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Protein

Camphor 5-monooxygenase

Gene

camC

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in a camphor oxidation system.

Catalytic activityi

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

Cofactori

Pathwayi: (R)-camphor degradation

This protein is involved in the pathway (R)-camphor degradation, which is part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the pathway (R)-camphor degradation and in Terpene metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi358Iron (heme axial ligand)1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3021.
BRENDAi1.14.15.1. 5092.
UniPathwayiUPA00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Camphor 5-monooxygenase (EC:1.14.15.1)
Alternative name(s):
Cytochrome P450-cam
Short name:
Cytochrome P450cam
Gene namesi
Name:camC
Synonyms:cyp101
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5594.
DrugBankiDB01744. Camphor.
DB01011. Metyrapone.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000522042 – 415Camphor 5-monooxygenaseAdd BLAST414

Interactioni

Protein-protein interaction databases

DIPiDIP-29809N.

Chemistry databases

BindingDBiP00183.

Structurei

Secondary structure

1415
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni6 – 8Combined sources3
Helixi21 – 23Combined sources3
Beta strandi29 – 31Combined sources3
Helixi35 – 37Combined sources3
Helixi39 – 43Combined sources5
Helixi44 – 47Combined sources4
Beta strandi48 – 51Combined sources4
Beta strandi53 – 57Combined sources5
Helixi59 – 61Combined sources3
Beta strandi63 – 66Combined sources4
Helixi69 – 77Combined sources9
Turni79 – 81Combined sources3
Beta strandi82 – 86Combined sources5
Beta strandi88 – 90Combined sources3
Helixi91 – 96Combined sources6
Turni100 – 103Combined sources4
Turni106 – 108Combined sources3
Helixi109 – 120Combined sources12
Helixi122 – 143Combined sources22
Helixi144 – 146Combined sources3
Beta strandi147 – 150Combined sources4
Helixi151 – 154Combined sources4
Turni155 – 157Combined sources3
Helixi158 – 168Combined sources11
Helixi172 – 174Combined sources3
Helixi175 – 186Combined sources12
Beta strandi190 – 192Combined sources3
Helixi194 – 214Combined sources21
Helixi220 – 225Combined sources6
Beta strandi230 – 233Combined sources4
Helixi236 – 251Combined sources16
Helixi253 – 266Combined sources14
Helixi269 – 277Combined sources9
Helixi279 – 281Combined sources3
Helixi282 – 292Combined sources11
Beta strandi298 – 304Combined sources7
Beta strandi306 – 308Combined sources3
Beta strandi311 – 313Combined sources3
Beta strandi318 – 321Combined sources4
Helixi323 – 328Combined sources6
Turni330 – 332Combined sources3
Beta strandi333 – 335Combined sources3
Helixi354 – 356Combined sources3
Helixi361 – 378Combined sources18
Beta strandi382 – 384Combined sources3
Beta strandi395 – 397Combined sources3
Beta strandi399 – 401Combined sources3
Beta strandi404 – 406Combined sources3
Helixi409 – 411Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKDX-ray1.80A2-415[»]
1C8JX-ray2.10A/B2-415[»]
1CP4X-ray1.90A2-415[»]
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/D2-415[»]
1K2OX-ray1.65A/B2-415[»]
1LWLX-ray2.20A1-415[»]
1MPWX-ray2.34A/B2-415[»]
1NOOX-ray2.20A2-415[»]
1O76X-ray1.80A/B2-415[»]
1P2YX-ray2.30A2-415[»]
1P7RX-ray2.85A2-415[»]
1PHAX-ray1.63A2-415[»]
1PHBX-ray1.60A2-415[»]
1PHCX-ray1.60A2-415[»]
1PHDX-ray1.60A2-415[»]
1PHEX-ray1.60A2-415[»]
1PHFX-ray1.60A2-415[»]
1PHGX-ray1.60A2-415[»]
1QMQX-ray1.55A2-415[»]
1RE9X-ray1.45A2-415[»]
1RF9X-ray1.80A1-415[»]
1T85X-ray1.80A2-415[»]
1T86X-ray1.90A/B2-415[»]
1T87X-ray1.80A/B2-415[»]
1T88X-ray1.90A/B2-415[»]
1UYUX-ray2.00A/B2-415[»]
1YRCX-ray1.40A2-415[»]
1YRDX-ray1.70A2-415[»]
2A1MX-ray2.10A/B1-415[»]
2A1NX-ray1.90A/B1-415[»]
2A1OX-ray1.55A/B1-415[»]
2CP4X-ray2.10A2-415[»]
2CPPX-ray1.63A2-415[»]
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-ray1.50A2-415[»]
2H7RX-ray2.10A2-415[»]
2H7SX-ray2.15A/C2-415[»]
2L8MNMR-A1-415[»]
2LQDNMR-A3-415[»]
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-ray2.30A2-415[»]
3CPPX-ray1.90A2-415[»]
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[»]
3WRHX-ray1.62A/E1-415[»]
3WRIX-ray2.90A/B1-415[»]
3WRJX-ray1.85A/E1-415[»]
