CPXA_PSEPU
ID CPXA_PSEPU Reviewed; 415 AA.
AC P00183;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Camphor 5-monooxygenase;
DE EC=1.14.15.1;
DE AltName: Full=Cytochrome P450-cam;
DE Short=Cytochrome P450cam;
GN Name=camC; Synonyms=cyp101;
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=G1 / ATCC 17453;
RX PubMed=3003058; DOI=10.1016/s0021-9258(17)36068-4;
RA Unger B.P., Gunsalus I.C., Sligar S.G.;
RT "Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and
RT its expression in Escherichia coli.";
RL J. Biol. Chem. 261:1158-1163(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 386-415.
RC STRAIN=G1 / ATCC 17453;
RX PubMed=2613690; DOI=10.1093/oxfordjournals.jbchem.a122939;
RA Koga H., Yamaguchi E., Matsunaga K., Aramaki H., Horiuchi T.;
RT "Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene
RT (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam
RT hydroxylase of Pseudomonas putida.";
RL J. Biochem. 106:831-836(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-415.
RX PubMed=7130171; DOI=10.1016/s0021-9258(18)33562-2;
RA Haniu M., Armes L.G., Yasunobu K.T., Shastry B.A., Gunsalus I.C.;
RT "Amino acid sequence of the Pseudomonas putida cytochrome P-450. II.
RT Cyanogen bromide peptides, acid cleavage peptides, and the complete
RT sequence.";
RL J. Biol. Chem. 257:12664-12671(1982).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=4066706; DOI=10.1016/s0021-9258(17)36209-9;
RA Poulos T.L., Finzel B.C., Gunsalus I.C., Wagner G.C., Kraut J.;
RT "The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.";
RL J. Biol. Chem. 260:16122-16130(1985).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9357977; DOI=10.1016/s0014-5793(97)01135-6;
RA Schlichting I., Jung C., Schulze H.;
RT "Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor
RT enantiomer.";
RL FEBS Lett. 415:253-257(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RA Di Gleria K., Nickerson D.P., Hill H.A.O., Wong L.-L., Fueloep V.;
RT "Covalent attachment of an electroactive sulfydryl reagent in the active
RT site of cytochrome P450cam as revealed by the crystal structure of the
RT modified protein.";
RL J. Am. Chem. Soc. 120:46-52(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9649301; DOI=10.1021/bi980189f;
RA Vidakovic M., Sligar S.G., Li H., Poulos T.L.;
RT "Understanding the role of the essential Asp251 in cytochrome p450cam using
RT site-directed mutagenesis, crystallography, and kinetic solvent isotope
RT effect.";
RL Biochemistry 37:9211-9219(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=10557259; DOI=10.1073/pnas.96.23.12987;
RA Dmochowski I.J., Crane B.R., Wilker J.J., Winkler J.R., Gray H.B.;
RT "Optical detection of cytochrome P450 by sensitizer-linked substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12987-12990(1999).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10698731; DOI=10.1126/science.287.5458.1615;
RA Schlichting I., Berendzen J., Chu K., Stock A.M., Maves S.A., Benson D.E.,
RA Sweet R.M., Ringe D., Petsko G.A., Sligar S.G.;
RT "The catalytic pathway of cytochrome p450cam at atomic resolution.";
RL Science 287:1615-1622(2000).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
RX PubMed=11098139; DOI=10.1093/oxfordjournals.jbchem.a022848;
RA Hishiki T., Shimada H., Nagano S., Egawa T., Kanamori Y., Makino R.,
RA Park S.-Y., Adachi S., Shiro Y., Ishimura Y.;
RT "X-ray crystal structure and catalytic properties of Thr252Ile mutant of
RT cytochrome P450cam: roles of Thr252 and water in the active center.";
RL J. Biochem. 128:965-974(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=11258878; DOI=10.1021/bi002225s;
RA Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y.;
RT "Structural characterization of n-butyl-isocyanide complexes of cytochromes
RT P450nor and P450cam.";
RL Biochemistry 40:2669-2677(2001).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=11606730; DOI=10.1073/pnas.221297998;
RA Dunn A.R., Dmochowski I.J., Bilwes A.M., Gray H.B., Crane B.R.;
RT "Probing the open state of cytochrome P450cam with ruthenium-linker
RT substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12420-12425(2001).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=12464241; DOI=10.1016/s0003-9861(02)00555-6;
RA Fedorov R., Ghosh D.K., Schlichting I.;
RT "Crystal structures of cyanide complexes of P450cam and the oxygenase
RT domain of inducible nitric oxide synthase -- structural models of the
RT short-lived oxygen complexes.";
RL Arch. Biochem. Biophys. 409:25-31(2003).
