ID   C16B2_PICSI             Reviewed;         497 AA.
AC   Q50EK0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Cytochrome P450 716B2;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 CYPA2;
GN   Name=CYP716B2;
OS   Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15911762; DOI=10.1073/pnas.0500825102;
RA   Ro D.-K., Arimura G., Lau S.Y.W., Piers E., Bohlmann J.;
RT   "Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a
RT   multifunctional, multisubstrate cytochrome P450 monooxygenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:8060-8065(2005).
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; AY779543; AAX07437.1; -; mRNA.
DR   AlphaFoldDB; Q50EK0; -.
DR   SMR; Q50EK0; -.
DR   OMA; APGIMSV; -.
DR   BRENDA; 1.14.14.145; 8974.
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..497
FT                   /note="Cytochrome P450 716B2"
FT                   /id="PRO_0000352518"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         441
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   497 AA;  56458 MW;  6F9CCF8854AC5621 CRC64;
     MVWKEAVSVL QKAQELKEPP LMFTVFLASF IGLAFFFYLI SNHRTKAWRG IPPGTFGWPL
     IGETLEFLGC QRKGNPRDFF DSRTQKYGNV FTTSLVGHPT VVFCSPEGNR FLFSNENKLV
     VNSWPSSVGN LFRSSLITTV GDDAKRLRRI LMTFLRPEAL REFVGRVDSM TKRHLAEHWI
     GKDEVTALPL LKRYTFSLAC DLFASINNKD DLGRLWLHFM VFVKGVMQIP IDLPGTRYNK
     AKHAANAIRQ QLGSIINERK IGLEAGNASP EQDLLSFLLS NVDEQGESLT DNEIQDNILL
     LLYAGHDTSS STLTVLLKFL AENPHCYEEV LREQLDIAGS KEAGQLLEWE DLQRMKYSWR
     VAQEALRLFP AAQGSFRKAI KEFIYDGFTI PKGWKMYWTV NSTHRKSEYF SNPETFDPSR
     FEGEGPPPYT FVPFGGGPRM CPGNEFARLE ILVFLHNIVK NCKWNLVNPG EKVIVDPMPA
     PVNGLPIKLV PHDSVYI