ID   CPXO_PSEPU              Reviewed;         406 AA.
AC   Q59723;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Linalool 8-monooxygenase;
DE            EC=1.14.14.84 {ECO:0000269|PubMed:2295633};
DE   AltName: Full=Cytochrome P450 111;
DE   AltName: Full=Cytochrome P450lin;
GN   Name=linC; Synonyms=cyp111;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D110R;
RX   PubMed=8376348; DOI=10.1128/jb.175.18.6028-6037.1993;
RA   Ropp J.D., Gunsalus I.C., Sligar S.G.;
RT   "Cloning and expression of a member of a new cytochrome P-450 family:
RT   cytochrome P-450lin (CYP111) from Pseudomonas incognita.";
RL   J. Bacteriol. 175:6028-6037(1993).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=G777;
RX   PubMed=2295633; DOI=10.1016/s0021-9258(19)40020-3;
RA   Ullah A.J., Murray R.I., Bhattacharyya P.K., Wagner G.C., Gunsalus I.C.;
RT   "Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase.";
RL   J. Biol. Chem. 265:1345-1351(1990).
RN   [3]
RP   ABSORPTION SPECTROSCOPY.
RX   PubMed=3813557; DOI=10.1016/0003-9861(87)90642-4;
RA   Marden M.C., Hui Bon Hoa G.;
RT   "P-450 binding to substrates camphor and linalool versus pressure.";
RL   Arch. Biochem. Biophys. 253:100-107(1987).
RN   [4]
RP   FOURIER-TRANSFORM INFRARED SPECTROSCOPY.
RA   Jung C., Marlow F.;
RT   "Dynamic behavior of the active site structure in bacterial cytochrome P-
RT   450.";
RL   Studia Biophys. 120:241-251(1987).
RN   [5]
RP   ABSORPTION SPECTROSCOPY, AND FLUORESCENCE SPECTROSCOPY.
RX   PubMed=2578028; DOI=10.1021/bi00428a035;
RA   Hui Bon Hoa G., Di Primo C., Dondaine I., Sligar S.G., Gunsalus I.C.,
RA   Douzou P.;
RT   "Conformational changes of cytochromes P-450cam and P-450lin induced by
RT   high pressure.";
RL   Biochemistry 28:651-656(1989).
RN   [6]
RP   CIRCULAR DICHROISM ANALYSIS.
RX   PubMed=1610873; DOI=10.1016/0005-2728(92)90078-g;
RA   Nolting B., Jung C., Snatzke G.;
RT   "Multichannel circular dichroism investigations of the structural stability
RT   of bacterial cytochrome P-450.";
RL   Biochim. Biophys. Acta 1100:171-176(1992).
RN   [7]
RP   SUBSTRATE-PROTEIN INTERACTION.
RX   PubMed=12237225; DOI=10.1016/s0162-0134(02)00467-1;
RA   Deprez E., Gill E., Helms V., Wade R., Hui Bon Hoa G.;
RT   "Specific and non-specific effects of potassium cations on substrate-
RT   protein interactions in cytochromes P450cam and P450lin.";
RL   J. Inorg. Biochem. 91:597-606(2002).
CC   -!- FUNCTION: Catalyzes the 8-methyl hydroxylation of linalool.
CC       {ECO:0000269|PubMed:2295633}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=linalool + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] =
CC         (6E)-8-oxolinalool + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:32635, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17580, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:64259; EC=1.14.14.84;
CC         Evidence={ECO:0000269|PubMed:2295633};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- PATHWAY: Terpene metabolism; linalool degradation.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; L23310; AAA25810.1; -; Genomic_DNA.
DR   PIR; A48495; A48495.
DR   AlphaFoldDB; Q59723; -.
DR   SMR; Q59723; -.
DR   KEGG; ag:AAA25810; -.
DR   BRENDA; 1.14.14.84; 5092.
DR   UniPathway; UPA00721; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0050056; F:linalool 8-monooxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..406
FT                   /note="Linalool 8-monooxygenase"
FT                   /id="PRO_0000052225"
FT   BINDING         355
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   406 AA;  45637 MW;  46DC62A64D6309D6 CRC64;
     MERPDLKNPD LYTQQVPHDI FARLRREEPV YWNPESDGSG FWAVLRHKDI IEVSRQPLLF
     SSAYENGGHR IFNENEVGLT NAGEAAVGVP FISLDPPVHT QYRKVIMPAL SPARLGDIEQ
     RIRVRAEALI ERIPLGEEVD LVPLLSAPLP LLTLAELLGL DPDCWYELYN WTNAFVGEDD
     PEFRKSPEDM AKVLGEFMGF CQELFESRRA NPGPDIATLL ANAEINGQPV ALRDFIGNLT
     LTLVGGNETT RNSISHTIVT LSQQPDQWDI LRQRPELLKT ATAEMVRHAS PVLHMRRTAM
     EDTEIGGQAI AKGDKVVLWY ASGNRDESVF SDADRFDVTR TGVQHVGFGS GQHVCVGSRL
     AEMQLRVVFE ILSTRVKRFE LCSKSRRFRS NFLNGLKNLN VVLVPK