NTNF_NECSZ
ID NTNF_NECSZ Reviewed; 310 AA.
AC A0A455LM21;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Polyprenyl transferase ntnF {ECO:0000303|PubMed:29797385};
DE EC=2.5.1.- {ECO:0000305|PubMed:29797385};
DE AltName: Full=Nectripenoid biosynthesis cluster protein F {ECO:0000303|PubMed:29797385};
GN Name=ntnF {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: olyprenyl transferase; part of the gene cluster that mediates
CC the biosynthesis of the meroterpenoids nectripenoids A and B, as well
CC as cochliquninone D and isocochliquninone E (PubMed:29797385). The
CC pathway probably begins with the HR-PKS ntnH that catalyzes two chain-
CC extension steps to form a reduced triketide, which then primes the SAT
CC domain in the NR-PKS ntnG to initiate three more cycles of extension to
CC give a linear hexaketide corresponding to the polyketide part of
CC nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ then
CC performs an oxidative decarboxylation at C11 of the ntnH/ntnG product,
CC via an electrophilic aromatic hydroxylation with concomitant ipso-
CC decarboxylation (Probable). The membrane-bound polyprenyl transferase
CC ntnF then introduces a farnesyl group before the FAD-dependent
CC monooxygenase ntnK functions as the first epoxidase on terminal C12'-
CC C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by
CC ntnA (Probable). The terpene cyclase/mutase ntnI then initiates the
CC sequential tricyclic ring formation through protonation of the terminal
CC epoxide and catalyzes the regioselective and stereoselective 6/6/6-
CC tricyclic ring formation (Probable). The cytochrome P450 monooxygenase
CC ntnM may then hydroxylate C1' (Probable). {ECO:0000269|PubMed:29797385,
CC ECO:0000305|PubMed:29797385}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P32378};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:29797385}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; MH182999; AYO60866.1; -; mRNA.
DR AlphaFoldDB; A0A455LM21; -.
DR SMR; A0A455LM21; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 2: Evidence at transcript level;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..310
FT /note="Polyprenyl transferase ntnF"
FT /id="PRO_0000452567"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 310 AA; 33853 MW; 88EFD234D109A4E3 CRC64;
MAAAGARHYT SKDGSQHDLV RGIWKLLRLH TPEGLSTASI GWLALFFYAI QQQLSFESLR
YTFLGIFACY QITHGVFCMW NDICDRDFDA QVARTKKRPL PSGMVTYTEA MVAFIIGLAL
SLGVTYAMLG EDVTLTMGPI WGLSFIYPLC KRAIWAPQAV LGLTMAACVL PPWVALGNDA
TNAKLPASLF GAIFSWLVYL DLIYASQDRP DDEKAGVKSL AVFLGDKLKA CLTVLGALQI
AFFAVAAFEA SASSFLWVFG IAVWAISVPW SILSLNPRDR NSGGRIFLVN AILGIYLAAV
SGTDVWLSSR
