ID   C7D95_MENSP             Reviewed;         496 AA.
AC   Q6IV13;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Cytochrome P450 71D95;
DE            EC=1.14.14.99 {ECO:0000269|PubMed:15200648};
DE   AltName: Full=Limonene-3-hydroxylase;
GN   Name=CYP71D95; Synonyms=LIM3H;
OS   Mentha spicata (Spearmint).
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=29719;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC   TISSUE=Leaf;
RX   PubMed=15200648; DOI=10.1111/j.1365-313x.2004.02113.x;
RA   Luecker J., Schwab W., Franssen M.C.R., Van Der Plas L.H.W.,
RA   Bouwmeester H.J., Verhoeven H.A.;
RT   "Metabolic engineering of monoterpene biosynthesis: two-step production of
RT   (+)-trans-isopiperitenol by tobacco.";
RL   Plant J. 39:135-145(2004).
CC   -!- FUNCTION: Hydroxylates both (+)- and (-)-limonene to (+) and (-)-trans-
CC       isopiperitenol. {ECO:0000269|PubMed:15200648}.
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:15200648};
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY622319; AAT39473.1; -; mRNA.
DR   AlphaFoldDB; Q6IV13; -.
DR   SMR; Q6IV13; -.
DR   KEGG; ag:AAT39473; -.
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..496
FT                   /note="Cytochrome P450 71D95"
FT                   /id="PRO_0000389503"
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   496 AA;  56322 MW;  208040252F8211F8 CRC64;
     MELQISSAII ILVATFVASL LIKQWRKSES RQNLPPGPPK LPLVGHLHLL WGKLPQHAMA
     DMAKKYGPVT HVQLGEVFSV VLSSREATKE AMKLLDPACA DRFESIGTRI MWYDNDDIIF
     SPYSDHWRQM RKICVSELLS ARNVRSFGFI RQDEMSRLLR HLQSSAGETV DMTERIATLT
     CSIICRAAFG AIINDHEELV ELVKDSLSMA SGFELADLFP SSKLLNLLCW NKSKLWRMRR
     RVDTILEAIV DEHKLKKSGE FGGEDIIDVL FRMQKDSQIK VPITTNAIKA FIFDTFSAGT
     ETSSTTTLWV MAELMRNPAV MAKAQAEVRA ALKGKTSVDV DDVQELKYMK SVVKETMRMH
     PPIPLIPRSC REECEVNGYK IPNKARIMIN VWSMGRNPLY WEKPETFWPE RFDQVSRDFM
     GSDFEFIPFG AGRRICPGLN FGLANVEVPL AQLLYHFDWK LAEGMKPSDM DMSEAEGLTG
     IRKNNLLLVP TLYKSP