=10584035;
Zhou R., Linz J.E.;
"Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
Aspergillus parasiticus.";
Appl. Environ. Microbiol. 65:5639-5641(1999).
[11]
FUNCTION.
PubMed=11055914; DOI=10.1128/AEM.66.11.4715-4719.2000;
Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G.,
Bhatnagar D., Cleveland T.E.;
"adhA in Aspergillus parasiticus is involved in conversion of 5'-
hydroxyaverantin to averufin.";
Appl. Environ. Microbiol. 66:4715-4719(2000).
[12]
FUNCTION.
PubMed=16256699; DOI=10.1006/bioo.2001.1216;
Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
Townsend C.A.;
"Hexanoate synthase, a specialized type I fatty acid synthase in
aflatoxin B1 biosynthesis.";
Bioorg. Chem. 29:293-307(2001).
[13]
FUNCTION.
PubMed=11996570; DOI=10.1021/ja012185v;
Udwary D.W., Casillas L.K., Townsend C.A.;
"Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
cytochrome P-450 in the final step of aflatoxin biosynthesis.";
J. Am. Chem. Soc. 124:5294-5303(2002).
[14]
REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
PubMed=15006741; DOI=10.1128/AEM.70.3.1253-1262.2004;
Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D.,
Cleveland T.E., Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
"Clustered pathway genes in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 70:1253-1262(2004).
[15]
FUNCTION.
PubMed=15528514; DOI=10.1128/AEM.70.11.6518-6524.2004;
Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
"Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
formation.";
Appl. Environ. Microbiol. 70:6518-6524(2004).
[16]
FUNCTION.
PubMed=15932995; DOI=10.1128/AEM.71.6.2999-3006.2005;
Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K.,
Nakajima H.;
"Aspergillus parasiticus cyclase catalyzes two dehydration steps in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 71:2999-3006(2005).
[17]
FUNCTION.
PubMed=16332900; DOI=10.1128/AEM.71.12.8963-8965.2005;
Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
"An aflatoxin biosynthesis cluster gene encodes a novel oxidase
required for conversion of versicolorin a to sterigmatocystin.";
Appl. Environ. Microbiol. 71:8963-8965(2005).
[18]
FUNCTION.
PubMed=15771506; DOI=10.1021/ja0455188;
Henry K.M., Townsend C.A.;
"Ordering the reductive and cytochrome P450 oxidative steps in
demethylsterigmatocystin formation yields general insights into the
biosynthesis of aflatoxin and related fungal metabolites.";
J. Am. Chem. Soc. 127:3724-3733(2005).
[19]
FUNCTION.
PubMed=16461654; DOI=10.1128/AEM.72.2.1096-1101.2006;
Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
"The aflatoxin biosynthesis cluster gene, aflX, encodes an
oxidoreductase involved in conversion of versicolorin A to
demethylsterigmatocystin.";
Appl. Environ. Microbiol. 72:1096-1101(2006).
[20]
FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
PubMed=17086560; DOI=10.1002/cbic.200600341;
Ma Y., Smith L.H., Cox R.J., Beltran-Alvarez P., Arthur C.J.,
Simpson F.R.S.T.J.;
"Catalytic relationships between type I and type II iterative
polyketide synthases: The Aspergillus parasiticus norsolorinic acid
synthase.";
ChemBioChem 7:1951-1958(2006).
[21]
FUNCTION.
PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y.,
Adachi Y., Nakajima H., Yabe K.;
"Involvement of the nadA gene in formation of G-group aflatoxins in
Aspergillus parasiticus.";
Fungal Genet. Biol. 45:1081-1093(2008).
[22]
DOMAIN, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18403714; DOI=10.1126/science.1154711;
Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L.,
Kelleher N.L., Townsend C.A.;
"Deconstruction of iterative multidomain polyketide synthase
function.";
Science 320:243-246(2008).
[23]
INDUCTION.
PubMed=23113196;
Jahanshiri Z., Shams-Ghahfarokhi M., Allameh A., Razzaghi-Abyaneh M.;
"Effect of curcumin on Aspergillus parasiticus growth and expression
of major genes involved in the early and late stages of aflatoxin
biosynthesis.";
Iran. J. Public Health 41:72-79(2012).
[24]
STRUCTURE BY NMR OF 1705-1791 IN COMPLEX WITH PHOSPHOPANTETHEINE, AND
PHOSPHOPANTETHEINYLATION AT SER-1746.