RN [19]
RP STRUCTURE BY NMR.
RX PubMed=9315686; DOI=10.1016/s0014-5793(97)00995-2;
RA Mouro C., Bondon A., Simmoneaux G., Jung C.;
RT "1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme
RT resonances and substrate dependance of one cysteinate beta proton.";
RL FEBS Lett. 414:203-208(1997).
CC -!- FUNCTION: Involved in a camphor oxidation system.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,4R)-camphor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [putidaredoxin] = (1R,4R,5R)-5-hydroxycamphor + H2O + 2 oxidized
CC [2Fe-2S]-[putidaredoxin]; Xref=Rhea:RHEA:13525, Rhea:RHEA-COMP:14157,
CC Rhea:RHEA-COMP:14158, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15396, ChEBI:CHEBI:15398,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.1;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- PATHWAY: Terpene metabolism; (R)-camphor degradation.
CC -!- INTERACTION:
CC P00183; P00259: camB; NbExp=3; IntAct=EBI-15706256, EBI-15706395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M12546; AAA25760.1; -; Genomic_DNA.
DR EMBL; D00528; BAA00412.1; -; Genomic_DNA.
DR PIR; A25660; O4PSCP.
DR PDB; 1AKD; X-ray; 1.80 A; A=2-415.
DR PDB; 1C8J; X-ray; 2.10 A; A/B=2-415.
DR PDB; 1CP4; X-ray; 1.90 A; A=2-415.
DR PDB; 1DZ4; X-ray; 1.60 A; A/B=2-415.
DR PDB; 1DZ6; X-ray; 1.90 A; A/B=2-415.
DR PDB; 1DZ8; X-ray; 1.90 A; A/B=2-415.
DR PDB; 1DZ9; X-ray; 1.90 A; A/B=2-415.
DR PDB; 1GEB; X-ray; 2.03 A; A=1-415.
DR PDB; 1GEK; X-ray; 1.70 A; A=1-415.
DR PDB; 1GEM; X-ray; 2.00 A; A=1-415.
DR PDB; 1GJM; X-ray; 2.20 A; A=2-415.
DR PDB; 1IWI; X-ray; 2.00 A; A=1-415.
DR PDB; 1IWJ; X-ray; 2.00 A; A=1-415.
DR PDB; 1IWK; X-ray; 2.00 A; A=1-415.
DR PDB; 1J51; X-ray; 2.20 A; A/B/C/D=2-415.
DR PDB; 1K2O; X-ray; 1.65 A; A/B=2-415.
DR PDB; 1LWL; X-ray; 2.20 A; A=1-415.
DR PDB; 1MPW; X-ray; 2.34 A; A/B=2-415.
DR PDB; 1NOO; X-ray; 2.20 A; A=2-415.
DR PDB; 1O76; X-ray; 1.80 A; A/B=2-415.
DR PDB; 1P2Y; X-ray; 2.30 A; A=2-415.
DR PDB; 1P7R; X-ray; 2.85 A; A=2-415.
DR PDB; 1PHA; X-ray; 1.63 A; A=2-415.
DR PDB; 1PHB; X-ray; 1.60 A; A=2-415.
DR PDB; 1PHC; X-ray; 1.60 A; A=2-415.
DR PDB; 1PHD; X-ray; 1.60 A; A=2-415.
DR PDB; 1PHE; X-ray; 1.60 A; A=2-415.
DR PDB; 1PHF; X-ray; 1.60 A; A=2-415.
DR PDB; 1PHG; X-ray; 1.60 A; A=2-415.
DR PDB; 1QMQ; X-ray; 1.55 A; A=2-415.
