GENTAUR Molecular Products.

 CLD_IDEDE               Reviewed;         285 AA.
 Q9F437;
 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2001, sequence version 1.
 23-MAY-2018, entry version 36.
 RecName: Full=Chlorite dismutase;
          EC=1.13.11.49;
 AltName: Full=Chlorite O(2)-lyase;
 Flags: Precursor;
 Name=cld;
 Ideonella dechloratans.
 Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
 Ideonella.
 NCBI_TaxID=36863;
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-63; 77-87
 AND 171-185, AND COFACTOR.
 STRAIN=ATCC 51718 / CCUG 30977;
 PubMed=12359335; DOI=10.1016/S0167-4781(02)00446-3;
 Danielsson Thorell H., Karlsson J., Portelius E., Nilsson T.;
 "Cloning, characterisation, and expression of a novel gene encoding
 chlorite dismutase from Ideonella dechloratans.";
 Biochim. Biophys. Acta 1577:445-451(2002).
 [2]
 PROTEIN SEQUENCE OF 39-60, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
 SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
 STRAIN=ATCC 51718 / CCUG 30977;
 PubMed=11472023; DOI=10.1007/s007750100237;
 Stenklo K., Danielsson Thorell H., Bergius H., Aasa R., Nilsson T.;
 "Chlorite dismutase from Ideonella dechloratans.";
 J. Biol. Inorg. Chem. 6:601-607(2001).
 [3]
 PROTEIN SEQUENCE OF 281-285, AND IDENTIFICATION BY MASS SPECTROMETRY.
 STRAIN=ATCC 51718 / CCUG 30977;
 PubMed=15317589; DOI=10.1111/j.0014-2956.2004.04290.x;
 Danielsson Thorell H., Beyer N.H., Heegaard N.H., Oehman M.,
 Nilsson T.;
 "Comparison of native and recombinant chlorite dismutase from
 Ideonella dechloratans.";
 Eur. J. Biochem. 271:3539-3546(2004).
 [4]
 FUNCTION, AND INDUCTION.
 STRAIN=ATCC 51718 / CCUG 30977;
 PubMed=22492460; DOI=10.1128/AEM.07303-11;
 Lindqvist M.H., Johansson N., Nilsson T., Rova M.;
 "Expression of chlorite dismutase and chlorate reductase in the
 presence of oxygen and/or chlorate as the terminal electron acceptor
 in Ideonella dechloratans.";
 Appl. Environ. Microbiol. 78:4380-4385(2012).
 -!- FUNCTION: Catalyzes the heme-dependent decomposition of chlorite
     to O(2) 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. {ECO:0000269|PubMed:11472023,
     ECO:0000269|PubMed:22492460}.
 -!- CATALYTIC ACTIVITY: Chloride + O(2) = chlorite.
     {ECO:0000269|PubMed:11472023}.
 -!- COFACTOR:
     Name=heme b; Xref=ChEBI:CHEBI:60344;
       Evidence={ECO:0000269|PubMed:11472023,
       ECO:0000269|PubMed:12359335};
     Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
     monomer. {ECO:0000269|PubMed:11472023,
     ECO:0000269|PubMed:12359335};
 -!- BIOPHYSICOCHEMICAL PROPERTIES:
     Kinetic parameters:
       KM=0.26 mM for chlorite {ECO:0000269|PubMed:11472023};
       Vmax=4.3 mmol/min/mg enzyme {ECO:0000269|PubMed:11472023};
 -!- SUBUNIT: Homopentamer. {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11472023}.
 -!- INDUCTION: Expressed under aerobic conditions. Significantly
     increased upon shift to anaerobic conditions.
     {ECO:0000269|PubMed:22492460}.
 -!- SIMILARITY: Belongs to the chlorite dismutase family.
     {ECO:0000305}.
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 EMBL; AJ296077; CAC14884.1; -; Genomic_DNA.
 ProteinModelPortal; Q9F437; -.
 SMR; Q9F437; -.
 PRIDE; Q9F437; -.
 KEGG; ag:CAC14884; -.
 KO; K09162; -.
 GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
 GO; GO:0050587; F:chlorite O2-lyase activity; IDA:UniProtKB.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 InterPro; IPR011008; Dimeric_a/b-barrel.
 InterPro; IPR010644; Put_peroxidase/dismutase.
 PANTHER; PTHR36843; PTHR36843; 1.
 Pfam; PF06778; Chlor_dismutase; 1.
 SUPFAM; SSF54909; SSF54909; 1.
 1: Evidence at protein level;
 Calcium; Direct protein sequencing; Heme; Iron; Metal-binding;
 Oxidoreductase; Periplasm; Signal.
 SIGNAL        1     38       {ECO:0000269|PubMed:11472023,
                              ECO:0000269|PubMed:12359335}.
 CHAIN        39    285       Chlorite dismutase.
                              /FTId=PRO_5000066624.
 ACT_SITE    218    218       Proton acceptor. {ECO:0000250}.
 METAL       105    105       Calcium. {ECO:0000250}.
 METAL       205    205       Iron (heme axial ligand); via tele
                              nitrogen. {ECO:0000250}.
 METAL       227    227       Calcium. {ECO:0000250}.
 METAL       266    266       Calcium; via carbonyl oxygen.
                              {ECO:0000250}.
 CONFLICT     59     59       F -> P (in Ref. 2; AA sequence).
                              {ECO:0000305}.
 SEQUENCE   285 AA;  31429 MW;  BE83EA65AB19D9D0 CRC64;
 MKVRCVSLVA AGLLTIAGSA IGQPAPAPMP AMAPAAKPAM NTPVDRAKIL SAPGVFVAFS
 TYKIRPDYFK VALAERKGAA DEVMAVLEKH KEKVIVDAYL TRGYEAKSDY FLRVHAYDAV
 AAQAFLVDFR ATRFGMYSDV TESLVGITKA LNYISKDKSP DLNKGLSGAT YAGDAPRFAF
 MIPVKKNADW WNLTDEQRLK EMETHTLPTL PFLVNVKRKL YHSTGLDDTD FITYFETNDL
 GAFNNLMLSL AKVPENKYHV RWGNPTVLGT IQPIENLVKT LSMGN

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