PubMed=20136099; DOI=10.1021/bi902176v;
Wattana-amorn P., Williams C., Ploskon E., Cox R.J., Simpson T.J.,
Crosby J., Crump M.P.;
"Solution structure of an acyl carrier protein domain from a fungal
type I polyketide synthase.";
Biochemistry 49:2186-2193(2010).
[25]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1305-1660, DOMAIN, AND
MUTAGENESIS OF HIS-1345; GLY-1491; ASP-1543; THR-1546; GLN-1547 AND
ASN-1554.
PubMed=19847268; DOI=10.1038/nature08475;
Crawford J.M., Korman T.P., Labonte J.W., Vagstad A.L., Hill E.A.,
Kamari-Bidkorpeh O., Tsai S.C., Townsend C.A.;
"Structural basis for biosynthetic programming of fungal aromatic
polyketide cyclization.";
Nature 461:1139-1143(2009).
[26]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1845-2109, DOMAIN, ACTIVE
SITE, AND MUTAGENESIS OF SER-1937; ASP-1964; ASP-2070 AND HIS-2088.
PubMed=20332208; DOI=10.1073/pnas.0913531107;
Korman T.P., Crawford J.M., Labonte J.W., Newman A.G., Wong J.,
Townsend C.A., Tsai S.C.;
"Structure and function of an iterative polyketide synthase
thioesterase domain catalyzing Claisen cyclization in aflatoxin
biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:6246-6251(2010).
-!- FUNCTION: Norsolorinic acid synthase; part of the gene cluster
that mediates the biosynthesis of aflatoxins, a group of
polyketide-derived furanocoumarins, and part of the most toxic and
carcinogenic compounds among the known mycotoxins (PubMed:7592391,
PubMed:15094053, PubMed:7565588, PubMed:15006741). The four major
aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1),
aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2)
(PubMed:15006741). The first step of the pathway is the conversion
of acetate to norsolorinic acid (NOR) and requires the fatty acid
synthase subunits aflA and aflB, as well as the PKS aflC
(PubMed:15006741). AflC combines a hexanoyl starter unit and 7
malonyl-CoA extender units to synthesize the precursor NOR
(PubMed:17086560, PubMed:18403714). The hexanoyl starter unit is
provided to the acyl-carrier protein (ACP) domain by the fungal
fatty acid synthase aflA/aflB (PubMed:16256699). The second step
is the conversion of NOR to averantin (AVN) and requires the
norsolorinic acid ketoreductase aflD, which catalyzes the
dehydration of norsolorinic acid to form (1'S)-averantin
(PubMed:10584035). The norsolorinic acid reductases aflE and aflF
may also play a role in the conversion of NOR to AVN
(PubMed:15006741). The cytochrome P450 monooxygenase aflG then
catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN)
(PubMed:8368836). The next step is performed by the 5'-
hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-
oxoaverantin (OAVN) which is further converted to averufin (AVF)
by aflK that plays a dual role in the pathway, as a 5'-
oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin,
as well as a versicolorin B synthase in a later step in the
pathway (PubMed:15006741, PubMed:11055914, PubMed:15932995). The
averufin oxidase aflI catalyzes the conversion of AVF to
versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is then
the substrate for the versiconal hemiacetal acetate esterase aflJ
to yield versiconal (VAL) (PubMed:15006741). Versicolorin B
synthase aflK then converts VAL to versicolorin B (VERB) by
closing the bisfuran ring of aflatoxin which is required for DNA-
binding, thus giving to aflatoxin its activity as a mutagen
(PubMed:15006741, PubMed:8368837, PubMed:15932995). Then, the
activity of the versicolorin B desaturase aflL leads to
versicolorin A (VERA) (PubMed:15006741, PubMed:8368837). A branch
point starts from VERB since it can also be converted to
dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL,
VERA being a precursor for aflatoxins B1 and G1, and DMDHST for
aflatoxins B2 and G2 (PubMed:15006741). Next, the versicolorin
reductase aflM and the cytochrome P450 monooxygenase aflN are
involved in conversion of VERA to demethylsterigmatocystin (DMST)
(PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and aflY
seem also involved in this step, through probable aflX-mediated
epoxide ring-opening step following versicolorin A oxidation and
aflY-mediated Baeyer-Villiger oxidation required for the formation
of the xanthone ring (PubMed:16332900, PubMed:16461654). The
methyltransferase aflO then leads to the modification of DMST to
sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin
(DHST) (PubMed:10543813). Both ST and DHST are then substrates of
the O-methyltransferase aflP to yield O-methylsterigmatocystin
(OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively
(PubMed:8434913). Finally OMST is converted to aflatoxins B1 and
G1, and DHOMST to aflatoxins B2 and G2, via the action of several
enzymes including O-methylsterigmatocystin oxidoreductase aflQ,
the cytodhrome P450 monooxygenase aflU, but also the NADH-
dependent flavin oxidoreductase nadA which is specifically
required for the synthesis of AFG1 (PubMed:15006741,
PubMed:11996570, PubMed:15528514, PubMed:18486503).
