NTNG_NECSZ
ID NTNG_NECSZ Reviewed; 1985 AA.
AC A0A455LXK0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Non-reducing polyketide synthase ntnG {ECO:0000303|PubMed:29797385};
DE Short=NR-PKS ntnG {ECO:0000303|PubMed:29797385};
DE EC=2.3.1.- {ECO:0000305|PubMed:29797385};
DE AltName: Full=Nectripenoid biosynthesis cluster protein G {ECO:0000303|PubMed:29797385};
GN Name=ntnG {ECO:0000303|PubMed:29797385};
OS Nectria sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Nectria.
OX NCBI_TaxID=1755444;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, FUNCTION, AND PATHWAY.
RC STRAIN=Z14-w;
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 nectripenoids A
CC and B, as well as cochliquninone D and isocochliquninone E
CC (PubMed:29797385). The pathway probably begins with the HR-PKS ntnH
CC that catalyzes two chain-extension steps to form a reduced triketide,
CC which then primes the SAT domain in the NR-PKS ntnG to initiate three
CC more cycles of extension to give a linear hexaketide corresponding to
CC the polyketide part of nectripenoids (Probable). The FAD-dependent
CC monooxygenase ntnJ then performs an oxidative decarboxylation at C11 of
CC the ntnH/ntnG product, via an electrophilic aromatic hydroxylation with
CC concomitant ipso-decarboxylation (Probable). The membrane-bound
CC polyprenyl transferase ntnF then introduces a farnesyl group before the
CC FAD-dependent monooxygenase ntnK functions as the first epoxidase on
CC terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8'
CC catalyzed by ntnA (Probable). The terpene cyclase/mutase ntnI then
CC initiates the sequential tricyclic ring formation through protonation
CC of the terminal epoxide and catalyzes the regioselective and
CC stereoselective 6/6/6-tricyclic ring formation (Probable). The
CC cytochrome P450 monooxygenase ntnM may then hydroxylate C1' (Probable).
CC {ECO:0000269|PubMed:29797385, ECO:0000305|PubMed:29797385}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|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}.
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DR EMBL; MH183000; AYO60867.1; -; mRNA.
DR AlphaFoldDB; A0A455LXK0; -.
DR SMR; A0A455LXK0; -.
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; 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 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 2: Evidence at transcript level;
KW Acyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Transferase.
FT CHAIN 1..1985
FT /note="Non-reducing polyketide synthase ntnG"
FT /id="PRO_0000452557"
FT DOMAIN 1622..1699
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29797385"
FT REGION 7..243
FT /note="N-terminal acylcarrier protein transacylase (SAT)
FT domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT REGION 367..795
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT REGION 889..1148
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT REGION 1265..1566
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT REGION 1578..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1719..1913
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29797385"
FT COMPBIAS 1580..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 536
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 980
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1659
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1985 AA; 216909 MW; 410B9504047FF3E4 CRC64;
MAAHNILLFG DQADAPIPMI RRIVEKSRYS KNLEYFLQSA VDNVQLEVAK LTPAERETVG
SFQSVQDLIT ALTSKSDRHG IAQMVLVFIA RIGELILHAE SNPTLLSSST PLLSLGICGG
LLPAAAAAVA TNVGELVEVA SYMAGVNCRV AAMISRRSLQ IEDNAGSWAF SVLGKLVMQL
PTILDGFHNE QSIPRHRRAY IAISTPTWAT VFGPPSVLKK LLETSAALSK SDITILPAFG
AVHAGHLAAP EFEELVDESP LLNKSIKSGY KLLSGSKYAP FAGSSLRDLL PQIMLDIFQN
STNPSRLFEV GGSYLQKGKE LSLYMLGATS YLVLLRRSLH AQGFDVALKT NAPILQASEL
RGGSGSVAII GMSGQFPGAS SVDEMWELLM QREELHKKIP SDRFNADDYL DETGRGFNAI
TTAYGCFLEH PGLFDHKMFN VSPREAMQMD PGQRLVMHAV YEALEDAGVA NNGSVATDSK
RIGTYIGDGS DDWRELQQPH GVDKYILQGT QRSFTPGRLN HHFKWEGATF CVDSACGSTA
SAVGLAYRAL VNRDCDTAIA GGSNIIATPF WQSALSKGGF LSTTGGCKTF RGDADGYCRG
EAIGVIVLKR LEDALYDNDN IISVIRSYAR NHSADTVSIT RPHVPAQERV YRRVLQKAGL
EPNDISYVEM HGTGTTAGDS AELESVVNIL AQKGERETPL VVGAIKANLG HSEAASGISS
IMKAAIMFRK GVIPPQVGIP QKLGNFECLE RGSVLIPGNP IPYTRQSIGK KRTMIVNNFD
AAGGNSCFVL EEPPVPQIKA PDPRPYHVVT VSAHCPQSLE RNEQLLRQFL LDNADISLAD
LAYTTTARRM HHSMRSAYSG NSIKAIVDGI NRVLSKKKEA PTARKPPVVF AFTGQGAHYA
GMGADLFRSS QAFRATITSL QRICESHGFP PFVQLISKSE SPVEKATTVQ IHLALIALEI
ALADLWKTWG IAPDLVIGHS IGEYAALYAA GVLSATDAMY IVGRRATLIQ ENCKEGTHGM
LSISGTSDDV AAILSDERIM SSCEVACRNS PGMIVLSGEH EELLQIEGLL KDQQIKCRLL
DVPYAMHSHQ MDGIVEGLRE AAQGVLFGTP RVKVISTLLG VEHTKFDSDY LVRHTRQAVN
FEQAISHCTS HGLVDKTSLW LEIGPNPVSL GLIRSNTNVT SDRALHSLKN GDDNWKSISA
TLASFYKAGM SIQWREYHRD FANNLSLITL PKYAFDTRDF WMKYTEGQRH SEVQPISTCL
HRLVKQEDTA KEQHATFTAE IGHPSLLKII KGHKLSGITV CPAGVFSEMS LTAARYLLTN
GSSKASFPSL SVLDTQIDHP IMPKADSKQT VQVEINRSKQ SNEFFVSIAD QAKPSVINSK
CVVRLRDEHA FDLERRQMLE VIQPKIAKLT KAAAGGRANR FQGKLFYRLF ANLMDYTGQY
EGVQEAIVSS DFTEALATVQ LPKAQSSGES WTLSPYWIDA LTHLAGFLFN GNPMNSGDYV
FIGIHMERME IVAKDLSTDV TYQCYAFIEQ SEGSDIYRGH VYILDGDLIV GFLEGARFRK
MPRTTLHRIL GKAEPVKNTK QVPHPTTNGS AIANGVNRNP SHNEPSTPPV ANGVNGTNGD
QSDRKSLYSV LVQQLIEETG MEESELTPST FFVEIGVDSL MSISILAALK AETGTELNAS
FLMDYPTLED AQRELRRLEG KDSVNSNDQS TMVNGKEKTR ECNVVLMQGP SSSTSRKPVF
LIADGAGSAA AYIHFPKLGQ DLPVYAVESP WVNDPENFVC SFDEAAAMYL AAIRSKQPHG
PYILGGWSAG GVFAYEVARL LLEAGERVLG LIIIDITGPR HEDRSKVESP TMEIIDQIGM
LSGIERNFDD TTTQSRRLKQ HMLSTVTCFS KMDPTPMSPG RHPDCTFVIW AKKDILPKAA
LDTLPAGLNA WFYPSSHDLG PNGWDALVGN KMEYFQIEGD HFSIMTAPEV TQLGKIIQEA
IGKIS