DR PDB; 1RE9; X-ray; 1.45 A; A=2-415.
DR PDB; 1RF9; X-ray; 1.80 A; A=1-415.
DR PDB; 1T85; X-ray; 1.80 A; A=2-415.
DR PDB; 1T86; X-ray; 1.90 A; A/B=2-415.
DR PDB; 1T87; X-ray; 1.80 A; A/B=2-415.
DR PDB; 1T88; X-ray; 1.90 A; A/B=2-415.
DR PDB; 1UYU; X-ray; 2.00 A; A/B=2-415.
DR PDB; 1YRC; X-ray; 1.40 A; A=2-415.
DR PDB; 1YRD; X-ray; 1.70 A; A=2-415.
DR PDB; 2A1M; X-ray; 2.10 A; A/B=1-415.
DR PDB; 2A1N; X-ray; 1.90 A; A/B=1-415.
DR PDB; 2A1O; X-ray; 1.55 A; A/B=1-415.
DR PDB; 2CP4; X-ray; 2.10 A; A=2-415.
DR PDB; 2CPP; X-ray; 1.63 A; A=2-415.
DR PDB; 2FE6; X-ray; 1.50 A; A=1-415.
DR PDB; 2FER; X-ray; 1.70 A; A=11-415.
DR PDB; 2FEU; X-ray; 1.70 A; A/B=11-415.
DR PDB; 2FRZ; X-ray; 2.10 A; A/B=2-415.
DR PDB; 2GQX; X-ray; 2.10 A; A/B=11-415.
DR PDB; 2GR6; X-ray; 2.30 A; A/B=11-415.
DR PDB; 2H7Q; X-ray; 1.50 A; A=2-415.
DR PDB; 2H7R; X-ray; 2.10 A; A=2-415.
DR PDB; 2H7S; X-ray; 2.15 A; A/C=2-415.
DR PDB; 2L8M; NMR; -; A=1-415.
DR PDB; 2LQD; NMR; -; A=3-415.
DR PDB; 2M56; NMR; -; A=12-415.
DR PDB; 2QBL; X-ray; 1.80 A; A=1-415.
DR PDB; 2QBM; X-ray; 1.80 A; A=1-415.
DR PDB; 2QBN; X-ray; 1.75 A; A=1-415.
DR PDB; 2QBO; X-ray; 1.90 A; A=1-415.
DR PDB; 2Z97; X-ray; 1.80 A; A=1-415.
DR PDB; 2ZAW; X-ray; 1.55 A; A=1-415.
DR PDB; 2ZAX; X-ray; 1.60 A; A=1-415.
DR PDB; 2ZUH; X-ray; 1.55 A; A=1-415.
DR PDB; 2ZUI; X-ray; 1.50 A; A=1-415.
DR PDB; 2ZUJ; X-ray; 1.60 A; A=1-415.
DR PDB; 2ZWT; X-ray; 1.35 A; A=1-415.
DR PDB; 2ZWU; X-ray; 1.30 A; A=1-415.
DR PDB; 3CP4; X-ray; 2.30 A; A=2-415.
DR PDB; 3CPP; X-ray; 1.90 A; A=2-415.
DR PDB; 3FWF; X-ray; 1.83 A; A/B=11-415.
DR PDB; 3FWG; X-ray; 1.55 A; A/B=11-415.
DR PDB; 3FWI; X-ray; 2.40 A; A=11-415.
DR PDB; 3FWJ; X-ray; 1.90 A; A=11-415.
DR PDB; 3L61; X-ray; 1.50 A; A=2-415.
DR PDB; 3L62; X-ray; 1.70 A; A=2-415.
DR PDB; 3L63; X-ray; 1.50 A; A=2-415.
DR PDB; 3OIA; X-ray; 1.65 A; A=2-415.
DR PDB; 3OL5; X-ray; 1.75 A; A=2-415.
DR PDB; 3P6M; X-ray; 2.00 A; A=2-415.
DR PDB; 3P6N; X-ray; 1.70 A; A=2-415.
DR PDB; 3P6O; X-ray; 2.00 A; A=2-415.
