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 13-SEP-2023, entry version 167. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:MONOMER-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 CDD; cd11035; P450cam-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1. DR PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00359; BP450. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 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 //