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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi358 – 3581Iron (heme axial ligand)

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

ChEMBLiCHEMBL5594.
DrugBankiDB01744. Camphor.
DB01011. Metyrapone.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 415414Camphor 5-monooxygenasePRO_0000052204Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-29809N.

Chemistry

BindingDBiP00183.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83Combined sources
Helixi21 – 233Combined sources
Beta strandi29 – 313Combined sources
Helixi35 – 373Combined sources
Helixi39 – 435Combined sources
Helixi44 – 474Combined sources
Beta strandi48 – 514Combined sources
Beta strandi53 – 575Combined sources
Helixi59 – 613Combined sources
Beta strandi63 – 664Combined sources
Helixi69 – 779Combined sources
Turni79 – 813Combined sources
Beta strandi82 – 865Combined sources
Beta strandi88 – 903Combined sources
Helixi91 – 966Combined sources
Turni100 – 1034Combined sources
Turni106 – 1083Combined sources
Helixi109 – 12012Combined sources
Helixi122 – 14322Combined sources
Helixi144 – 1463Combined sources
Beta strandi147 – 1504Combined sources
Helixi151 – 1544Combined sources
Turni155 – 1573Combined sources
Helixi158 – 16811Combined sources
Helixi172 – 1743Combined sources
Helixi175 – 18612Combined sources
Beta strandi190 – 1923Combined sources
Helixi194 – 21421Combined sources
Helixi220 – 2256Combined sources
Beta strandi230 – 2334Combined sources
Helixi236 – 25116Combined sources
Helixi253 – 26614Combined sources
Helixi269 – 2779Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 29211Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi306 – 3083Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi318 – 3214Combined sources
Helixi323 – 3286Combined sources
Turni330 – 3323Combined sources
Beta strandi333 – 3353Combined sources
Helixi354 – 3563Combined sources
Helixi361 – 37818Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi399 – 4013Combined sources
Beta strandi404 – 4063Combined sources
Helixi409 – 4113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 10-415.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 572Missing AA sequence (PubMed:7130171).Curated
Sequence conflicti277 – 2771E → Q AA sequence (PubMed:7130171).Curated
Sequence conflicti362 – 3621H → S AA sequence (PubMed:7130171).Curated
Sequence conflicti408 – 4081D → N AA sequence (PubMed:7130171).Curated

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
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. Positions 10-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29809N.

Chemistry

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: July 6, 2016
This is version 142 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.