C72B1_PINTA
ID C72B1_PINTA Reviewed; 481 AA.
AC Q50EK6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Abietadienol/abietadienal oxidase;
DE Short=PtAO;
DE EC=1.14.14.145 {ECO:0000269|PubMed:15911762};
DE AltName: Full=Cytochrome P450 720B1;
DE AltName: Full=Cytochrome P450 CYPA;
GN Name=CYP720B1;
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 -!- FUNCTION: Multifunctional and multisubstrate cytochrome P450 that
CC oxidizes the respective carbon 18 of abietadienol, abietadienal,
CC levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal,
CC dehydroabietadienol, and dehydroabietadienal.
CC {ECO:0000269|PubMed:15911762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=abieta-7,13-dien-18-ol + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = abieta-7,13-dien-18-oate + 3 H(+) + 3 H2O + 2 oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:26221, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29510,
CC ChEBI:CHEBI:35680, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.145; Evidence={ECO:0000269|PubMed:15911762};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for abietadienol {ECO:0000269|PubMed:15911762};
CC KM=5.3 uM for dehydroabietadienol {ECO:0000269|PubMed:15911762};
CC KM=1.5 uM for isopimaradienol {ECO:0000269|PubMed:15911762};
CC KM=1.9 uM for levopimaradienol {ECO:0000269|PubMed:15911762};
CC KM=0.5 uM for abietadienal {ECO:0000269|PubMed:15911762};
CC KM=0.6 uM for dehydroabietadienal {ECO:0000269|PubMed:15911762};
CC KM=0.6 uM for isopimaradienal {ECO:0000269|PubMed:15911762};
CC Vmax=77 pmol/min/mg enzyme with abietadienol as substrate
CC {ECO:0000269|PubMed:15911762};
CC Vmax=211 pmol/min/mg enzyme with dehydroabietadienol as substrate
CC {ECO:0000269|PubMed:15911762};
CC Vmax=122 pmol/min/mg enzyme with isopimaradienol as substrate
CC {ECO:0000269|PubMed:15911762};
CC Vmax=137 pmol/min/mg enzyme with levopimaradienol as substrate
CC {ECO:0000269|PubMed:15911762};
CC Vmax=181 pmol/min/mg enzyme with abietadienal as substrate
CC {ECO:0000269|PubMed:15911762};
CC Vmax=379 pmol/min/mg enzyme with dehydroabietadienal as substrate
CC {ECO:0000269|PubMed:15911762};
CC Vmax=226 pmol/min/mg enzyme with isopimaradienal as substrate
CC {ECO:0000269|PubMed:15911762};
CC pH dependence:
CC Optimum pH is7.5-7.6. {ECO:0000269|PubMed:15911762};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young tissues such as flushing buds
CC and green bark tissues. Lower levels in mature needles and bark.
CC {ECO:0000269|PubMed:15911762}.
CC -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:15911762}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY779537; AAX07431.1; -; mRNA.
DR AlphaFoldDB; Q50EK6; -.
DR SMR; Q50EK6; -.
DR KEGG; ag:AAX07431; -.
DR BioCyc; MetaCyc:MON-12739; -.
DR BRENDA; 1.14.14.145; 4861.
DR SABIO-RK; Q50EK6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036204; F:abieta-7,13-dien-18-ol hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; 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 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="Abietadienol/abietadienal oxidase"
FT /id="PRO_0000352514"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 430
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 481 AA; 55702 MW; 26D45BCDFB3EBA94 CRC64;
MADQISLLLV VFTAAVALLH LIYRWWNAQR GQKRTSNEKN QELHLPPGST GWPLIGETYS
YYRSMTSNRP RQFIDDREKR YDSDVFVSHL FGSQAVISSD PQFNKYVLQN EGRFFQAHYP
KALKALIGDY GLLSVHGDLQ RKLHGIAVNL LRFERLKFDF MEEIQNLVHS TLDRWVDKKE
IALQNECHQM VLNLMAKQLL DLSPSKETNE ICELFVDYTN AVIAIPIKIP GSTYAKGLKA
RELLIRKISN MIKERRDHPH IVHKDLLTKL LEEDSISDEI ICDFILFLLF AGHETSSRAM
TFAIKFLTTC PKALTQMKEE HDAILKAKGG HKKLEWDDYK SMKFTQCVIN ETLRLGNFGP
GVFRETKEDT KVKDCLIPKG WVVFAFLTAT HLDEKFHNEA LTFNPWRWEL DQDVSNNHLF
SPFGGGARLC PGSHLARLEL ALFLHIFITR FRWEALADEH PSYFPLPYLA KGFPMRLYNR
E