DR PDB; 3P6P; X-ray; 1.90 A; A=2-415.
DR PDB; 3P6Q; X-ray; 1.95 A; A=2-415.
DR PDB; 3P6R; X-ray; 2.10 A; A=2-415.
DR PDB; 3P6S; X-ray; 2.00 A; A=2-415.
DR PDB; 3P6T; X-ray; 1.90 A; A=2-415.
DR PDB; 3P6U; X-ray; 1.70 A; A=2-415.
DR PDB; 3P6V; X-ray; 2.00 A; A=2-415.
DR PDB; 3P6W; X-ray; 2.10 A; A=2-415.
DR PDB; 3P6X; X-ray; 1.65 A; A=2-415.
DR PDB; 3W9C; X-ray; 2.50 A; A=2-415.
DR PDB; 3WRH; X-ray; 1.62 A; A/E=1-415.
DR PDB; 3WRI; X-ray; 2.90 A; A/B=1-415.
DR PDB; 3WRJ; X-ray; 1.85 A; A/E=1-415.
DR PDB; 3WRK; X-ray; 2.61 A; A/D=1-415.
DR PDB; 3WRL; X-ray; 1.65 A; A/E=1-415.
DR PDB; 3WRM; X-ray; 1.95 A; A/F=1-415.
DR PDB; 4CP4; X-ray; 2.10 A; A=2-415.
DR PDB; 4CPP; X-ray; 2.11 A; A=2-415.
DR PDB; 4EK1; X-ray; 1.97 A; A/B=2-415.
DR PDB; 4G3R; X-ray; 2.20 A; A/B=2-415.
DR PDB; 4JWS; X-ray; 2.15 A; A/B=1-415.
DR PDB; 4JWU; X-ray; 2.20 A; A/B=1-415.
DR PDB; 4JX1; X-ray; 2.09 A; A/B/E/F=1-415.
DR PDB; 4KKY; X-ray; 2.00 A; X=2-414.
DR PDB; 4L49; X-ray; 2.13 A; A=1-415.
DR PDB; 4L4A; X-ray; 2.10 A; A=1-415.
DR PDB; 4L4B; X-ray; 2.10 A; A=1-415.
DR PDB; 4L4C; X-ray; 2.20 A; A/B=1-415.
DR PDB; 4L4D; X-ray; 2.10 A; A=1-415.
DR PDB; 4L4E; X-ray; 1.26 A; A=1-415.
DR PDB; 4L4F; X-ray; 1.29 A; A=1-415.
DR PDB; 4L4G; X-ray; 1.55 A; A=1-415.
DR PDB; 5CP4; X-ray; 1.75 A; A=2-415.
DR PDB; 5CPP; X-ray; 2.08 A; A=2-415.
DR PDB; 5GXG; X-ray; 1.70 A; A=2-415.
DR PDB; 5IK1; X-ray; 1.53 A; A=10-415.
DR PDB; 5WK7; X-ray; 1.98 A; A=1-415.
DR PDB; 5WK9; X-ray; 1.98 A; A=1-415.
DR PDB; 6CP4; X-ray; 1.90 A; A=2-415.
DR PDB; 6CPP; X-ray; 1.90 A; A=2-415.
DR PDB; 6NBL; X-ray; 2.15 A; A/B=1-415.
DR PDB; 6WE6; X-ray; 2.16 A; A/B=1-415.
DR PDB; 6WFL; X-ray; 1.60 A; A=1-415.
DR PDB; 7CPP; X-ray; 2.00 A; A=2-415.
DR PDB; 8CPP; X-ray; 2.10 A; A=2-415.
DR PDBsum; 1AKD; -.
DR PDBsum; 1C8J; -.
DR PDBsum; 1CP4; -.
DR PDBsum; 1DZ4; -.
DR PDBsum; 1DZ6; -.
DR PDBsum; 1DZ8; -.
DR PDBsum; 1DZ9; -.
DR PDBsum; 1GEB; -.
DR PDBsum; 1GEK; -.
DR PDBsum; 1GEM; -.
DR PDBsum; 1GJM; -.
DR PDBsum; 1IWI; -.
DR PDBsum; 1IWJ; -.
