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Non-reducing polyketide synthase aptA (NRPKS) (EC 2.3.1.-) (Asperthecin synthesis protein A)

 APTA_EMENI              Reviewed;        1792 AA.
Q5B0D0; C8V346;
11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
28-FEB-2018, entry version 98.
RecName: Full=Non-reducing polyketide synthase aptA {ECO:0000305};
Short=NRPKS {ECO:0000303|PubMed:20479000};
EC=2.3.1.- {ECO:0000269|PubMed:20479000, ECO:0000269|PubMed:21866960, ECO:0000305|PubMed:18978088};
AltName: Full=Asperthecin synthesis protein A {ECO:0000303|PubMed:18978088};
Name=aptA {ECO:0000303|PubMed:18978088}; ORFNames=AN6000.2;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[2]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[3]
FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND CATALYTIC ACTIVITY.
PubMed=18978088; DOI=10.1128/AEM.01743-08;
Szewczyk E., Chiang Y.M., Oakley C.E., Davidson A.D., Wang C.C.,
Oakley B.R.;
"Identification and characterization of the asperthecin gene cluster
of Aspergillus nidulans.";
Appl. Environ. Microbiol. 74:7607-7612(2008).
[4]
FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
PubMed=20479000; DOI=10.1074/jbc.M110.128504;
Li Y., Image I.I., Xu W., Image I., Tang Y., Image I.;
"Classification, prediction, and verification of the regioselectivity
of fungal polyketide synthase product template domains.";
J. Biol. Chem. 285:22764-22773(2010).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21866960; DOI=10.1021/ja206906d;
Li Y., Chooi Y.H., Sheng Y., Valentine J.S., Tang Y.;
"Comparative characterization of fungal anthracenone and
naphthacenedione biosynthetic pathways reveals an alpha-hydroxylation-
dependent Claisen-like cyclization catalyzed by a dimanganese
thioesterase.";
J. Am. Chem. Soc. 133:15773-15785(2011).
[6]
INDUCTION.
PubMed=26773375; DOI=10.1016/j.fgb.2016.01.004;
Bayram O., Feussner K., Dumkow M., Herrfurth C., Feussner I.,
Braus G.H.;
"Changes of global gene expression and secondary metabolite
accumulation during light-dependent Aspergillus nidulans
development.";
Fungal Genet. Biol. 87:30-53(2016).
-!- FUNCTION: Non-reducing polyketide synthase (NRPKS); part of the
gene cluster that mediates the biosynthesis of asperthecin, an
anthraquinone pigment (PubMed:18978088, PubMed:21866960).
Catalyzes the formation of the aromatic polyketide from acetyl
coenzyme A and seven malonyl coenzyme A molecules
(PubMed:18978088, PubMed:21866960). Through its product template
(PT) domain, catalyzes the cyclization of the polyketide backbone
via C6-C11 aldolcondensation (PubMed:20479000). Polyketide is
subsequently hydrolyzed from the NRPKS by the action of the
hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088).
Endocrocin-9-anthrone is then oxidized into endocrocin by aptC
(PubMed:18978088). Endocrocin is likely to decarboxylate
spontaneously to form emodin which explains why there is no
decarboxylase in the asperthecin biosynthesis cluster
(PubMed:18978088). Finally, aptC or another endogenous oxygenase
catalyzes additional oxidation steps to form asperthecin
(PubMed:18978088). {ECO:0000269|PubMed:18978088,
ECO:0000269|PubMed:20479000, ECO:0000269|PubMed:21866960}.
-!- COFACTOR:
Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:21866960, ECO:0000305|PubMed:18978088}.
-!- INDUCTION: Expression is induced during late sexual development in
the dark (PubMed:26773375). {ECO:0000269|PubMed:26773375}.
-!- DOMAIN: Multidomain protein; including a starter unit:ACP
transacylase (SAT) that selects the starter unit; a ketosynthase
(KS) that catalyzes repeated decarboxylative condensation to
elongate the polyketide backbone; a malonyl-CoA:ACP transacylase
(MAT) that selects and transfers the extender unit malonyl-CoA; a
product template (PT) domain that controls the immediate
cyclization regioselectivity of the reactive polyketide backbone;
and an acyl-carrier protein (ACP) that serves as the tether of the
growing and completed polyketide via its phosphopantetheinyl arm
(PubMed:18978088, PubMed:20479000). {ECO:0000269|PubMed:20479000,
ECO:0000305|PubMed:18978088}.
-!- DISRUPTION PHENOTYPE: Fails to produce asperthecin
(PubMed:18978088). {ECO:0000269|PubMed:18978088}.
-----------------------------------------------------------------------
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EMBL; BN001301; CBF70387.1; -; Genomic_DNA.
EMBL; AACD01000102; EAA57749.1; -; Genomic_DNA.
RefSeq; XP_663604.1; XM_658512.1.
ProteinModelPortal; Q5B0D0; -.
SMR; Q5B0D0; -.
STRING; 162425.CADANIAP00007018; -.
EnsemblFungi; CADANIAT00007018; CADANIAP00007018; CADANIAG00007018.
EnsemblFungi; EAA57749; EAA57749; AN6000.2.
GeneID; 2871043; -.
KEGG; ani:AN6000.2; -.
HOGENOM; HOG000168774; -.
KO; K15317; -.
OMA; YAEMALV; -.
