ID   NTNL_NECSZ              Reviewed;         201 AA.
AC   A0A455LN84;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=NAD(P)H-dependent FMN reductase ntnL {ECO:0000303|PubMed:29797385};
DE            Short=FMN reductase ntnL {ECO:0000303|PubMed:29797385};
DE            EC=1.5.1.39 {ECO:0000305|PubMed:29797385};
DE   AltName: Full=Nectripenoid biosynthesis cluster protein L {ECO:0000303|PubMed:29797385};
GN   Name=ntnL {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: NAD(P)H-dependent FMN reductase; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.39;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.39;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:29797385}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q07923}.
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DR   EMBL; MH183005; AYO60872.1; -; mRNA.
DR   AlphaFoldDB; A0A455LN84; -.
DR   SMR; A0A455LN84; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   2: Evidence at transcript level;
KW   Flavoprotein; FMN; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..201
FT                   /note="NAD(P)H-dependent FMN reductase ntnL"
FT                   /id="PRO_0000452571"
FT   BINDING         12
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q07923"
FT   BINDING         90..93
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q07923"
FT   BINDING         120
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q07923"
SQ   SEQUENCE   201 AA;  21931 MW;  D347A74DBC0FABA3 CRC64;
     MAKIALILGS VRSPRVGNDV TGWVHDVLKS RPSDDLQIEP LVIADFNLPV YDEPVMPAMV
     PAMKQFTKEH SKRWSAAIAS YQGYIFVIPE YNGGIAGGTK NAVDYLYNEW PGKPVAIISY
     GTQGGNRANA QLSESLELVM KMKVAPTKVL LPFAAGTDVF SAINDGVLGE ESQKAWAEAG
     KKEDILKALD EVKELLKQPK E