ID   NTNJ_NECSZ              Reviewed;         420 AA.
AC   A0A455LLW9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=FAD-dependent monooxygenase ntnJ {ECO:0000303|PubMed:29797385};
DE            EC=1.-.-.- {ECO:0000305|PubMed:29797385};
DE   AltName: Full=Nectripenoid biosynthesis cluster protein J {ECO:0000303|PubMed:29797385};
GN   Name=ntnJ {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], 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: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the meroterpenoids nectripenoids A and B,
CC       as well as cochliquninone D and isocochliquninone E (PubMed:29797385).
CC       The pathway probably begins with the HR-PKS ntnH that catalyzes two
CC       chain-extension steps to form a reduced triketide, which then primes
CC       the SAT domain in the NR-PKS ntnG to initiate three more cycles of
CC       extension to give a linear hexaketide corresponding to the polyketide
CC       part of nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ
CC       then performs an oxidative decarboxylation at C11 of the ntnH/ntnG
CC       product, via an electrophilic aromatic hydroxylation with concomitant
CC       ipso-decarboxylation (Probable). The membrane-bound polyprenyl
CC       transferase ntnF then introduces a farnesyl group before the FAD-
CC       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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A6T923};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:29797385}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MH183004; AYO60871.1; -; mRNA.
DR   AlphaFoldDB; A0A455LLW9; -.
DR   SMR; A0A455LLW9; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..420
FT                   /note="FAD-dependent monooxygenase ntnJ"
FT                   /id="PRO_0000452555"
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         41..42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         231..233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         312..316
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   420 AA;  46020 MW;  41A801A68D0110A4 CRC64;
     MSNKHSACQV QFRVIVVGAG IGGLSAAVAL ANRGHSVLVL ESTTKLSHVG AGVALPPTTR
     KWYESEGVLR AESGCIPLDG IELRKWDTGE LVTRTAANPI GKQNAIHHGD MQQALLARAA
     QLDNISIRLG ARVMDIDIDS NTVLLHNGEQ VEGDVIIAAD GVKSVIKPKI CPPGASKAQS
     TGEAAYRFTL ARDLLKDDEE LLDLVQRSWA TRWDGPSRHV VAYPVRNHQL LNVVLIHPDD
     GNTEESWTTV ADKQDVIEHY QDWNLTLNKL IHLAPTQVPN FRMFLYPPSP VWVKGSTILL
     GDACHAMLPY LGQGVGQAAD DAVAIATVLS TIEHREQLPL ALQAYEVSRK SRVEQIQAAT
     YQAREHLHLK DREAQAARDL QRKSASESNQ NSDVVKMQHS YWVWDAAKVA QIALTELITG