APTA_EMENI
ID APTA_EMENI Reviewed; 1792 AA.
AC Q5B0D0; C8V346;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Non-reducing polyketide synthase aptA {ECO:0000305};
DE Short=NRPKS {ECO:0000303|PubMed:20479000};
DE EC=2.3.1.- {ECO:0000269|PubMed:20479000, ECO:0000269|PubMed:21866960, ECO:0000305|PubMed:18978088};
DE AltName: Full=Asperthecin synthesis protein A {ECO:0000303|PubMed:18978088};
GN Name=aptA {ECO:0000303|PubMed:18978088}; ORFNames=AN6000.2;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=18978088; DOI=10.1128/aem.01743-08;
RA Szewczyk E., Chiang Y.M., Oakley C.E., Davidson A.D., Wang C.C.,
RA Oakley B.R.;
RT "Identification and characterization of the asperthecin gene cluster of
RT Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 74:7607-7612(2008).
RN [4]
RP FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=20479000; DOI=10.1074/jbc.m110.128504;
RA Li Y., Image I.I., Xu W., Image I., Tang Y., Image I.;
RT "Classification, prediction, and verification of the regioselectivity of
RT fungal polyketide synthase product template domains.";
RL J. Biol. Chem. 285:22764-22773(2010).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21866960; DOI=10.1021/ja206906d;
RA Li Y., Chooi Y.H., Sheng Y., Valentine J.S., Tang Y.;
RT "Comparative characterization of fungal anthracenone and naphthacenedione
RT biosynthetic pathways reveals an alpha-hydroxylation-dependent Claisen-like
RT cyclization catalyzed by a dimanganese thioesterase.";
RL J. Am. Chem. Soc. 133:15773-15785(2011).
RN [6]
RP INDUCTION.
RX PubMed=26773375; DOI=10.1016/j.fgb.2016.01.004;
RA Bayram O., Feussner K., Dumkow M., Herrfurth C., Feussner I., Braus G.H.;
RT "Changes of global gene expression and secondary metabolite accumulation
RT during light-dependent Aspergillus nidulans development.";
RL Fungal Genet. Biol. 87:30-53(2016).
CC -!- FUNCTION: Non-reducing polyketide synthase (NRPKS); part of the gene
CC cluster that mediates the biosynthesis of asperthecin, an anthraquinone
CC pigment (PubMed:18978088, PubMed:21866960). Catalyzes the formation of
CC the aromatic polyketide from acetyl coenzyme A and seven malonyl
CC coenzyme A molecules (PubMed:18978088, PubMed:21866960). Through its
CC product template (PT) domain, catalyzes the cyclization of the
CC polyketide backbone via C6-C11 aldolcondensation (PubMed:20479000).
CC Polyketide is subsequently hydrolyzed from the NRPKS by the action of
CC the hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088).
CC Endocrocin-9-anthrone is then oxidized into endocrocin by aptC
CC (PubMed:18978088). Endocrocin is likely to decarboxylate spontaneously
CC to form emodin which explains why there is no decarboxylase in the
CC asperthecin biosynthesis cluster (PubMed:18978088). Finally, aptC or
CC another endogenous oxygenase catalyzes additional oxidation steps to
CC form asperthecin (PubMed:18978088). {ECO:0000269|PubMed:18978088,
CC ECO:0000269|PubMed:20479000, ECO:0000269|PubMed:21866960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 8 H(+) + holo-[ACP] + 8 malonyl-CoA = 3,6,8,9-
CC tetrahydroxy-1-oxo-3-(2-oxopropyl)-1,2,3,4-tetrahydroanthracene-2-
CC carboxyl-[ACP] + 8 CO2 + 9 CoA + 2 H2O; Xref=Rhea:RHEA:64072,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16516, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:149685; Evidence={ECO:0000269|PubMed:20479000,
CC ECO:0000269|PubMed:21866960, ECO:0000305|PubMed:18978088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64073;
CC Evidence={ECO:0000269|PubMed:20479000, ECO:0000269|PubMed:21866960,
CC ECO:0000305|PubMed:18978088};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:21866960, ECO:0000305|PubMed:18978088}.
CC -!- INDUCTION: Expression is induced during late sexual development in the
CC dark (PubMed:26773375). {ECO:0000269|PubMed:26773375}.
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 (PubMed:18978088, PubMed:20479000).
CC {ECO:0000269|PubMed:20479000, ECO:0000305|PubMed:18978088}.
CC -!- DISRUPTION PHENOTYPE: Fails to produce asperthecin (PubMed:18978088).
CC {ECO:0000269|PubMed:18978088}.
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DR EMBL; BN001301; CBF70387.1; -; Genomic_DNA.
DR EMBL; AACD01000102; EAA57749.1; -; Genomic_DNA.
DR RefSeq; XP_663604.1; XM_658512.1.
DR AlphaFoldDB; Q5B0D0; -.
DR SMR; Q5B0D0; -.
DR STRING; 162425.CADANIAP00007018; -.
DR EnsemblFungi; CBF70387; CBF70387; ANIA_06000.
DR EnsemblFungi; EAA57749; EAA57749; AN6000.2.
DR GeneID; 2871043; -.
DR KEGG; ani:AN6000.2; -.
DR VEuPathDB; FungiDB:AN6000; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_1_1; -.
DR InParanoid; Q5B0D0; -.
DR OMA; LNTHYDP; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0036184; P:asperthecin biosynthetic process; IMP:AspGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA: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 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; 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; PF16073; SAT; 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; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..1792
FT /note="Non-reducing polyketide synthase aptA"
FT /id="PRO_0000436108"
FT DOMAIN 1715..1792
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..395
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 391..766
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 926..1243
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1308..1625
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:20479000"
FT REGION 1634..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1752
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ 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