OrthoDB; EOG092C01G3; -.
Proteomes; UP000000560; Chromosome I.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
GO; GO:0036184; P:asperthecin biosynthetic process; IMP:AspGD.
GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.40.366.10; -; 1.
Gene3D; 3.40.47.10; -; 1.
InterPro; IPR001227; Ac_transferase_dom_sf.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR018201; Ketoacyl_synth_AS.
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; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR030918; PT_fungal_PKS.
InterPro; IPR032088; SAT.
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; PF16073; SAT; 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; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1792 Non-reducing polyketide synthase aptA.
/FTId=PRO_0000436108.
DOMAIN 1715 1792 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 1 395 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255}.
REGION 391 766 Ketosynthase (KS) domain. {ECO:0000255}.
REGION 926 1243 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255}.
REGION 1308 1625 Product template (PT) domain.
{ECO:0000255,
ECO:0000269|PubMed:20479000}.
ACT_SITE 564 564 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 1752 1752 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 1792 AA; 195194 MW; F0B4BFD61DF046C2 CRC64;
MKDNTHSTTL IFFGNEFPND DLKGLFRCLL RLSKDRRFRQ LAAFLEESTL VLKKEVAALP
QPLRDLVPHF HTVLPLAELG DFRQGPLGAA MESALLTVLE LGMFIGHYEA EGRDWNLLEH
NTTLAGLSIG LLAAAGVALS TNLAEVAQNG AECVRVSFRL GVYVSEISRK LEAPQADGTL
LSWAHVVTGE TKSAIQDELS KYNSESGTPE LLKVFISAAD KTSVSVSGPP SRMKACFSSS
HLLRYSKSFA LPVYDGLCHA SHLYNEDSIN TVINSAESVI PVSRPVQLSL HSSNTGQPFP
AATAHELFQA IGKELLTGTI YLDNIIDGII KRIEGFNPSD LQVETFRTSI VFKSVRAALE
GEFPDLEIKI TDLIPWAFRD YGPRLPRSFA HSKLAVVGMA CRMPGGGNDT ELFWEILEQG
RDVHTTVPAD RFDLSTHYDP SGKTDNAATT PYGNFVDKPG LFDAGFFNMS PKEAEQTDPM
QRLALVTAYE ALEMAGVVPG RTASSNPKRI GTYYGQASDD WRELNASQNI GTYAVTGGVR
AFGNGRINYY FKFPGPSFNV DTACSSGLAA VQVACSALWA GEADTVLAGG LNIITDPDNY
AGLGCGHFLS KTGQCKVWDE TADGYCRADG IGSVVIKRLE DAEADNDNII AVVLSAATNH
SAEAISITHP HAGNQKDNYR QVIDMAAVNP LDVSYIELHG TGTQAGDAVE SESVLDVFAP
RSPPRRPDQL LQLGAVKSNI GHGEAAAGIA SFLKVLLMYQ KNMIPAHIGI HTVINPTIPK
DLEQRRVRLT QTNTPWPRLP GKKRIAMVNS FGAHGGNTTV LLEDAPERNK DVARENRSTH
TVVISAKSKK SLQANIANLA LHLEENPDID LGDLSYTTCA RRIHYTLRVG FAVSSIAGLK
EALRKAGEKE ALAEVRPTPG DVPPVVFAFT GQGAFYQGIA RELFESFSYF RDEVLQLDHI
VQRLGFQSIV PVIDGSIGEN PSATVSQLSI VVIEIALAHL WTLLLGMQPS AVIGHSLGEY
AALVVAGVLS TADGIFLAGR RAQLIEKCCT AGSHAMLSVR ASVSEISKLL GNAKYEISCQ
NTLNDTVIGG TKANLDAARQ VLESSSIKCV PVDVPFAFHT EQVDPVLDQL TRVAETVHFK
APSIPIISPL LRSVVFDGKT INSSYLIRAT REPVHFAGAI EAAQDLGMVN DKTVWVDVGP
HPICASFVRS LIPKARVASS CRRNEDNYAT MAKNLVALHL AGCTPVWDEY FRANEKAYNL
LTLPKYAWND VNYWIQYIGT WTLDKAHLKY TGTNGPPQVK PSSSALRTSL IHEIIEETIG
EETATLKTVS DLQHPEFLEA VHGHRMNNCG VATSSIWTDM SLTVGEYLYN KLAPGSKVHM
NVGELEVLHA TVANPAKNCT QNLYLDAHLD LRTQKMSLAW FNVDPATGSK AAESYATGSV
RFEADAEKWK SEWERLTHLV LGRIETLESM AKDGQASQLS KALSYALFKN VVDYADHYRG
MERVVMHDYE AFCDIKLTPE RRGMFHTPPH WIDSVSHLAG LIMNGSDASN TRDYFFVTPG
YESFRLLAKL DPDVKYQSYV RMFPLPEANM YGGDLYILQD NQIIGMVGHF KFRRVPRLLM
DRFFSAEAAS KQSVAASASS APKTATKHAP LPASKPAQAP AEPTPSSLPT VQAQNTSPPQ
QVTPSKPAMN GVKTPEEEKP GKADAEGPNG TTSQPEATGV VGQCLQLIAN ETGQSVNELT
PDATFVQLGV DSLMSLVLSE KFRAELGLEV KSSLFLECPT VGDMMDWLEQ YC


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