Reviewed, UniProtKB/Swiss-Prot P00183 (CPXA_PSEPU)

Names and origin

Protein names

Recommended name:
    Camphor 5-monooxygenase
    EC=1.14.15.1
Alternative name(s):
    Cytochrome P450-cam
      Short name=P450cam

Gene names

Name:	camC
Synonyms:	cyp101

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in a camphor oxidation system.
Catalytic activity	+-camphor + 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 component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	camphor 5-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 415

414

Camphor 5-monooxygenase

PRO_0000052204

Sites

Metal binding

358

1

Iron (heme axial ligand)

Experimental info

Sequence conflict

56 – 57

2

Missing AA sequence Ref.3

Sequence conflict

277

1

E → Q AA sequence Ref.3

Sequence conflict

362

1

H → S AA sequence Ref.3

Sequence conflict

408

1

D → N AA sequence Ref.3

Secondary structure

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415

Helix Strand Turn

Details...

Helix

21 – 23

3

Helix

35 – 37

3

Helix

39 – 43

5

Helix

44 – 47

4

Beta strand

53 – 57

5

Helix

59 – 61

3

Beta strand

63 – 66

4

Helix

69 – 77

9

Turn

79 – 81

3

Beta strand

88 – 90

3

Helix

91 – 96

6

Turn

100 – 103

4

Turn

106 – 108

3

Helix

109 – 120

12

Helix

122 – 143

22

Helix

144 – 146

3

Beta strand

147 – 150

4

Helix

151 – 154

4

Turn

155 – 157

3

Helix

158 – 167

10

Helix

172 – 174

3

Helix

175 – 186

12

Beta strand

190 – 192

3

Helix

194 – 214

21

Helix

220 – 225

6

Helix

236 – 248

13

Turn

249 – 251

3

Helix

252 – 267

16

Helix

269 – 277

9

Helix

279 – 281

3

Helix

282 – 292

11

Beta strand

299 – 304

6

Beta strand

306 – 308

3

Beta strand

311 – 313

3

Beta strand

318 – 320

3

Helix

323 – 328

6

Turn

330 – 332

3

Beta strand

333 – 335

3

Helix

354 – 356

3

Helix

361 – 378

18

Beta strand

395 – 397

3

Beta strand

399 – 401

3

Beta strand

404 – 406

3

Helix

409 – 411

3

Sequences

	Sequence		Length	Mass (Da)
	P00183-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E84641B4A65DD2D3	FASTA	415	46,669
	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

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: 3003058] [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: 2613690] [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: 7130171] [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: 3813557] [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: 2578028] [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: 1610873] [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: 12237225] [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: 4066706] [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: 9357977] [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: 9649301] [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: 10557259] [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: 10698731] [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: 11098139] [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: 11258878] [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: 11606730] [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: 12464241] [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: 9315686] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M12546 Genomic DNA. Translation: AAA25760.1.
D00528 Genomic DNA. Translation: BAA00412.1.

