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Database: UniProt
Entry: Q50EK6
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Original site: Q50EK6 
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   13-SEP-2023, entry version 78.
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:MONOMER-12739; -.
DR   BRENDA; 1.14.14.145; 4861.
DR   SABIO-RK; Q50EK6; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd11043; CYP90-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR   PANTHER; PTHR24286:SF232; CYTOCHROME P450 SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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
//
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