DR PDBsum; 1IWK; -.
DR PDBsum; 1J51; -.
DR PDBsum; 1K2O; -.
DR PDBsum; 1LWL; -.
DR PDBsum; 1MPW; -.
DR PDBsum; 1NOO; -.
DR PDBsum; 1O76; -.
DR PDBsum; 1P2Y; -.
DR PDBsum; 1P7R; -.
DR PDBsum; 1PHA; -.
DR PDBsum; 1PHB; -.
DR PDBsum; 1PHC; -.
DR PDBsum; 1PHD; -.
DR PDBsum; 1PHE; -.
DR PDBsum; 1PHF; -.
DR PDBsum; 1PHG; -.
DR PDBsum; 1QMQ; -.
DR PDBsum; 1RE9; -.
DR PDBsum; 1RF9; -.
DR PDBsum; 1T85; -.
DR PDBsum; 1T86; -.
DR PDBsum; 1T87; -.
DR PDBsum; 1T88; -.
DR PDBsum; 1UYU; -.
DR PDBsum; 1YRC; -.
DR PDBsum; 1YRD; -.
DR PDBsum; 2A1M; -.
DR PDBsum; 2A1N; -.
DR PDBsum; 2A1O; -.
DR PDBsum; 2CP4; -.
DR PDBsum; 2CPP; -.
DR PDBsum; 2FE6; -.
DR PDBsum; 2FER; -.
DR PDBsum; 2FEU; -.
DR PDBsum; 2FRZ; -.
DR PDBsum; 2GQX; -.
DR PDBsum; 2GR6; -.
DR PDBsum; 2H7Q; -.
DR PDBsum; 2H7R; -.
DR PDBsum; 2H7S; -.
DR PDBsum; 2L8M; -.
DR PDBsum; 2LQD; -.
DR PDBsum; 2M56; -.
DR PDBsum; 2QBL; -.
DR PDBsum; 2QBM; -.
DR PDBsum; 2QBN; -.
DR PDBsum; 2QBO; -.
DR PDBsum; 2Z97; -.
DR PDBsum; 2ZAW; -.
DR PDBsum; 2ZAX; -.
DR PDBsum; 2ZUH; -.
DR PDBsum; 2ZUI; -.
DR PDBsum; 2ZUJ; -.
DR PDBsum; 2ZWT; -.
DR PDBsum; 2ZWU; -.
DR PDBsum; 3CP4; -.
DR PDBsum; 3CPP; -.
DR PDBsum; 3FWF; -.
DR PDBsum; 3FWG; -.
DR PDBsum; 3FWI; -.
DR PDBsum; 3FWJ; -.
DR PDBsum; 3L61; -.
DR PDBsum; 3L62; -.
DR PDBsum; 3L63; -.
DR PDBsum; 3OIA; -.
DR PDBsum; 3OL5; -.
DR PDBsum; 3P6M; -.
DR PDBsum; 3P6N; -.
DR PDBsum; 3P6O; -.
DR PDBsum; 3P6P; -.
DR PDBsum; 3P6Q; -.
DR PDBsum; 3P6R; -.
DR PDBsum; 3P6S; -.
DR PDBsum; 3P6T; -.
DR PDBsum; 3P6U; -.
DR PDBsum; 3P6V; -.
DR PDBsum; 3P6W; -.
DR PDBsum; 3P6X; -.
DR PDBsum; 3W9C; -.
DR PDBsum; 3WRH; -.
DR PDBsum; 3WRI; -.
DR PDBsum; 3WRJ; -.
DR PDBsum; 3WRK; -.
DR PDBsum; 3WRL; -.
DR PDBsum; 3WRM; -.
DR PDBsum; 4CP4; -.
DR PDBsum; 4CPP; -.
DR PDBsum; 4EK1; -.
DR PDBsum; 4G3R; -.
DR PDBsum; 4JWS; -.
DR PDBsum; 4JWU; -.
DR PDBsum; 4JX1; -.
DR PDBsum; 4KKY; -.
DR PDBsum; 4L49; -.
DR PDBsum; 4L4A; -.
DR PDBsum; 4L4B; -.