{ECO:0000269|PubMed:10543813, ECO:0000269|PubMed:10584035,
ECO:0000269|PubMed:11055914, ECO:0000269|PubMed:11996570,
ECO:0000269|PubMed:1339261, ECO:0000269|PubMed:15006741,
ECO:0000269|PubMed:15528514, ECO:0000269|PubMed:15771506,
ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:16256699,
ECO:0000269|PubMed:16332900, ECO:0000269|PubMed:16461654,
ECO:0000269|PubMed:17086560, ECO:0000269|PubMed:18403714,
ECO:0000269|PubMed:18486503, ECO:0000269|PubMed:7565588,
ECO:0000269|PubMed:7592391, ECO:0000269|PubMed:8368836,
ECO:0000269|PubMed:8368837, ECO:0000269|PubMed:8434913,
ECO:0000305|PubMed:15006741, ECO:0000305|PubMed:15094053}.
-!- CATALYTIC ACTIVITY: 7 malonyl-CoA + hexanoyl-[acyl-carrier
protein] = 7 CoA + norsolorinate anthrone + [acyl-carrier protein]
+ 7 CO(2) + 2 H(2)O. {ECO:0000269|PubMed:18403714}.
-!- COFACTOR:
Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
Evidence={ECO:0000269|PubMed:20136099};
Note=Binds 1 phosphopantetheine covalently.
{ECO:0000269|PubMed:20136099};
-!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
{ECO:0000269|PubMed:15094053, ECO:0000305|PubMed:15006741}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-15811477, EBI-15811477;
-!- INDUCTION: Actively expressed at 27 degrees Celsius but not at all
at a temperature higher than 35 degrees Celsius (PubMed:7592391).
Expression is repressed by curcumin (PubMed:23113196).
{ECO:0000269|PubMed:23113196, ECO:0000269|PubMed:7592391}.
-!- DOMAIN: The domain architecture includes starter unit:ACP
transacylase (SAT), beta-ketoacyl synthase (KS), malonyl-CoA:ACP
transacylase (MAT), product template (PT), acyl-carrier domain
(ACP), and thioesterase/Claisen cyclase (TE/CLC) domains
(PubMed:17086560). The SAT domain receives a C6-fatty acid starter
unit and transfers it onto the ACP for chain elongation. The KS
accepts the hexanoyl-ACP unit and subsequent malonate extender
units are loaded onto the ACP from the MAT domain for chain
extension to generate the linear poly-beta-keto ACP-bound
intermediate. The linear intermediate is then cyclized and
aromatized in the PT domain. The resulting bicyclic intermediate
is ultimately transferred from the ACP to the TE/CLC domain and
undergoes Claisen-type C-C bond cyclization to release the product
norsolorinic acid anthrone (noranthrone), which spontaneously
oxidizes in vitro to norsolorinic acid (PubMed:17086560,
PubMed:18403714, PubMed:19847268, PubMed:20332208).
{ECO:0000269|PubMed:17086560, ECO:0000269|PubMed:18403714,
ECO:0000269|PubMed:19847268, ECO:0000269|PubMed:20332208}.
-!- DISRUPTION PHENOTYPE: Impairs the production of norsolorinic acid,
as well as of the four major forms of aflatoxin: AFB1, AFB2, AFG1
and AFG2 (PubMed:7592391, PubMed:7565588).
{ECO:0000269|PubMed:7565588, ECO:0000269|PubMed:7592391}.
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EMBL; L42766; AAC41675.1; -; mRNA.
