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P00183 (CPXA_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Camphor 5-monooxygenase

EC=1.14.15.1
Alternative name(s):
Cytochrome P450-cam
Short name=Cytochrome P450cam
Gene names
Name:camC
Synonyms:cyp101
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in a camphor oxidation system.

Catalytic activity

+-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O.

Cofactor

Heme group.

Pathway

Terpene metabolism; (R)-camphor degradation.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_process(+)-camphor catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncamphor 5-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 415414Camphor 5-monooxygenase
PRO_0000052204

Sites

Metal binding3581Iron (heme axial ligand)

Experimental info

Sequence conflict56 – 572Missing AA sequence Ref.3
Sequence conflict2771E → Q AA sequence Ref.3
Sequence conflict3621H → S AA sequence Ref.3
Sequence conflict4081D → N AA sequence Ref.3

Secondary structure

.................................................................................... 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00183 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E84641B4A65DD2D3

FASTA41546,669
        10         20         30         40         50         60 
MTTETIQSNA NLAPLPPHVP EHLVFDFDMY NPSNLSAGVQ EAWAVLQESN VPDLVWTRCN 

        70         80         90        100        110        120 
GGHWIATRGQ LIREAYEDYR HFSSECPFIP REAGEAYDFI PTSMDPPEQR QFRALANQVV 

       130        140        150        160        170        180 
GMPVVDKLEN RIQELACSLI ESLRPQGQCN FTEDYAEPFP IRIFMLLAGL PEEDIPHLKY 

       190        200        210        220        230        240 
LTDQMTRPDG SMTFAEAKEA LYDYLIPIIE QRRQKPGTDA ISIVANGQVN GRPITSDEAK 

       250        260        270        280        290        300 
RMCGLLLVGG LDTVVNFLSF SMEFLAKSPE HRQELIERPE RIPAACEELL RRFSLVADGR 

       310        320        330        340        350        360 
ILTSDYEFHG VQLKKGDQIL LPQMLSGLDE RENACPMHVD FSRQKVSHTT FGHGSHLCLG 

