Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

6-oxocamphor hydrolase

Gene

camK

Organism
Rhodococcus sp.
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401Substrate1 Publication
    Active sitei124 – 1241NucleophileBy similarity
    Binding sitei145 – 1451Substrate1 Publication
    Binding sitei154 – 1541Substrate1 Publication
    Binding sitei244 – 2441Substrate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17352.
    BRENDAi3.7.1.18. 5397.
    SABIO-RKQ93TU6.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451H → A: Great decrease of catalytic efficiency.
    Mutagenesisi122 – 1221H → A: Great decrease of catalytic efficiency, and the binding affinity is five times that of the wild-type. 1 Publication
    Mutagenesisi145 – 1451H → A: Very large decrease in the catalytic efficiency. 100-fold decrease in the binding affinity. 1 Publication
    Mutagenesisi154 – 1541D → N: 100-fold decrease in the binding affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2572576-oxocamphor hydrolasePRO_0000422737Add
    BLAST

    Interactioni

    Subunit structurei

    Hexamer. Dimer of trimers.3 Publications

    Structurei

    Secondary structure

    1
    257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114Combined sources
    Beta strandi18 – 236Combined sources
    Beta strandi26 – 316Combined sources
    Helixi42 – 5716Combined sources
    Beta strandi63 – 675Combined sources
    Beta strandi72 – 743Combined sources
    Helixi79 – 813Combined sources
    Helixi87 – 10620Combined sources
    Beta strandi111 – 1155Combined sources
    Helixi124 – 1274Combined sources
    Beta strandi129 – 1357Combined sources
    Beta strandi139 – 1413Combined sources
    Turni143 – 1453Combined sources
    Helixi146 – 1483Combined sources
    Turni153 – 1553Combined sources
    Helixi156 – 1649Combined sources
    Helixi166 – 1749Combined sources
    Beta strandi178 – 1803Combined sources
    Helixi181 – 1866Combined sources
    Beta strandi191 – 1944Combined sources
    Helixi196 – 21116Combined sources
    Helixi215 – 22511Combined sources
    Helixi227 – 25125Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 4-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93TU6.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    [Graphical view]
    PfamiPF00378. ECH_1. 1 hit.
    [Graphical view]
    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.

    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
    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. Positions 4-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAK50622.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17352.
    BRENDAi3.7.1.18. 5397.
    SABIO-RKQ93TU6.

    Miscellaneous databases

    EvolutionaryTraceiQ93TU6.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    [Graphical view]
    PfamiPF00378. ECH_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "The desymmetrization of bicyclic beta -diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily."
      Grogan G., Roberts G.A., Bougioukou D., Turner N.J., Flitsch S.L.
      J. Biol. Chem. 276:12565-12572(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT.
      Strain: NCIMB 9784.
    2. "Nucleotide sequence of a portion of the camphor-degrading gene cluster from Rhodococcus sp. NCIMB 9784."
      Roberts G.A., Grogan G., Turner N.J., Flitsch S.L.
      DNA Seq. 15:96-103(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NCIMB 9784.
    3. "The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily."
      Whittingham J.L., Turkenburg J.P., Verma C.S., Walsh M.A., Grogan G.
      J. Biol. Chem. 278:1744-1750(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), SUBUNIT.
      Strain: NCIMB 9784.
    4. "Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog."
      Leonard P.M., Grogan G.
      J. Biol. Chem. 279:31312-31317(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS ALA-122 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF HIS-122; HIS-145 AND ASP-154, FUNCTION, REACTION MECHANISM, SUBUNIT.

    Entry informationi

    Entry nameiCAMK_RHOSO
    AccessioniPrimary (citable) accession number: Q93TU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2013
    Last sequence update: December 1, 2001
    Last modified: July 6, 2016
    This is version 48 of the entry and version 1 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.