EMBL; L42765; AAC41674.1; -; Genomic_DNA.
EMBL; AY371490; AAS66004.1; -; Genomic_DNA.
EMBL; JZEE01000728; KJK60793.1; -; Genomic_DNA.
PIR; T17490; T17490.
PDB; 2KR5; NMR; -; A=1705-1791.
PDB; 3HRQ; X-ray; 1.80 A; A/B=1305-1660.
PDB; 3HRR; X-ray; 1.90 A; A/B=1305-1660.
PDB; 3ILS; X-ray; 1.70 A; A=1845-2109.
PDB; 5KBZ; X-ray; 1.80 A; A/B=1305-1660.
PDBsum; 2KR5; -.
PDBsum; 3HRQ; -.
PDBsum; 3HRR; -.
PDBsum; 3ILS; -.
PDBsum; 5KBZ; -.
ProteinModelPortal; Q12053; -.
SMR; Q12053; -.
DIP; DIP-59286N; -.
ESTHER; aspor-PKSL1; Thioesterase.
PRIDE; Q12053; -.
EnsemblFungi; KJK60793; KJK60793; P875_00052995.
BRENDA; 2.3.1.221; 523.
UniPathway; UPA00287; -.
EvolutionaryTrace; Q12053; -.
Proteomes; UP000033540; Unassembled WGS sequence.
GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0102973; F:norsolorinate anthrone synthase activity; IEA:UniProtKB-EC.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.30.70.250; -; 1.
Gene3D; 3.40.47.10; -; 2.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR030918; PT_fungal_PKS.
InterPro; IPR032088; SAT.
InterPro; IPR001031; Thioesterase.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
Pfam; PF16073; SAT; 1.
Pfam; PF00975; Thioesterase; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53474; SSF53474; 1.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS50075; CARRIER; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome;
Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 2109 Norsolorinic acid synthase.
/FTId=PRO_0000180303.
DOMAIN 1709 1788 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258,
ECO:0000269|PubMed:17086560}.
REGION 1 374 Starter unit:ACP transacylase (SAT)
domain. {ECO:0000255}.
REGION 363 819 Ketoacyl synthase (KS)domain.
{ECO:0000255,
ECO:0000269|PubMed:17086560}.
REGION 895 1216 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255,
ECO:0000269|PubMed:17086560}.
REGION 1206 1713 Product template (PT) domain.
{ECO:0000255}.
REGION 1867 2102 Thioesterase/Claisen cyclase (TE/CLC)
domain. {ECO:0000255}.
ACT_SITE 543 543 For beta-ketoacyl synthase activity.
{ECO:0000250}.
ACT_SITE 993 993 For acyl/malonyl transferase activity.
{ECO:0000250}.
ACT_SITE 1937 1937 For thioesterase activity.
{ECO:0000269|PubMed:20332208}.
MOD_RES 1746 1746 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258,
ECO:0000269|PubMed:20136099}.
MUTAGEN 1345 1345 H->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19847268}.
MUTAGEN 1491 1491 G->L: Abolishes catalytic activity.
{ECO:0000269|PubMed:19847268}.
MUTAGEN 1543 1543 D->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19847268}.
MUTAGEN 1546 1546 T->A: 40% decrease in catalytic activity.
{ECO:0000269|PubMed:19847268}.
MUTAGEN 1547 1547 Q->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19847268}.
MUTAGEN 1554 1554 N->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19847268}.
MUTAGEN 1937 1937 S->A: Abolishes hydrolytic activity.
{ECO:0000269|PubMed:20332208}.
MUTAGEN 1964 1964 D->N: Abolishes hydrolytic activity.
{ECO:0000269|PubMed:20332208}.
MUTAGEN 2070 2070 D->N: Slight reduction in hydrolytic
activity. {ECO:0000269|PubMed:20332208}.
MUTAGEN 2088 2088 H->F: Abolishes hydrolytic activity.
{ECO:0000269|PubMed:20332208}.
STRAND 1314 1321 {ECO:0000244|PDB:3HRQ}.
STRAND 1324 1332 {ECO:0000244|PDB:3HRQ}.
TURN 1336 1338 {ECO:0000244|PDB:3HRQ}.
HELIX 1339 1342 {ECO:0000244|PDB:3HRQ}.
STRAND 1345 1347 {ECO:0000244|PDB:3HRQ}.
