ID   C7D95_MENGR             Reviewed;         497 AA.
AC   Q6WKY9;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cytochrome P450 71D95;
DE            EC=1.14.14.99 {ECO:0000269|PubMed:14599518};
DE   AltName: Full=(-)-(4S)-Limonene-3-hydroxylase;
GN   Name=CYP71D95;
OS   Mentha gracilis (Gingermint).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC   Mentha.
OX   NCBI_TaxID=241069;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=14599518; DOI=10.1016/j.phytochem.2003.09.002;
RA   Bertea C., Schalk M., Mau C.J.D., Karp F., Wildung M.R., Croteau R.;
RT   "Molecular evaluation of a spearmint mutant altered in the expression of
RT   limonene hydroxylases that direct essential oil monoterpene biosynthesis.";
RL   Phytochemistry 64:1203-1211(2003).
CC   -!- FUNCTION: Hydroxylates (-)-(4S)-limonene to (-)-trans-isopiperitenol, a
CC       precursor of (-)-menthol. No activity with (+)- or (-)-piperitone, (-)-
CC       isopiperitone and piperitenone. {ECO:0000269|PubMed:14599518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] =
CC         (1S,6R)-isopiperitenol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:15129, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15383, ChEBI:CHEBI:15406, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.99;
CC         Evidence={ECO:0000269|PubMed:14599518};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: This gene is normally not expressed in wild type plants.
CC       Gamma irradiation induced probably a mutation in a regulatory gene,
CC       leading to the repression of the native limonene-6-hydroxylase and in
CC       the novel expression of this previously silent limonene-3-hydroxylase.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY281027; AAQ18708.1; -; mRNA.
DR   AlphaFoldDB; Q6WKY9; -.
DR   SMR; Q6WKY9; -.
DR   KEGG; ag:AAQ18708; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0018674; F:(S)-limonene 3-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; 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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..497
FT                   /note="Cytochrome P450 71D95"
FT                   /id="PRO_0000389502"
FT   TRANSMEM        2..22
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   BINDING         436
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"
SQ   SEQUENCE   497 AA;  56364 MW;  56A41C95671E8FAB CRC64;
     MELQISSAII ILVATFVASL LIKQWRKSES QQNLPPGPPK LPLVGHLHLL WGKLPQHAMA
     DMAKKYGPVT HVQLGEVFSV VLSSREATKE AMKLLDPACA DRFESIGTRI MWYDNDDIIF
     SPYSDHWRQM RKICVSELLS ARNVRSFGFI RQDEMSRLLR HLQSSAGETV DMTERIATLT
     CSIICRAAFG AIINDHEELV ELVKDSLSMA SGFELADLFP SSKLLNLLCW NKSKLWRMRR
     RVDTILEAIV EEHKLKKSGE FGGEDIIDVL FRMQKDSQIK VPITTNAIKA FIFDTFSAGT
     ETSSTTTLWV MAELMRNPAV MAKAQAEVRA ALKGKTSVDV DDVQELKYMK SVVKETMRMH
     PPIPLIPRSC REECEVNGYK IPNKARIMIN VWSMGRNPLY WEKPETFWPE RFDQVSRDFM
     GSDFEFIPFG AGRRICPGLN FGLANVEVPL AQLLYHFDWK LAEGMKPSDM DMSEAEGLTG
     IRKNNLLLVP TPYNPSS