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Protein

Chlorite dismutase

Gene

Daro_2580

Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the heme-dependent decomposition of chlorite to O2 and chloride with high efficiency and specificity. Used to detoxify chlorite, a by-product of the reduction of perchlorate, a primarily anthropogenic pollutant, in perchlorate-respiring bacteria.1 Publication

Catalytic activityi

Chloride + O2 = chlorite.2 Publications

Cofactori

heme b1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.1 Publication

Kineticsi

kcat is 4.53 min(-1) with chlorite as substrate.

  1. KM=620 µM for chlorite (at 4 degrees Celsius and pH 5.2)2 Publications
  2. KM=215 µM for chlorite (at 4 degrees Celsius and pH 6.8)2 Publications
  3. KM=430 µM for chlorite (at 4 degrees Celsius and pH 7.6)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi104 – 1041Calcium1 Publication
    Metal bindingi204 – 2041Iron (heme axial ligand); via tele nitrogen
    Active sitei217 – 2171Proton acceptor1 Publication
    Metal bindingi226 – 2261Calcium1 Publication
    Metal bindingi265 – 2651Calcium; via carbonyl oxygen1 Publication

    GO - Molecular functioni

    • chlorite O2-lyase activity Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciDARO159087:GI5B-2646-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chlorite dismutase (EC:1.13.11.49)
    Alternative name(s):
    Chlorite O(2)-lyase
    Gene namesi
    Ordered Locus Names:Daro_2580
    OrganismiDechloromonas aromatica (strain RCB)
    Taxonomic identifieri159087 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
    Proteomesi
    • UP000000550 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    • periplasmic space Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence analysisAdd
    BLAST
    Chaini32 – 282251Chlorite dismutasePRO_5000100107Add
    BLAST

    Interactioni

    Subunit structurei

    Homopentamer.1 Publication

    Protein-protein interaction databases

    STRINGi159087.Daro_2580.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi45 – 484Combined sources
    Beta strandi51 – 533Combined sources
    Beta strandi55 – 639Combined sources
    Helixi65 – 695Combined sources
    Turni72 – 776Combined sources
    Helixi78 – 8811Combined sources
    Turni89 – 924Combined sources
    Beta strandi93 – 997Combined sources
    Turni101 – 1033Combined sources
    Beta strandi108 – 1169Combined sources
    Helixi118 – 12811Combined sources
    Helixi132 – 1354Combined sources
    Beta strandi137 – 14610Combined sources
    Beta strandi151 – 1544Combined sources
    Turni155 – 1573Combined sources
    Helixi159 – 1668Combined sources
    Beta strandi177 – 1859Combined sources
    Helixi187 – 1904Combined sources
    Helixi194 – 20815Combined sources
    Helixi209 – 2135Combined sources
    Beta strandi215 – 2217Combined sources
    Beta strandi226 – 23712Combined sources
    Helixi239 – 25012Combined sources
    Helixi253 – 2575Combined sources
    Beta strandi258 – 2614Combined sources
    Beta strandi266 – 2705Combined sources
    Helixi273 – 2819Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q08X-ray3.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T35-282[»]
    3Q09X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T35-282[»]
    ProteinModelPortaliQ47CX0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chlorite dismutase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000068200.
    KOiK09162.
    OrthoDBiEOG6MSS1F.

    Family and domain databases

    InterProiIPR011008. Dimeric_a/b-barrel.
    IPR010644. Put_peroxidase/dismutase.
    [Graphical view]
    PfamiPF06778. Chlor_dismutase. 1 hit.
    [Graphical view]
    SUPFAMiSSF54909. SSF54909. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q47CX0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTNLSIHNFK LSLVAAVIGS AMVMTSSPVA AQQAMQPMQS MKIERGTILT
    60 70 80 90 100
    QPGVFGVFTM FKLRPDWNKV PVAERKGAAE EVKKLIEKHK DNVLVDLYLT
    110 120 130 140 150
    RGLETNSDFF FRINAYDLAK AQTFMREFRS TTVGKNADVF ETLVGVTKPL
    160 170 180 190 200
    NYISKDKSPG LNAGLSSATY SGPAPRYVIV IPVKKNAEWW NMSPEERLKE
    210 220 230 240 250
    MEVHTTPTLA YLVNVKRKLY HSTGLDDTDF ITYFETDDLT AFNNLMLSLA
    260 270 280
    QVKENKFHVR WGSPTTLGTI HSPEDVIKAL AD
    Length:282
    Mass (Da):31,613
    Last modified:September 13, 2005 - v1
    Checksum:i61499C27EAE5AEF5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ47311.1.
    RefSeqiWP_011288310.1. NC_007298.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ47311; AAZ47311; Daro_2580.
    KEGGidar:Daro_2580.
    PATRICi21603820. VBIDecAro89105_2562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ47311.1.
    RefSeqiWP_011288310.1. NC_007298.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q08X-ray3.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T35-282[»]
    3Q09X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T35-282[»]
    ProteinModelPortaliQ47CX0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi159087.Daro_2580.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAZ47311; AAZ47311; Daro_2580.
    KEGGidar:Daro_2580.
    PATRICi21603820. VBIDecAro89105_2562.

    Phylogenomic databases

    HOGENOMiHOG000068200.
    KOiK09162.
    OrthoDBiEOG6MSS1F.

    Enzyme and pathway databases

    BioCyciDARO159087:GI5B-2646-MONOMER.

    Family and domain databases

    InterProiIPR011008. Dimeric_a/b-barrel.
    IPR010644. Put_peroxidase/dismutase.
    [Graphical view]
    PfamiPF06778. Chlor_dismutase. 1 hit.
    [Graphical view]
    SUPFAMiSSF54909. SSF54909. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
      Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
      BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RCB.
    2. "Chemical and steady-state kinetic analyses of a heterologously expressed heme dependent chlorite dismutase."
      Streit B.R., DuBois J.L.
      Biochemistry 47:5271-5280(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    3. "Mechanism of and exquisite selectivity for O-O bond formation by the heme-dependent chlorite dismutase."
      Lee A.Q., Streit B.R., Zdilla M.J., Abu-Omar M.M., DuBois J.L.
      Proc. Natl. Acad. Sci. U.S.A. 105:15654-15659(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    4. "How active-site protonation state influences the reactivity and ligation of the heme in chlorite dismutase."
      Streit B.R., Blanc B., Lukat-Rodgers G.S., Rodgers K.R., DuBois J.L.
      J. Am. Chem. Soc. 132:5711-5724(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE.
    5. "Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase."
      Goblirsch B.R., Streit B.R., Dubois J.L., Wilmot C.M.
      J. Biol. Inorg. Chem. 15:879-888(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 35-282 IN COMPLEX WITH CALCIUM AND HEME, SUBUNIT.
      Strain: RCB.

    Entry informationi

    Entry nameiCLD_DECAR
    AccessioniPrimary (citable) accession number: Q47CX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 16, 2013
    Last sequence update: September 13, 2005
    Last modified: December 9, 2015
    This is version 59 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, Complete proteome, Reference proteome

    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.