DR PDBsum; 4L4C; -.
DR PDBsum; 4L4D; -.
DR PDBsum; 4L4E; -.
DR PDBsum; 4L4F; -.
DR PDBsum; 4L4G; -.
DR PDBsum; 5CP4; -.
DR PDBsum; 5CPP; -.
DR PDBsum; 5GXG; -.
DR PDBsum; 5IK1; -.
DR PDBsum; 5WK7; -.
DR PDBsum; 5WK9; -.
DR PDBsum; 6CP4; -.
DR PDBsum; 6CPP; -.
DR PDBsum; 6NBL; -.
DR PDBsum; 6WE6; -.
DR PDBsum; 6WFL; -.
DR PDBsum; 7CPP; -.
DR PDBsum; 8CPP; -.
DR AlphaFoldDB; P00183; -.
DR BMRB; P00183; -.
DR SMR; P00183; -.
DR DIP; DIP-29809N; -.
DR IntAct; P00183; 1.
DR BindingDB; P00183; -.
DR ChEMBL; CHEMBL5594; -.
DR DrugBank; DB03836; 1,3,5-trichlorobenzene.
DR DrugBank; DB02617; 1-(N-Imidazolyl)-2-Hydroxy-2-(2,3-Dichlorophenyl)Octane.
DR DrugBank; DB02817; 5-Exo-Hydroxycamphor.
DR DrugBank; DB03627; Adamantane.
DR DrugBank; DB04032; Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Butyl-Amide.
DR DrugBank; DB03031; Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Octyl-Amide.
DR DrugBank; DB02125; Adamantanone.
DR DrugBank; DB04501; Camphane.
DR DrugBank; DB01744; Camphor.
DR DrugBank; DB01663; lambda-bis(2,2'-bipyridine)-(5-methyl-2-2'-bipyridine)-C9-adamantane ruthenium (II).
DR DrugBank; DB01011; Metyrapone.
DR DrugBank; DB01703; N-(2-ferrocenylethyl)maleimide.
DR DrugBank; DB01826; N-Butyl Isocyanide.
DR DrugBank; DB03540; Norcamphor.
DR DrugBank; DB02851; Thiocamphor.
DR KEGG; ag:AAA25760; -.
DR BioCyc; MetaCyc:MON-3021; -.
DR BRENDA; 1.14.15.1; 5092.
DR UniPathway; UPA00719; -.
DR EvolutionaryTrace; P00183; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018683; F:camphor 5-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019383; P:(+)-camphor catabolic process; IEA:UniProtKB-UniPathway.
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 PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Monooxygenase; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7130171"
FT CHAIN 2..415
FT /note="Camphor 5-monooxygenase"
FT /id="PRO_0000052204"
FT BINDING 358
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 CONFLICT 56..57
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="H -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:4KKY"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2H7S"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1O76"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:4L4E"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1GEK"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:4L4E"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4L4E"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 122..143
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4L4E"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 194..214
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:2H7R"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:4L4E"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 361..378
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3CP4"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:4L4E"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:4L4E"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:4L4E"
SQ SEQUENCE 415 AA; 46669 MW; E84641B4A65DD2D3 CRC64;
MTTETIQSNA NLAPLPPHVP EHLVFDFDMY NPSNLSAGVQ EAWAVLQESN VPDLVWTRCN
GGHWIATRGQ LIREAYEDYR HFSSECPFIP REAGEAYDFI PTSMDPPEQR QFRALANQVV
GMPVVDKLEN RIQELACSLI ESLRPQGQCN FTEDYAEPFP IRIFMLLAGL PEEDIPHLKY
LTDQMTRPDG SMTFAEAKEA LYDYLIPIIE QRRQKPGTDA ISIVANGQVN GRPITSDEAK
RMCGLLLVGG LDTVVNFLSF SMEFLAKSPE HRQELIERPE RIPAACEELL RRFSLVADGR
ILTSDYEFHG VQLKKGDQIL LPQMLSGLDE RENACPMHVD FSRQKVSHTT FGHGSHLCLG
QHLARREIIV TLKEWLTRIP DFSIAPGAQI QHKSGIVSGV QALPLVWDPA TTKAV