PIR

O4PSCP. A25660.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AKD	X-ray	1.80	A	2-415	[»]
1C8J	X-ray	2.10	A/B	2-415	[»]
1CP4	X-ray	1.90	A	2-414	[»]
1DZ4	X-ray	1.60	A/B	2-415	[»]
1DZ6	X-ray	1.90	A/B	2-415	[»]
1DZ8	X-ray	1.90	A/B	2-415	[»]
1DZ9	X-ray	1.90	A/B	2-415	[»]
1GEB	X-ray	2.03	A	1-415	[»]
1GEK	X-ray	1.70	A	1-415	[»]
1GEM	X-ray	2.00	A	1-415	[»]
1GJM	X-ray	2.20	A	2-415	[»]
1IWI	X-ray	2.00	A	1-415	[»]
1IWJ	X-ray	2.00	A	1-415	[»]
1IWK	X-ray	2.00	A	1-415	[»]
1J51	X-ray	2.20	A/B/C/D	2-414	[»]
1K2O	X-ray	1.65	A/B	2-415	[»]
1LWL	X-ray	2.20	A	1-415	[»]
1MPW	X-ray	2.34	A/B	2-414	[»]
1NOO	X-ray	2.20	A	2-415	[»]
1O76	X-ray	1.80	A/B	2-415	[»]
1P2Y	X-ray	2.30	A	2-414	[»]
1P7R	X-ray	2.85	A	2-414	[»]
1PHA	X-ray	1.63	A	2-414	[»]
1PHB	X-ray	1.60	A	2-414	[»]
1PHC	X-ray	1.60	A	2-414	[»]
1PHD	X-ray	1.60	A	2-414	[»]
1PHE	X-ray	1.60	A	2-414	[»]
1PHF	X-ray	1.60	A	2-414	[»]
1PHG	X-ray	1.60	A	2-414	[»]
1QMQ	X-ray	1.55	A	2-415	[»]
1RE9	X-ray	1.45	A	2-414	[»]
1RF9	X-ray	1.80	A	1-415	[»]
1T85	X-ray	1.80	A	2-414	[»]
1T86	X-ray	1.90	A/B	2-414	[»]
1T87	X-ray	1.80	A/B	2-414	[»]
1T88	X-ray	1.90	A/B	2-414	[»]
1UYU	X-ray	2.00	A/B	2-414	[»]
1YRC	X-ray	1.40	A	2-414	[»]
1YRD	X-ray	1.70	A	2-414	[»]
2A1M	X-ray	2.10	A/B	1-415	[»]
2A1N	X-ray	1.90	A/B	1-415	[»]
2A1O	X-ray	1.55	A/B	1-415	[»]
2CP4	X-ray	2.10	A	2-414	[»]
2CPP	X-ray	1.63	A	2-414	[»]
2FE6	X-ray	1.50	A	1-415	[»]
2FER	X-ray	1.70	A	11-415	[»]
2FEU	X-ray	1.70	A/B	11-415	[»]
2FRZ	X-ray	2.10	A/B	2-415	[»]
2GQX	X-ray	2.10	A/B	11-415	[»]
2GR6	X-ray	2.30	A/B	11-415	[»]
2H7Q	X-ray	1.50	A	2-414	[»]
2H7R	X-ray	2.10	A	2-414	[»]
2H7S	X-ray	2.15	A/C	2-414	[»]
2QBL	X-ray	1.80	A	1-415	[»]
2QBM	X-ray	1.80	A	1-415	[»]
2QBN	X-ray	1.75	A	1-415	[»]
2QBO	X-ray	1.90	A	1-415	[»]
2Z97	X-ray	1.80	A	1-415	[»]
2ZAW	X-ray	1.55	A	1-415	[»]
2ZAX	X-ray	1.60	A	1-415	[»]
2ZWT	X-ray	1.35	A	1-415	[»]
2ZWU	X-ray	1.30	A	1-415	[»]
3CP4	X-ray	2.30	A	2-414	[»]
3CPP	X-ray	1.90	A	2-414	[»]
3FWF	X-ray	1.83	A/B	11-415	[»]
3FWG	X-ray	1.55	A/B	11-415	[»]
3FWI	X-ray	2.40	A	11-415	[»]
3FWJ	X-ray	1.90	A	11-415	[»]
4CP4	X-ray	2.10	A	2-414	[»]
4CPP	X-ray	2.11	A	2-414	[»]
5CP4	X-ray	1.75	A	2-415	[»]
5CPP	X-ray	2.08	A	2-414	[»]
6CP4	X-ray	1.90	A	2-415	[»]
6CPP	X-ray	1.90	A	2-414	[»]
7CPP	X-ray	2.00	A	2-414	[»]
8CPP	X-ray	2.10	A	2-414	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3021.

BRENDA

1.14.15.1. 403.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

PANTHER

PTHR19383. Cyt_P450. 1 hit.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00359. BP450.
PR00385. P450.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01011. Metyrapone.
DB00184. Nicotine.

Entry information

Entry name

CPXA_PSEPU

Accession

Primary (citable) accession number: P00183

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)