ID   C72B2_PINTA             Reviewed;         487 AA.
AC   Q50EK5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Cytochrome P450 720B2;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 CYPB;
GN   Name=CYP720B2;
OS   Pinus taeda (Loblolly pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352;
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; AY779538; AAX07432.1; -; mRNA.
DR   AlphaFoldDB; Q50EK5; -.
DR   SMR; Q50EK5; -.
DR   BRENDA; 1.14.14.145; 4861.
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..487
FT                   /note="Cytochrome P450 720B2"
FT                   /id="PRO_0000352515"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         436
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   487 AA;  56222 MW;  4C3B1361BFEE0BAB CRC64;
     MGSGIMTETL TDSWLVGLLC LVLGFLLLQL YKLVWGASSR AYKLPPGSTG WPLIGETISF
     FRGINSTAQP RQFIQEREQR YGEIFRSNLF GRSRIVVSVD PEFNKHVLQH EGRQFQANYP
     KPLRNLIGKY GLLSVHGDLQ RKLHGAAVNL LRFERLSVDF MEDIQNLLHI TLAKWEAKRD
     IHLQEECHQL VLNLMAKQLL DLSPSKDTEE ICEAFGHFSE ALLAVPIKIP GTKYARGFKA
     REFLIKKIYE SIEDRRQHPE AVHNDLLTKL LKEDSFSEEI IADFILFLLF AGHETSSRSM
     SFAIKFLTDC PRALEELKAE HDALLKRKGN LKNQKLNWDD YQSLKFTQCV IHETLRVGNF
     GPGVFRETKE DIKTKGGFVI PRGWTVYVFL TGTHLDEKYH SSALKFDPWR WQPHLQDQEL
     LKNPSFMPFG GGARLCPGMH LAKMELALFL HNFVTKFRWE ALQDDKISYF PFPRLIKGLP
     IRLRLRE