ID   C75A1_PINTA             Reviewed;         525 AA.
AC   Q50EK4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cytochrome P450 750A1;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 CYPC;
GN   Name=CYP750A1;
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; AY779539; AAX07433.1; -; mRNA.
DR   AlphaFoldDB; Q50EK4; -.
DR   SMR; Q50EK4; -.
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..525
FT                   /note="Cytochrome P450 750A1"
FT                   /id="PRO_0000352519"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         465
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   525 AA;  59073 MW;  900DB1C10B8B9093 CRC64;
     MSFDKLLQAL PPPLPLPAIL IATFIFFFSC WILHQSQRNE RLPPGPYPWP IIGNFHQVRL
     PLHRTLKNLA EKYGPILFLR FGSVPTVVVS SSEKAKHFLK THDLIFASRP PTSVGKYFFY
     NFKDIAFSPY GDHWRKMRKI CVLELLTSKR IESFKHVRQE ELSAMIHSIW EESESGRIAV
     NVSKAISTSL ANILWRILAR KKFSDNDLGA DGKGFADLVV EVSIAVGSLN IGDFIPYLDC
     LDLQGIKRAL KKANARFDAF AEKMIDEHIN ASTIRNGEAD AGCHVKDIID VLLEMAKNDN
     TGAKVTREII KAITYELFSA GMETSANVLE WAMSELLRHP HAMKKLQQEI ESVVGQQGTV
     KESDLASIVY LHCVVKETLR LYPSLPLALP HESLEAVTVG GYYIPKKTMV IMNLWAIGRD
     PSVWGADASE FKPERFMQME ENGIDLSGGQ SDFRMLPFGA GRRTCPGSAM AILTVEFTLA
     QLLHTFDWRV EGDPSELDMK EACATKMPRQ TPLLAYPRLR LPRCP