ID   C71DI_MENGR             Reviewed;         496 AA.
AC   Q6WKZ1;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Cytochrome P450 71D18;
DE            EC=1.14.14.51 {ECO:0000269|PubMed:11368174, ECO:0000269|PubMed:14599518};
DE   AltName: Full=(-)-(4S)-Limonene-6-hydroxylase;
GN   Name=CYP71D18;
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], FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11368174; DOI=10.1006/abbi.2000.2248;
RA   Wuest M., Little D.B., Schalk M., Croteau R.;
RT   "Hydroxylation of limonene enantiomers and analogs by recombinant (-)-
RT   limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for
RT   catalysis within sterically constrained active sites.";
RL   Arch. Biochem. Biophys. 387:125-136(2001).
CC   -!- FUNCTION: Hydroxylates (-)-(4S)-limonene to (-)-trans-carveol, a
CC       precursor of (-)-carvone. Fluorinated substrate analogs are
CC       hydroxylated with the same regio- and stereochemistry.
CC       {ECO:0000269|PubMed:11368174, ECO:0000269|PubMed:14599518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] =
CC         (1S,5R)-carveol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17945, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15383, ChEBI:CHEBI:15389, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.51;
CC         Evidence={ECO:0000269|PubMed:11368174, 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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY281025; AAQ18706.1; -; mRNA.
DR   AlphaFoldDB; Q6WKZ1; -.
DR   SMR; Q6WKZ1; -.
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:0018675; F:(S)-limonene 6-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 71D18"
FT                   /id="PRO_0000389498"
FT   TRANSMEM        2..22
FT                   /note="Helical; Signal-anchor for type II membrane protein"
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;  56149 MW;  06E4370F95EB91C0 CRC64;
     MELDLLSAII ILVATYIVSL LINQWRKSKS QQNLPPSPPK LPVIGHLHFL WGGLPQHVFR
     SIAQKYGPVA HVQLGEVYSV VLSSAEAAKQ AMKVLDPNFA DRFDGIGSRT MWYDKDDIIF
     SPYNDHWRQM RRICVTELLS PKNVRSFGYI RQEEIERLIR LLGSSGGAPV DVTEEVSKMS
     CVVVCRAAFG SVLKDQGSLA ELVKESLALA SGFELADLYP SSWLLNLLSL NKYRLQRMRR
     RLDHILDGFL EEHREKKSGE FGGEDIVDVL FRMQKGSDIK IPITSNCIKG FIFDTFSAGA
     ETSSTTISWA LSELMRNPAK MAKVQAEVRE ALKGKTVVDL SEVQELKYLR SVLKETLRLH
     PPFPLIPRQS REECEVNGYT IPAKTRIFIN VWAIGRDPQY WEDPDTFRPE RFDEVSRDFM
     GNDFEFIPFG AGRRICPGLH FGLANVEIPL AQLLYHFDWK LPQGMTDADL DMTETPGLSG
     PKKKNVCLVP TLYKSP