ID   C71A8_MENPI             Reviewed;         502 AA.
AC   Q42716;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cytochrome P450 71A8;
DE            EC=1.14.-.-;
GN   Name=CYP71A8;
OS   Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata).
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=34256;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kang M.H., Choi Y.D.;
RT   "Molecular cloning of a genomic DNA for cytochrome P-450 oxidase from
RT   Mentha piperita.";
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; Z33875; CAA83941.1; -; Genomic_DNA.
DR   PIR; S45039; S45039.
DR   AlphaFoldDB; Q42716; -.
DR   SMR; Q42716; -.
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   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="Cytochrome P450 71A8"
FT                   /id="PRO_0000052061"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          93..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         447
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   502 AA;  57213 MW;  EE78AE5922CCDFE7 CRC64;
     MYSIAFMLVL RKMDEIISHT LAFQALVSLI LLISITKWLS NSPKNKNSSP PSPRKLPILG
     NLLQLGSLPH HNLRSMARKH GPIMLLHLGS VRPVSSRRRP RGNHENSRSR LRRPRGSRSA
     ALQLQGRVGG YGEYWRQLKT ICVVQLLSNK RVQSFRSVRE EETELLMKKI GDSSGNVNLS
     HMFTQLTNDV VCRSAIGRKY GAGDENGEKF LEILREFLEL LGAISIGDFV PSLWWINRIN
     GFDRRVDRIA KEMDEFLEKV IHERLENPAA KAEENFVDIL LEIYRNNSAG VSIDRDSIKA
     IILDVFAAGT DTTAVVLEWA MTELLRHPEI MKKLQSEVRQ VVKDKHNITD DDIEKMHYLK
     AVMKETMRFH TPIPLLVPRV ARNDVEVMGY DVPVGTMVMI NAWAIGRDPT SWDEPEKFRP
     ERFLNSSVDF KGLDFELIPF GAGRRGCPGT TFPMATLEFT LANLMQKFDW ELPHECRELD
     MSERPGVAIR RVIPLLAIGT KM