ID   ATNG_ARTSZ              Reviewed;        1996 AA.
AC   A0A455M7S4;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Non-reducing polyketide synthase atnG {ECO:0000303|PubMed:29797385};
DE            Short=NR-PKS atnG {ECO:0000303|PubMed:29797385};
DE            EC=2.3.1.- {ECO:0000269|PubMed:29797385};
DE   AltName: Full=Arthripenoid biosynthesis cluster protein G {ECO:0000303|PubMed:29797385};
GN   Name=atnG {ECO:0000303|PubMed:29797385};
OS   Arthrinium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Apiosporaceae; Arthrinium;
OC   unclassified Arthrinium.
OX   NCBI_TaxID=1756131;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, FUNCTION, CATALYTIC ACTIVITY,
RP   DISRUPTION PHENOTYPE, AND PATHWAY.
RC   STRAIN=NF2194;
RX   PubMed=29797385; DOI=10.1002/anie.201804317;
RA   Zhang X., Wang T.T., Xu Q.L., Xiong Y., Zhang L., Han H., Xu K., Guo W.J.,
RA   Xu Q., Tan R.X., Ge H.M.;
RT   "Genome mining and comparative biosynthesis of meroterpenoids from two
RT   phylogenetically distinct fungi.";
RL   Angew. Chem. Int. Ed. 57:8184-8188(2018).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of the meroterpenoids arthripenoids
CC       (PubMed:29797385). The pathway begins with the HR-PKS atnH that
CC       catalyzes two chain-extension steps to form a reduced triketide, which
CC       then primes the SAT domain in the NR-PKS atnG to initiate three more
CC       cycles of extension to give a linear hexaketide corresponding to the
CC       polyketide part of arthripenoids (PubMed:29797385). The FAD-dependent
CC       monooxygenase atnJ then performs an oxidative decarboxylation at C11 of
CC       the atnH/atnG product, via an electrophilic aromatic hydroxylation with
CC       concomitant ipso-decarboxylation (PubMed:29797385). The membrane-bound
CC       polyprenyl transferase atnF then introduces a farnesyl group before the
CC       FAD-dependent monooxygenase atnK functions as the first epoxidase on
CC       terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8'
CC       catalyzed by atnA (PubMed:29797385). The terpene cyclase/mutase atnI
CC       then initiates the sequential tricyclic ring formation through
CC       protonation of the terminal epoxide and catalyzes the regioselective
CC       and stereoselective 6/6/6-tricyclic ring formation (PubMed:29797385).
CC       The cytochrome P450 monooxygenase atnM is responsible for hydroxylating
CC       both C1' and C10' (Probable). The next steps may involve ketoreduction
CC       and acetyl transfer by the ketoreductase atnB and the acetyltransferase
CC       atnC, and lead to the production of arthripenoid B, the final
CC       biosynthetic product of the atn cluster (PubMed:29797385). The
CC       hydroquinone moiety in arthripenoid B is prone to undergo spontaneous
CC       oxidation to afford a benzoquinone compound, a key intermediate for
CC       generating structure diversity (Probable). For instance, addition of a
CC       cysteine followed by ring contraction gives arthripenoid A,
CC       tautomerization gives the main product arthripenoid C, addition of a
CC       molecular of water or amine affords arthripenoid D or E, respectively,
CC       and loss of one water forms arthripenoid F (Probable).
CC       {ECO:0000269|PubMed:29797385, ECO:0000305|PubMed:29797385}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:29797385}.
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. {ECO:0000305|PubMed:29797385}.
CC   -!- DOMAIN: The SAT domain at the N-terminus facilitates crosstalk between
CC       the two PKSs atnH and atnG encoded by the cluster.
CC       {ECO:0000305|PubMed:29797385}.
CC   -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC       polyketide synthase is mediated by the thioesterase (TE) domain
CC       localized at the C-ter of the protein. {ECO:0000305|PubMed:29797385}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of arthripenoids.
CC       {ECO:0000269|PubMed:29797385}.
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DR   EMBL; MH183013; AYO60880.1; -; mRNA.
DR   AlphaFoldDB; A0A455M7S4; -.
DR   SMR; A0A455M7S4; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; IPR020802; PKS_thioesterase.
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; 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   SMART; SM00824; PKS_TE; 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   Acyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW   Phosphoprotein; Transferase.