STRAND 1350 1352 {ECO:0000244|PDB:3HRQ}.
HELIX 1355 1372 {ECO:0000244|PDB:3HRQ}.
STRAND 1386 1394 {ECO:0000244|PDB:3HRQ}.
STRAND 1407 1415 {ECO:0000244|PDB:3HRQ}.
HELIX 1421 1423 {ECO:0000244|PDB:3HRQ}.
STRAND 1426 1434 {ECO:0000244|PDB:3HRQ}.
STRAND 1442 1452 {ECO:0000244|PDB:3HRQ}.
HELIX 1455 1462 {ECO:0000244|PDB:3HRQ}.
HELIX 1464 1479 {ECO:0000244|PDB:3HRQ}.
STRAND 1483 1487 {ECO:0000244|PDB:3HRQ}.
HELIX 1488 1495 {ECO:0000244|PDB:3HRQ}.
TURN 1496 1498 {ECO:0000244|PDB:3HRQ}.
HELIX 1503 1505 {ECO:0000244|PDB:3HRQ}.
STRAND 1508 1514 {ECO:0000244|PDB:3HRQ}.
HELIX 1515 1517 {ECO:0000244|PDB:3HRQ}.
STRAND 1519 1525 {ECO:0000244|PDB:3HRQ}.
HELIX 1526 1528 {ECO:0000244|PDB:3HRQ}.
HELIX 1539 1554 {ECO:0000244|PDB:3HRQ}.
TURN 1561 1563 {ECO:0000244|PDB:3HRQ}.
STRAND 1564 1576 {ECO:0000244|PDB:3HRQ}.
STRAND 1585 1591 {ECO:0000244|PDB:3HRQ}.
STRAND 1600 1609 {ECO:0000244|PDB:3HRQ}.
STRAND 1612 1626 {ECO:0000244|PDB:3HRQ}.
HELIX 1627 1635 {ECO:0000244|PDB:3HRQ}.
HELIX 1712 1726 {ECO:0000244|PDB:2KR5}.
HELIX 1730 1732 {ECO:0000244|PDB:2KR5}.
HELIX 1739 1742 {ECO:0000244|PDB:2KR5}.
HELIX 1746 1758 {ECO:0000244|PDB:2KR5}.
TURN 1770 1772 {ECO:0000244|PDB:2KR5}.
HELIX 1777 1785 {ECO:0000244|PDB:2KR5}.
STRAND 1853 1859 {ECO:0000244|PDB:3ILS}.
TURN 1861 1863 {ECO:0000244|PDB:3ILS}.
STRAND 1864 1871 {ECO:0000244|PDB:3ILS}.
HELIX 1878 1881 {ECO:0000244|PDB:3ILS}.
STRAND 1888 1897 {ECO:0000244|PDB:3ILS}.
TURN 1899 1902 {ECO:0000244|PDB:3ILS}.
HELIX 1904 1906 {ECO:0000244|PDB:3ILS}.
HELIX 1911 1925 {ECO:0000244|PDB:3ILS}.
STRAND 1931 1936 {ECO:0000244|PDB:3ILS}.
HELIX 1938 1952 {ECO:0000244|PDB:3ILS}.
STRAND 1957 1964 {ECO:0000244|PDB:3ILS}.
HELIX 1976 1984 {ECO:0000244|PDB:3ILS}.
TURN 1985 1990 {ECO:0000244|PDB:3ILS}.
STRAND 1991 1994 {ECO:0000244|PDB:3ILS}.
STRAND 1996 1998 {ECO:0000244|PDB:3ILS}.
HELIX 2006 2016 {ECO:0000244|PDB:3ILS}.
TURN 2017 2019 {ECO:0000244|PDB:3ILS}.
STRAND 2032 2040 {ECO:0000244|PDB:3ILS}.
TURN 2045 2047 {ECO:0000244|PDB:3ILS}.
TURN 2056 2058 {ECO:0000244|PDB:3ILS}.
HELIX 2069 2072 {ECO:0000244|PDB:3ILS}.
STRAND 2078 2087 {ECO:0000244|PDB:3ILS}.
HELIX 2090 2092 {ECO:0000244|PDB:3ILS}.
TURN 2094 2097 {ECO:0000244|PDB:3ILS}.
HELIX 2098 2107 {ECO:0000244|PDB:3ILS}.
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


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