       370        380        390        400        410 
QHLARREIIV TLKEWLTRIP DFSIAPGAQI QHKSGIVSGV QALPLVWDPA TTKAV 

« Hide

References

[1]"Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli."
Unger B.P., Gunsalus I.C., Sligar S.G.
J. Biol. Chem. 261:1158-1163(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G1 / ATCC 17453.
[2]"Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida."
Koga H., Yamaguchi E., Matsunaga K., Aramaki H., Horiuchi T.
J. Biochem. 106:831-836(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 386-415.
Strain: G1 / ATCC 17453.
[3]"Amino acid sequence of the Pseudomonas putida cytochrome P-450. II. Cyanogen bromide peptides, acid cleavage peptides, and the complete sequence."
Haniu M., Armes L.G., Yasunobu K.T., Shastry B.A., Gunsalus I.C.
J. Biol. Chem. 257:12664-12671(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-415.
[4]"P-450 binding to substrates camphor and linalool versus pressure."
Marden M.C., Hui Bon Hoa G.
Arch. Biochem. Biophys. 253:100-107(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ABSORPTION SPECTROSCOPY.
[5]"Dynamic behavior of the active site structure in bacterial cytochrome P-450."
Jung C., Marlow F.
Studia Biophys. 120:241-251(1987)
Cited for: FOURIER-TRANSFORM INFRARED SPECTROSCOPY.
[6]"Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure."
Hui Bon Hoa G., Di Primo C., Dondaine I., Sligar S.G., Gunsalus I.C., Douzou P.
Biochemistry 28:651-656(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ABSORPTION SPECTROSCOPY, FLUORESCENCE SPECTROSCOPY.
[7]"Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450."
Nolting B., Jung C., Snatzke G.
Biochim. Biophys. Acta 1100:171-176(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CIRCULAR DICHROISM ANALYSIS.
[8]"Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin."
Deprez E., Gill E., Helms V., Wade R., Hui Bon Hoa G.
J. Inorg. Biochem. 91:597-606(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE-PROTEIN INTERACTION.
[9]"The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450."
Poulos T.L., Finzel B.C., Gunsalus I.C., Wagner G.C., Kraut J.
J. Biol. Chem. 260:16122-16130(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[10]"Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer."
Schlichting I., Jung C., Schulze H.
FEBS Lett. 415:253-257(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[11]"Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein."
Di Gleria K., Nickerson D.P., Hill H.A.O., Wong L.-L., Fueloep V.
J. Am. Chem. Soc. 120:46-52(1998)
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[12]"Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect."
Vidakovic M., Sligar S.G., Li H., Poulos T.L.
Biochemistry 37:9211-9219(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[13]"Optical detection of cytochrome P450 by sensitizer-linked substrates."
Dmochowski I.J., Crane B.R., Wilker J.J., Winkler J.R., Gray H.B.
Proc. Natl. Acad. Sci. U.S.A. 96:12987-12990(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
[14]"The catalytic pathway of cytochrome p450cam at atomic resolution."
Schlichting I., Berendzen J., Chu K., Stock A.M., Maves S.A., Benson D.E., Sweet R.M., Ringe D., Petsko G.A., Sligar S.G.
Science 287:1615-1622(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[15]"X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center."
Hishiki T., Shimada H., Nagano S., Egawa T., Kanamori Y., Makino R., Park S.-Y., Adachi S., Shiro Y., Ishimura Y.
J. Biochem. 128:965-974(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
[16]"Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam."
Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y.
Biochemistry 40:2669-2677(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[17]"Probing the open state of cytochrome P450cam with ruthenium-linker substrates."
Dunn A.R., Dmochowski I.J., Bilwes A.M., Gray H.B., Crane B.R.
