ID   C16B1_PICSI             Reviewed;         493 AA.
AC   Q50EK1;
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 716B1;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 CYPA1;
GN   Name=CYP716B1;
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; AY779542; AAX07436.1; -; mRNA.
DR   AlphaFoldDB; Q50EK1; -.
DR   SMR; Q50EK1; -.
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..493
FT                   /note="Cytochrome P450 716B1"
FT                   /id="PRO_0000352517"
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   493 AA;  56273 MW;  2381E5BFFF06120D CRC64;
     MVWKEAVSVL QKAQELKEPP LMFTVFLASF IGLAFFFYLI SNHRTKAWRG IPPGTFGWPL
     IGETLEFLGC QRKGNPRDFF DSRTQKYGNV FTTSLVGHPT VVFCSPEGNR FLFSNENKLV
     VNSWPSSVGN LFRSSLITTV GDDAKRLRRI LMTFLRPEAL REFVGRVDSM TKRHLAEHWI
     GKDEVMALPL LKRYTFSLAC DLFASINTKD DLDRLWLHFM VFVKGVMQIP IDLPGTRYNK
     TKHAANAIRQ QLGSIINERK IALEAGNASP EQDLLSFLLS NVDEQGESLT DNEIQDNILL
     LLYAGHDTSS STLTVLLKFL AENPHCYEEV LREQLNIAGS KEEGQLLEWE DLQRMKYSWR
     VAQEALRLFP AVQGSFRKAI KEFIYDGFTI PKGWKLHWTV NSTHQKSEYF SNPEKFDPSR
     FEGEGPPPYT FVPFGGGPRM CPGNEFARME ILIFLHNIVK NFNWNLVNPL EKVIVDPMPA
     PVNGLPIKLV PHD