FT   CHAIN           1..1996
FT                   /note="Non-reducing polyketide synthase atnG"
FT                   /id="PRO_0000452559"
FT   DOMAIN          1620..1697
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:29797385"
FT   REGION          9..245
FT                   /note="N-terminal acylcarrier protein transacylase (SAT)
FT                   domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT   REGION          369..797
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT   REGION          891..1150
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT   REGION          1267..1568
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT   REGION          1573..1621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1725..1923
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT   COMPBIAS        1589..1612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        538
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        982
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         1657
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1996 AA;  216162 MW;  44A28DA6A28ADD43 CRC64;
     MDVAAQHVFL FGDQADAPMP MVRRVVERSR HSKNLESFLQ SAIDNVQLEV ARLTPAERDT
     IGPFHSLEGL ADSLKEKSDR HGIAQMVSVF IARIGELILH AENDPALLDS STPLLSLGIC
     GGLLPAAAVA AATNIHELIE VASYLARVNC RVAVAISRRS IEIESGPGSW AFSVLGSAVA
     QLPDILEDFH REQSIPRHRR AWIAVSTPTW ATVFGPPSVL SKLRETSITL KKSDAAELPA
     FGAVHAAHLV APNFGDLVGE SPLLNRPLKT GYKLLSGSKY APYNATTLKD LLPQIMLDIF
     QNETNPARVF DVGGSYLRKG GPISLYMLGA TSYLVLLRRS LHTQKFEVNL KTNPPSLQNS
     ELRGGSGSVA VIGMSGQFPG AASVDELWDV LMRREERHRK IPIERFNADD YLDETGRGSS
     AITTAYGCFL ENPGLFDHKM FNVSPREAMQ MDPGQRLLLH GVYTALEDAG LVTGSSTAAD
     NKRISTYIGD GSDDWRDLQS QHGVDKYIVQ GTQRSFTPGR INHHFKWEGA TWLVDAACGS
     TASAVGLAYR ALINRDCDTA VAGGANIIAT PFWHSALSKG GFLSKTGGCK TFRADADGYC
     RGEAVGVVVL KRLEDALQDN DNIVSVIRGY SRNHSADTVS ITRPHVPAQM RAYQAVLHNS
     GLEPEDISYV EMHGTGTTAG DSAELESIVN VLAQKNTRET PLVVGAIKAN LGHSEAASGI
     SSLIKASLTF RKGMVPPQVG IPEKMGSFAC LDHGTVHVPG APVSFTRESV GKTRAMVMNN
     FDAAGGNSCF VLEEPPTPSL KSADPRPYHV VTVSAHCQTS LEENKRQLLQ FLTENKETSL
     ADLSYTTTAR RMHHTLRSAY TGGSIQDIIN SLGRDLGKNH GQDKPGAPRV AFAFTGQGAH
     YAGMGADLFK VSQPFRTTIT GLQKICVTHG FPQFAHLISD PSTPMENVST AQIHLSLAAL
     EIALVDLWKI LGISPDLVIG HSIGEYAALY AAGVLSATDA MYLVGTRAML LQDSLEEGVN
     GMLSISGTPQ DVAAIVSDES VMADCEVACH NSPGMVVLGG RRPRLAELEE LLRARKFKCK
     LLDVPYAMHS SQLDTILPGF RKAARGVCFG TPTIKVISTL TGTEQQHFDS EYLVRQTRES
     VKYTQAISHC LSQGLVDSAT LWLEIGPGPV CLGLIRSNTN VATNLAMPSL KKDDQNWKSI
     SSALASLYVA GKAIGWREYH SDFIDSLSLI SLPSYAFDNR NFWMPYTTGG KHQDVQPIST
     CLHHLVSQDD NGKEQSATFT AVVSQPSLLK MIQGHKLSGI TVCPAGVFAE MALTAARYVL
     TGGSFSAPVP SLSVIDIQID HPITPQSGSQ QVIQVNVRRP KQSRDFAVSI VDQAKPSLIT
     AKCCIRQTDE QDVIATRRQQ LDMIRPKISK LMQDAASGIA NRFQGKLFYK LFANLMDYGG
     QYEGVKEAIV GDDFTEALAT IRLPKAQDSN ESCTLSPYWI DALTHLVGFL LNGNPMNSGD
     DVYIGTQMER MEILAKDFSP DVVYQSYAYL EPSQDSVNYR GHVYILSGDS IVGFLEGARF
     RKMPRTTLHR ILGKAVPPKP AKETSHPSVE ATAPATTNGR SSATNAQAEA PAPPVNGSNG
     HRKTVESVLI ACLIEETGME ESEILPSTFF AEIGVDSLMS ISILSEIKNE TGVELNASFL
     MEYPTLGDAQ RQLRTLERKR EGANPSTNGT DVAVVVNGEK PAKPKRECNV VLMQGQAPED
     SSSIPLFLLA DGAGSAAAYI HLPKLGLEDD LAVYAVESPW VRDPAEFTCS FEEAAALYLA
     AVRAKQPRGP YLLGGWSGGG VFSYEVARRL LAAGERVLGL VVIDIRAPSL RPNPHAAAPT
     MDIIDQIGML SGIERTFADD ASPEAARLKR HMLSTVTCFS RLVPTPMPPH LRPERTFVVW
     AKKDVLPKAA YDQLPPGLDA WFYPASHDMG PNGWDELVGD AVEYSQVEGD HFSIMTFPEV
     TELGRVLQAA VAKCRV