ATR6_STAC4
ID ATR6_STAC4 Reviewed; 2435 AA.
AC A0A084R1H6;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Highly reducing polyketide synthase ATR6 {ECO:0000303|PubMed:25015739};
DE EC=2.3.1.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Core atranone cluster (CAC) protein 6 {ECO:0000303|PubMed:25015739};
GN Name=ATR6 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03331;
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP FUNCTION.
RC STRAIN=IBT 40285;
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the core
CC atranone cluster (CAC) which products are predicted to catalyze most or
CC all steps of mycotoxin atranone synthesis, starting from geranylgeranyl
CC pyrophosphate (GGPP) (PubMed:25015739). The initial cyclization of GGPP
CC to dolabellane is probably performed by the terpene cyclase ATR13
CC (PubMed:25015739). The Baeyer-Villiger oxidation near the end of the
CC atranone synthesis, which converts atranones D and E to atranones F and
CC G is predicted to be catalyzed by the monooxygenase ATR8
CC (PubMed:25015739). Of the CAC's other predicted gene products, the
CC reducing PKS ATR6 might synthesize a polyketide chain
CC (PubMed:25015739). This polyketide is probably transferred onto the
CC atranone backbone by the polyketide transferase ATR5 (By similarity).
CC Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4,
CC and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a
CC methyltransferase (ATR12) (PubMed:25015739). These may all be involved
CC in the various steps of atranone biosynthesis, although their specific
CC roles must await experimental determination (PubMed:25015739).
CC {ECO:0000250|UniProtKB:Q4WAY4, ECO:0000305|PubMed:25015739}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25015739}.
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DR EMBL; KL659308; KFA70061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084R1H6; -.
DR SMR; A0A084R1H6; -.
DR EnsemblFungi; KFA70061; KFA70061; S40285_03331.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; MFIEDID; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
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; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF08659; KR; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..2435
FT /note="Highly reducing polyketide synthase ATR6"
FT /id="PRO_0000442400"
FT DOMAIN 2353..2429
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 21..453
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 586..883
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 979..1291
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1724..2037
FT /note="Enoylreductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2062..2301
FT /note="Catalytic ketoreductase (KRc) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 192
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT ACT_SITE 682
