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Protein

6-oxocamphor hydrolase

Gene

camK

Organism
Rhodococcus sp.
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the carbon-carbon bond cleavage of the bicyclic beta-diketone 6-oxocamphor via a retro-Claisen reaction to yield the optically active (2R,4S)-beta-campholinic acid. It is also able to cleave 2,2-disubstituted cyclohexa-1,3-diones such as 2-methyl-2-propylcyclohexa-1,3-dione and 2-methyl-2-butylcyclohexa-1,3-dione which result in racemic keto acid products. Transformations of the bicyclic diketone substrates bicyclo[2.2.1]heptane 2,6-dione and bicyclo[2.2.2]octane-2,6-dione yield (S)-keto acid products.2 Publications

Catalytic activityi

Bornane-2,6-dione + H2O = ((1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl)acetate.1 Publication

Activity regulationi

Inhibited by copper and mercury ions. Also inhibited by thiol active reagents, such as N-ethylmaleimide and hydroxymercuribenzoate. EDTA has a slight activating effect.1 Publication

Kineticsi

Kcat is 167 sec(-1) with 6-oxocamphor.
  1. KM=0.05 mM for 6-oxocamphor1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei40Substrate1 Publication1
    Active sitei124NucleophileBy similarity1
    Binding sitei145Substrate1 Publication1
    Binding sitei154Substrate1 Publication1
    Binding sitei244Substrate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17352
    BRENDAi3.7.1.18 5397
    SABIO-RKiQ93TU6

    Protein family/group databases

    UniLectiniQ93TU6

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-oxocamphor hydrolase (EC:3.7.1.18)
    Short name:
    OCH
    Alternative name(s):
    Beta-diketone hydrolase
    Gene namesi
    Name:camK
    OrganismiRhodococcus sp.
    Taxonomic identifieri1831 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi45H → A: Great decrease of catalytic efficiency. 1
    Mutagenesisi122H → A: Great decrease of catalytic efficiency, and the binding affinity is five times that of the wild-type. 1 Publication1
    Mutagenesisi145H → A: Very large decrease in the catalytic efficiency. 100-fold decrease in the binding affinity. 1 Publication1
    Mutagenesisi154D → N: 100-fold decrease in the binding affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004227371 – 2576-oxocamphor hydrolaseAdd BLAST257

    Interactioni

    Subunit structurei

    Hexamer. Dimer of trimers.3 Publications

    Structurei

    Secondary structure

    1257
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliQ93TU6
    SMRiQ93TU6
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93TU6

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK20765

    Family and domain databases

    InterProiView protein in InterPro
    IPR029045 ClpP/crotonase-like_dom_sf
    IPR001753 Enoyl-CoA_hydra/iso
    PfamiView protein in Pfam
    PF00378 ECH_1, 1 hit
    SUPFAMiSSF52096 SSF52096, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q93TU6-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKQLATPFQE YSQKYENIRL ERDGGVLLVT VHTEGKSLVW TSTAHDELAY
    60 70 80 90 100
    CFHDIACDRE NKVVILTGTG PSFCNEIDFT SFNLGTPHDW DEIIFEGQRL
    110 120 130 140 150
    LNNLLSIEVP VIAAVNGPVT NHPEIPVMSD IVLAAESATF QDGPHFPSGI
    160 170 180 190 200
    VPGDGAHVVW PHVLGSNRGR YFLLTGQELD ARTALDYGAV NEVLSEQELL
    210 220 230 240 250
    PRAWELARGI AEKPLLARRY ARKVLTRQLR RVMEADLSLG LAHEALAAID

    LGMESEQ
    Length:257
    Mass (Da):28,483
    Last modified:December 1, 2001 - v1
    Checksum:i0AE4A9E54CE83EFF
    GO

    Mass spectrometryi

    Molecular mass is 28488 Da from positions 1 - 257. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF323755 Genomic DNA Translation: AAK50622.1

    Genome annotation databases

    KEGGiag:AAK50622

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF323755 Genomic DNA Translation: AAK50622.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1O8UX-ray2.00A/B/C/D/E/F1-257[»]
    1SZOX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L1-257[»]
    ProteinModelPortaliQ93TU6
    SMRiQ93TU6
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    UniLectiniQ93TU6

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAK50622

    Phylogenomic databases

    KOiK20765

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17352
    BRENDAi3.7.1.18 5397
    SABIO-RKiQ93TU6

    Miscellaneous databases

    EvolutionaryTraceiQ93TU6

    Family and domain databases

    InterProiView protein in InterPro
    IPR029045 ClpP/crotonase-like_dom_sf
    IPR001753 Enoyl-CoA_hydra/iso
    PfamiView protein in Pfam
    PF00378 ECH_1, 1 hit
    SUPFAMiSSF52096 SSF52096, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCAMK_RHOSO
    AccessioniPrimary (citable) accession number: Q93TU6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2013
    Last sequence update: December 1, 2001
    Last modified: September 12, 2018
    This is version 56 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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