3WRKX-ray2.61A/D1-415[»]
3WRLX-ray1.65A/E1-415[»]
3WRMX-ray1.95A/F1-415[»]
4CP4X-ray2.10A2-415[»]
4CPPX-ray2.11A2-415[»]
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[»]
4KKYX-ray2.00X2-414[»]
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-ray2.08A2-415[»]
5IK1X-ray1.53A10-415[»]
6CP4X-ray1.90A2-415[»]
6CPPX-ray1.90A2-415[»]
7CPPX-ray2.00A2-415[»]
8CPPX-ray2.10A2-415[»]
ProteinModelPortaliP00183.
SMRiP00183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00183.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00359. BP450.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00183-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTETIQSNA NLAPLPPHVP EHLVFDFDMY NPSNLSAGVQ EAWAVLQESN
60 70 80 90 100
VPDLVWTRCN GGHWIATRGQ LIREAYEDYR HFSSECPFIP REAGEAYDFI
110 120 130 140 150
PTSMDPPEQR QFRALANQVV GMPVVDKLEN RIQELACSLI ESLRPQGQCN
160 170 180 190 200
FTEDYAEPFP IRIFMLLAGL PEEDIPHLKY LTDQMTRPDG SMTFAEAKEA
210 220 230 240 250
LYDYLIPIIE QRRQKPGTDA ISIVANGQVN GRPITSDEAK RMCGLLLVGG
260 270 280 290 300
LDTVVNFLSF SMEFLAKSPE HRQELIERPE RIPAACEELL RRFSLVADGR
310 320 330 340 350
ILTSDYEFHG VQLKKGDQIL LPQMLSGLDE RENACPMHVD FSRQKVSHTT
360 370 380 390 400
FGHGSHLCLG QHLARREIIV TLKEWLTRIP DFSIAPGAQI QHKSGIVSGV
410
QALPLVWDPA TTKAV
Length:415
Mass (Da):46,669
Last modified:January 23, 2007 - v2
Checksum:iE84641B4A65DD2D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56 – 57Missing AA sequence (PubMed:7130171).Curated2
Sequence conflicti277E → Q AA sequence (PubMed:7130171).Curated1
Sequence conflicti362H → S AA sequence (PubMed:7130171).Curated1
Sequence conflicti408D → N AA sequence (PubMed:7130171).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12546 Genomic DNA. Translation: AAA25760.1.
D00528 Genomic DNA. Translation: BAA00412.1.
PIRiA25660. O4PSCP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12546 Genomic DNA. Translation: AAA25760.1.
D00528 Genomic DNA. Translation: BAA00412.1.
PIRiA25660. O4PSCP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKDX-ray1.80A2-415[»]
1C8JX-ray2.10A/B2-415[»]
1CP4X-ray1.90A2-415[»]
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/D2-415[»]
1K2OX-ray1.65A/B2-415[»]
1LWLX-ray2.20A1-415[»]
1MPWX-ray2.34A/B2-415[»]
1NOOX-ray2.20A2-415[»]
1O76X-ray1.80A/B2-415[»]
1P2YX-ray2.30A2-415[»]
1P7RX-ray2.85A2-415[»]
1PHAX-ray1.63A2-415[»]
1PHBX-ray1.60A2-415[»]
1PHCX-ray1.60A2-415[»]
1PHDX-ray1.60A2-415[»]
1PHEX-ray1.60A2-415[»]
1PHFX-ray1.60A2-415[»]
1PHGX-ray1.60A2-415[»]
1QMQX-ray1.55A2-415[»]
1RE9X-ray1.45A2-415[»]
1RF9X-ray1.80A1-415[»]
1T85X-ray1.80A2-415[»]
1T86X-ray1.90A/B2-415[»]
1T87X-ray1.80A/B2-415[»]
1T88X-ray1.90A/B2-415[»]
1UYUX-ray2.00A/B2-415[»]
1YRCX-ray1.40A2-415[»]
1YRDX-ray1.70A2-415[»]
2A1MX-ray2.10A/B1-415[»]
2A1NX-ray1.90A/B1-415[»]
2A1OX-ray1.55A/B1-415[»]
2CP4X-ray2.10A2-415[»]
2CPPX-ray1.63A2-415[»]
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-ray1.50A2-415[»]
2H7RX-ray2.10A2-415[»]
2H7SX-ray2.15A/C2-415[»]
2L8MNMR-A1-415[»]
2LQDNMR-A3-415[»]
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-ray2.30A2-415[»]
3CPPX-ray1.90A2-415[»]
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[»]
3WRHX-ray1.62A/E1-415[»]
3WRIX-ray2.90A/B1-415[»]
3WRJX-ray1.85A/E1-415[»]
3WRKX-ray2.61A/D1-415[»]
3WRLX-ray1.65A/E1-415[»]
3WRMX-ray1.95A/F1-415[»]
4CP4X-ray2.10A2-415[»]
4CPPX-ray2.11A2-415[»]
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[»]
4KKYX-ray2.00X2-414[»]
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-ray2.08A2-415[»]
5IK1X-ray1.53A10-415[»]
6CP4X-ray1.90A2-415[»]
6CPPX-ray1.90A2-415[»]
7CPPX-ray2.00A2-415[»]
8CPPX-ray2.10A2-415[»]
ProteinModelPortaliP00183.
SMRiP00183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29809N.

Chemistry databases

BindingDBiP00183.
ChEMBLiCHEMBL5594.
DrugBankiDB01744. Camphor.
DB01011. Metyrapone.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00719.
BioCyciMetaCyc:MONOMER-3021.
BRENDAi1.14.15.1. 5092.

Miscellaneous databases

EvolutionaryTraceiP00183.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00359. BP450.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCPXA_PSEPU
AccessioniPrimary (citable) accession number: P00183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.