ID   C7D94_MENGR             Reviewed;         494 AA.
AC   Q6WKZ0;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Cytochrome P450 71D94;
GN   Name=CYP71D94;
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], 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: Cytochrome P450 oxygenase of undefined substrate. Not active
CC       with limonene, (+)- or (-)-piperitone, (-)-isopiperitone, piperitenone
CC       or (+)-pulegone. {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: The Thr-300 residue involved in activation of molecular
CC       oxygen during the hydroxylation reaction is replaced by Ala-300,
CC       suggesting that this cytochrome P450 might utilize limonene
CC       hydroperoxide as a substrate to produce limonene epoxide.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY281026; AAQ18707.1; -; mRNA.
DR   AlphaFoldDB; Q6WKZ0; -.
DR   SMR; Q6WKZ0; -.
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: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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   NADP; Oxidoreductase; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..494
FT                   /note="Cytochrome P450 71D94"
FT                   /id="PRO_0000389501"
FT   TRANSMEM        1..21
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   BINDING         434
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   494 AA;  56308 MW;  41CE17959B986700 CRC64;
     MELNLLLVII ILVATYTVSL LNKQWRKPKS QQKQPPKLPV IGHLHLLWGG LPPQHLLRSI
     AREYGPVAHV QLGEVYSVVL SSAEAAKQAM KVLDPNFADR FDSVGSRIMW YDNDDIIFSP
     YNDHWHQMRK ICVSELLSPK NVRSFGFIRQ EEIERLIRVM KQSEGAPVDV TEEVSKMSCF
     VVCRAAFGSV LKDQGSLAEL VKESLAMASG FELKDLYPSS WLLNLLSFNN YRLKRMRRRL
     DHVLDGFLEE HRVKKNGEFG GEDIVDVLFR MQKDSNIKIP ITSNGIKGFI FNTFSAGAEA
     SSTTISWALS ELMRNPAKMA KVQAEVREAL KGKTSVDLSE MQELKYMRSV VKETLRLHPP
     FPLIPRQSRE ECEINGFYIP ARTRILINAW SIGRDPLYWE DPDTFRPERF DEVSRDFMGN
     DFEFIPFGAG QRICPGLHFG LANVEIPLAQ LLYHFDWKLP QGMTDADLYV AGTPGLSGPR
     KKNVFLVPTI HKSR