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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)DescriptionActionsGraphical viewLength
    Metal bindingi104Calcium1 Publication1
    Metal bindingi204Iron (heme axial ligand); via tele nitrogen1
    Active sitei217Proton acceptor1 Publication1
    Metal bindingi226Calcium1 Publication1
    Metal bindingi265Calcium; via carbonyl oxygen1 Publication1

    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-2619-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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 31Sequence analysisAdd BLAST31
    ChainiPRO_500010010732 – 282Chlorite dismutaseAdd BLAST251

    Interactioni

    Subunit structurei

    Homopentamer.1 Publication

    Protein-protein interaction databases

    STRINGi159087.Daro_2580.

    Structurei

    Secondary structure

    1282
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi45 – 48Combined sources4
    Beta strandi51 – 53Combined sources3
    Beta strandi55 – 63Combined sources9
    Helixi65 – 69Combined sources5
    Turni72 – 77Combined sources6
    Helixi78 – 88Combined sources11
    Turni89 – 92Combined sources4
    Beta strandi93 – 99Combined sources7
    Turni101 – 103Combined sources3
    Beta strandi108 – 116Combined sources9
    Helixi118 – 128Combined sources11
    Helixi132 – 135Combined sources4
    Beta strandi137 – 146Combined sources10
    Beta strandi151 – 154Combined sources4
    Turni155 – 157Combined sources3
    Helixi159 – 166Combined sources8
    Beta strandi177 – 185Combined sources9
    Helixi187 – 190Combined sources4
    Helixi194 – 208Combined sources15
    Helixi209 – 213Combined sources5
    Beta strandi215 – 221Combined sources7
    Beta strandi226 – 237Combined sources12
    Helixi239 – 250Combined sources12
    Helixi253 – 257Combined sources5
    Beta strandi258 – 261Combined sources4
    Beta strandi266 – 270Combined sources5
    Helixi273 – 281Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiQ47CX0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chlorite dismutase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000068200.
    KOiK09162.
    OMAiEMEVHTT.
    OrthoDBiPOG091H0A5D.

    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
    PDB 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.
    SMRiQ47CX0.
    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.
    OMAiEMEVHTT.
    OrthoDBiPOG091H0A5D.

    Enzyme and pathway databases

    BioCyciDARO159087:GI5B-2619-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...

    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: November 2, 2016
    This is version 61 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.