ID   DOX1_PERHD              Reviewed;         503 AA.
AC   W0FKI0;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Drimenol monooxygenase {ECO:0000305};
DE            EC=1.14.14.72 {ECO:0000269|PubMed:28258968};
DE   AltName: Full=Cytochrome P450 76AJ1 {ECO:0000303|PubMed:28258968};
DE   AltName: Full=Drimenol oxidase 1 {ECO:0000303|PubMed:28258968};
DE            Short=PhDOX1 {ECO:0000303|PubMed:28258968};
GN   Name=CYP76AJ1 {ECO:0000303|PubMed:28258968};
OS   Persicaria hydropiper (Marshpepper knotweed) (Polygonum hydropiper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Polygonaceae; Polygonoideae; Persicarieae; Persicaria.
OX   NCBI_TaxID=46901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=28258968; DOI=10.1111/tpj.13527;
RA   Henquet M.G.L., Prota N., van der Hooft J.J.J., Varbanova-Herde M.,
RA   Hulzink R.J.M., de Vos M., Prins M., de Both M.T.J., Franssen M.C.R.,
RA   Bouwmeester H., Jongsma M.;
RT   "Identification of a drimenol synthase and drimenol oxidase from Persicaria
RT   hydropiper, involved in the biosynthesis of insect deterrent drimanes.";
RL   Plant J. 90:1052-1063(2017).
CC   -!- FUNCTION: Catalyzes the conversion of drimenol to drimendiol, a
CC       precursor of the sesquiterpenoid polygodial (PubMed:28258968).
CC       Polygodial has been shown to be an antifeedant for a number of
CC       herbivorous insects (Probable). {ECO:0000269|PubMed:28258968,
CC       ECO:0000305|PubMed:28258968}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S,9S,10S)-drim-7-en-11-ol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (5S,10S)-(9R)-7-drimene-11,12-diol + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55504,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:61148, ChEBI:CHEBI:138971;
CC         EC=1.14.14.72; Evidence={ECO:0000269|PubMed:28258968};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55505;
CC         Evidence={ECO:0000269|PubMed:28258968};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; KC754969; AHF22835.1; -; mRNA.
DR   AlphaFoldDB; W0FKI0; -.
DR   SMR; W0FKI0; -.
DR   KEGG; ag:AHF22835; -.
DR   BRENDA; 1.14.14.72; 13328.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..503
FT                   /note="Drimenol monooxygenase"
FT                   /id="PRO_0000449921"
FT   TRANSMEM        7..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         471
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q96242"
SQ   SEQUENCE   503 AA;  56147 MW;  6A9A15AA1B3F53C5 CRC64;
     MDYLILMICI VVSGLLLYSS RTSKMKLPPG PPGLPIVGNL FDLGSLPHRS LAKLAKLHGP
     VMCLRMGRLR VVVISSDSAA KEVLQTSDTL FCNRFVYDSL TASQHHTFSM ALLPPTALWK
     SLRKISASQL FTNARMNASQ HLRRKQLEDL LSYVESCSRS GTAINIAQAA FNTSVNLLSK
     TFFSVDLIDP SSSNSVEFKE MVWQIMLESG TPNLADYFPV LRRIDPQGNR RRMKIQFEKI
     LDLFNTMIRQ RLDEKGGCFD EINDTLDALL KINQDNSEEL DLSVIPHLLL DLFVGGSEST
     SSTVEWAMAL LFSNPEKMKK AKEELETVVG KGIAVKEEDT GRLPYLQAAI KETFRMHPPT
     PFLIPRKTDS DVDLCGFTVQ KGSQVIVNAW AIGRDPSLWE NADTFEPERF LGMEIDVKGR
     NFELIPFGAG RRICPGLPIA MRMLTLMVAN LINCFEWRLE GGAAPETLDM SDKIGFTLQR
     AHPFRVIPTS IIQGCDVSTA LNN