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT ACT_SITE 1011
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT MOD_RES 2389
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2435 AA; 263256 MW; B5250B5AB0363780 CRC64;
MDSEAPTPTS SSFALPYAEP IAIVSAACRL PGHIQNPHQL WQFLQAGGIA TSDVVPESRY
NVAGHFDGSG RPGTLKTPGG MFIEDIDLGA FDAPFFHIGK SDAVSMDPQQ RQLLEVVYEC
LENGGITMQG IDGDQIGCFV ASYSADWHEM QSRHPASRAP GTTAGTSRAI LSNRISHFFN
IKGSSWTIDT ACSGGLVGVD AACQYLRAGK LNGAIVAAAQ LWMSPEYNEE LGTMRAAASS
TGRCHSFDAK ADGYCRSEAV NAVYLKRLSD ALRDGDPVRA VIRGTANNSD GRTPGLHSPN
SDAQAAAIRA AYADAGIDST QYTKTAFMEC HATGTPAGDP SEVRGSASVL ASMRPPSDPL
IIGTIKSNLG HAEPGAGISG LMKAMMAVEK GIIPGNPTFI TPNPNIDFAG LRVRASQRNM
RWPQSTKDYR RASVASSGFG GSNAHVVLDN AEHYMQHHFL SVQPQFRTYV SSYAETGDVL
SMLSGFGLGA ANSSDKLAPL PNVLVFSAHD ADSLKRQMGA LSAHLVDPRV AIKLSDLSYT
LSERRSRHFH RSFIVCRPNK GGNIETLPTD LAKYAMKPTS PVRIGFVFTG QGAQWSGMGA
DLIRLFPKTA KAVVDELDAA LQELPADVRP SWSLLAELTE PRSSEHLREP EFSQPLVTAL
QLALLAVLKS WNVTADAVVG HSSGEIAAAC SAGLLTPGQA ILTAYFRGQA AKQVVMEGSM
GMLAVGLGSA GVQKYLEDTS RAGKVVIACY NSPASVTLSG PTSLLSELAQ VIQTDGHFAR
LLQVNLPYHS HYMSAIGDRY EKLLLDHGRL DEIQGETATR KIPMISSVST IVLEGSKSCS
AAYWKSNMVS AVQFDGACKR IVADQDLSAN LLIEIGPSAA LGGPIGQIIK QAGIDNVTYT
SAAQRGTDSI LALFGVAGQL FLHDCPVSLD HVNTDETALT EPKPAVIIDL PNYRWNHSTR
YWHESLASKD WRFRNFPEHD LLGGKVLGTA WESPSWTKTL RLEDVPWLRD HKIGSEILFP
ASGYIAMAVE AARQATISTA RSQNKAAPSA HAYHYVLRDV HFERGLVLED ETDTTLMLSL
APVARLGVKW WVFKVMSLAS GGSSSSSDSW IEHSNGLVRL ALNASEPLPR VTPDNYSLPL
QYPTPARFWY KAFENAGYGY GPGFQKQSYI ECTEGSFSAR STIMLNPPLS KWEPQPNYPL
HPASMESCIQ ATLTSMYRGD RAGINNVLVP NAIDRIILSG DTWRSNEAVS VTTSESSSGI
TSKPLSNASL FDPTNGVLII DLRGISMTSV GLQGNVCSFS TYTRVEWKPD ICHLDSDTKI
RRAILDLTDG TGDFVQEVLD LAAHKKPNMR VLEVDLTGGQ PRSLWLSGNE TSRITRAATS
EFNYASDRPE SVLSAQDLYS DMSSGYTSRF TLLPITSQSF VAPPELCRSD LVLIRTSQLP
SMETASILTR NARCLLTEGG TIVLHVLDVS KYSKVGQESL REALSRGKFS KIRQAADGLF
VAEATDADTA YSQGKSLVVL HFSTSPVFSW SSAVITSLID KGWPITELTL EEGCRLTELP
AKATILVMDE VNRPLFASME EYQLEAIQSI VQRDCSLLWV TQGSQMHVSS PLKAICHGVF
RSVRSMDPNA RIVTLDVDSA AEDQLAKMAD ILHTVLLQVR VTPESLPADF EFVERGGLLY
ISRLRPAQVD NESRSDGDKD GLQPVPVDLH STESTIGLVS GRPGILDTLH FAELGPGRLL
VLGPEDIEVE IFAASVDDGD YALAKNLDPE DSTRLGYGGA GIVTRTGDSI TDIRAGQRVA
LFHGGCVANR IVVARQVVFS VPDTMTFEDA ATLPTAFVPA IYSIYHLAQL RQGQRVLIHS
AANAVGIACV QLCQGLSCKP YVTVDSDEER KFLAEEVGVS SDHILLLNSE NFAREMQDSA
QNHGFDVIIN TSQHHLPDQG WGVVSPGGVH VALGQTINDR SLLPMDYFTN NRSFCSLDIR
TLPLDKLASP RACSQLSDLI YGSSIKHMLP KAVFPCHGVQ AALQSCHDHN RLRNVVISTG
PDKDVRILVK PEKQQPRCTF APEQTYLLVG KLKGVSGSLA LHLARCGAKY LVIMSPKNSE
NSENISRSIR AMGCSLRFFE GDAASIDDMR RCYGQISGPI GGIVHGAAAQ SFRLMSHETY
QATLARSVLS AWNLHTVSLE RDDSVPFFIM LSSTAGVVGD EKQPHHAGSD VFHNALATYR
CGLGLPSTSI NLGPINDDAL LPDSEKTFKT LSSGVWFGVN EAVFRRIIDH SLSREHHGAQ
RHFELASQAQ IITGIAVPQP GSSDILHDVR LLGLKLAQSG NSSSAASGRD DSQNREMQTF
LLCARSTNPD PAVLLSSAVG VLQAQFTKML RLNELMDPAY PLNTYGMDSL AAAEPRSWVR
TAFGVQLTTL DVVNAASLVV LCQKIISRMG LGKEV