Proc. Natl. Acad. Sci. U.S.A. 98:12420-12425(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[18]"Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase -- structural models of the short-lived oxygen complexes."
Fedorov R., Ghosh D.K., Schlichting I.
Arch. Biochem. Biophys. 409:25-31(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[19]"1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton."
Mouro C., Bondon A., Simmoneaux G., Jung C.
FEBS Lett. 414:203-208(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12546 Genomic DNA. Translation: AAA25760.1.
D00528 Genomic DNA. Translation: BAA00412.1.
PIRO4PSCP. A25660.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKDX-ray1.80A2-415[»]
1C8JX-ray2.10A/B2-415[»]
1CP4X-ray1.90A2-414[»]
1DZ4X-ray1.60A/B2-415[»]
1DZ6X-ray1.90A/B2-415[»]
1DZ8X-ray1.90A/B2-415[»]
1DZ9X-ray1.90A/B2-415[»]
1GEBX-ray2.03A1-415[»]
1GEKX-ray1.70A1-415[»]
1GEMX-ray2.00A1-415[»]
1GJMX-ray2.20A2-415[»]
1IWIX-ray2.00A1-415[»]
1IWJX-ray2.00A1-415[»]
1IWKX-ray2.00A1-415[»]
1J51X-ray2.20A/B/C/D2-414[»]
1K2OX-ray1.65A/B2-415[»]
1LWLX-ray2.20A1-415[»]
1MPWX-ray2.34A/B2-414[»]
1NOOX-ray2.20A2-415[»]
1O76X-ray1.80A/B2-415[»]
1P2YX-ray2.30A2-414[»]
1P7RX-ray2.85A2-414[»]
1PHAX-ray1.63A2-414[»]
1PHBX-ray1.60A2-414[»]
1PHCX-ray1.60A2-414[»]
1PHDX-ray1.60A2-414[»]
1PHEX-ray1.60A2-414[»]
1PHFX-ray1.60A2-414[»]
1PHGX-ray1.60A2-414[»]
1QMQX-ray1.55A2-415[»]
1RE9X-ray1.45A2-414[»]
1RF9X-ray1.80A1-415[»]
1T85X-ray1.80A2-414[»]
1T86X-ray1.90A/B2-414[»]
1T87X-ray1.80A/B2-414[»]
1T88X-ray1.90A/B2-414[»]
1UYUX-ray2.00A/B2-415[»]
1YRCX-ray1.40A2-414[»]
1YRDX-ray1.70A2-414[»]
2A1MX-ray2.10A/B1-415[»]
2A1NX-ray1.90A/B1-415[»]
2A1OX-ray1.55A/B1-415[»]
2CP4X-ray2.10A2-414[»]
2CPPX-ray1.63A2-414[»]
2FE6X-ray1.50A1-415[»]
2FERX-ray1.70A11-415[»]
2FEUX-ray1.70A/B11-415[»]
2FRZX-ray2.10A/B2-415[»]
2GQXX-ray2.10A/B11-415[»]
2GR6X-ray2.30A/B11-415[»]
2H7QX-ray1.50A2-414[»]
2H7RX-ray2.10A2-414[»]
2H7SX-ray2.15A/C2-414[»]
2L8MNMR-A1-415[»]
2LQDNMR-A11-415[»]
2M56NMR-A12-415[»]
2QBLX-ray1.80A1-415[»]
2QBMX-ray1.80A1-415[»]
2QBNX-ray1.75A1-415[»]
2QBOX-ray1.90A1-415[»]
2Z97X-ray1.80A1-415[»]
2ZAWX-ray1.55A1-415[»]
2ZAXX-ray1.60A1-415[»]
2ZUHX-ray1.55A1-415[»]
2ZUIX-ray1.50A1-415[»]
2ZUJX-ray1.60A1-415[»]
2ZWTX-ray1.35A1-415[»]
2ZWUX-ray1.30A1-415[»]
3CP4X-ray2.30A2-414[»]
3CPPX-ray1.90A2-414[»]
3FWFX-ray1.83A/B11-415[»]
3FWGX-ray1.55A/B11-415[»]
3FWIX-ray2.40A11-415[»]
3FWJX-ray1.90A11-415[»]
3L61X-ray1.50A2-415[»]
3L62X-ray1.70A2-415[»]
3L63X-ray1.50A2-415[»]
3OIAX-ray1.65A2-415[»]
3OL5X-ray1.75A2-415[»]
3P6MX-ray2.00A2-415[»]
3P6NX-ray1.70A2-415[»]
3P6OX-ray2.00A2-415[»]
3P6PX-ray1.90A2-415[»]
3P6QX-ray1.95A2-415[»]
3P6RX-ray2.10A2-415[»]
3P6SX-ray2.00A2-415[»]
3P6TX-ray1.90A2-415[»]
3P6UX-ray1.70A2-415[»]
3P6VX-ray2.00A2-415[»]
3P6WX-ray2.10A2-415[»]
3P6XX-ray1.65A2-415[»]
3W9CX-ray2.50A2-415[»]
4CP4X-ray2.10A2-414[»]
4CPPX-ray2.11A2-414[»]
4EK1X-ray1.97A/B2-415[»]
4G3RX-ray2.20A/B2-415[»]
4JWSX-ray2.15A/B1-415[»]
4JWUX-ray2.20A/B1-415[»]
4JX1X-ray2.09A/B/E/F1-415[»]
4L49X-ray2.13A1-415[»]
4L4AX-ray2.10A1-415[»]
4L4BX-ray2.10A1-415[»]
4L4CX-ray2.20A/B1-415[»]
4L4DX-ray2.10A1-415[»]
4L4EX-ray1.26A1-415[»]
4L4FX-ray1.29A1-415[»]
4L4GX-ray1.55A1-415[»]
5CP4X-ray1.75A2-415[»]
5CPPX-ray2.08A2-414[»]
6CP4X-ray1.90A2-415[»]
6CPPX-ray1.90A2-414[»]
7CPPX-ray2.00A2-414[»]
8CPPX-ray2.10A2-414[»]
ProteinModelPortalP00183.
SMRP00183. Positions 10-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29809N.

Chemistry

BindingDBP00183.
ChEMBLCHEMBL5594.
DrugBankDB01011. Metyrapone.
DB00184. Nicotine.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3021.
UniPathwayUPA00719.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00359. BP450.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00183.

Entry information

Entry nameCPXA_PSEPU
AccessionPrimary (citable) accession number: P00183
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 22, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways