ID   CYPD2_CATRO             Reviewed;         507 AA.
AC   W8JIT4;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Cytochrome P450 71D2 {ECO:0000303|PubMed:24710322};
DE            Short=CrCYP71D2 {ECO:0000303|PubMed:24710322};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP71D2 {ECO:0000303|PubMed:24710322};
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Little Bright Eyes;
RX   PubMed=24710322; DOI=10.1038/ncomms4606;
RA   Miettinen K., Dong L., Navrot N., Schneider T., Burlat V., Pollier J.,
RA   Woittiez L., van der Krol S., Lugan R., Ilc T., Verpoorte R.,
RA   Oksman-Caldentey K.M., Martinoia E., Bouwmeester H., Goossens A.,
RA   Memelink J., Werck-Reichhart D.;
RT   "The seco-iridoid pathway from Catharanthus roseus.";
RL   Nat. Commun. 5:3606-3606(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; KF302076; AHK60843.1; -; mRNA.
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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..507
FT                   /note="Cytochrome P450 71D2"
FT                   /id="PRO_0000446412"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         448
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|UniProtKB:P04798"
SQ   SEQUENCE   507 AA;  57924 MW;  3AF604B046CE7E58 CRC64;
     MDFEYLPFNL VTFFIFLFFV FLLIYGRRKS KRTXKINLPP GPWKLPILGN LHNMMMGSSP
     HHIFRDLSRK YGDLMLIKLG EFNTIVASSP RMAKEVLKTH DLSFLNRPII QATKILCYDN
     SALVFSQYGD SWRQMRKIFV LELLSTKRVR SFQPIRQDEG SRLVSLIKES VGKSIDLSEK
     IKLYTTSMVA RAAFGKVNDA GVTFLKLVTE AAEVAEGFDP ADMFPSYKFL NVFFNSRSNL
     LKIHGKTDMI LEEMIDEHIK SHQMGKKANG ENGEEDVIDI LLSIKDSGDL GISHWMNNVK
     ALIFDMFSAG TETSSATVEW AMTELMKNPS VMRKAQDEVR QAFKGKKTID ESDLEELKYL
     KLVVKEVLRL HPFAPLLVPR ECREACQIDG YDIPVKTRVF VNVWAIGRDE KYWKDPESFI
     PERFEDNSLD FTGNNFEYLP FGCGRRICPG MTFGLANVHL VLALLLYHFN WKLPPGVNDI
     DMAERPGLGA SKKHGLVLVP SFYQPSF