CLD_IDEDE
ID CLD_IDEDE Reviewed; 285 AA.
AC Q9F437;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Chlorite dismutase;
DE EC=1.13.11.49;
DE AltName: Full=Chlorite O(2)-lyase;
DE Flags: Precursor;
GN Name=cld;
OS Ideonella dechloratans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Ideonella.
OX NCBI_TaxID=36863;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-63; 77-87 AND
RP 171-185, AND COFACTOR.
RC STRAIN=ATCC 51718 / CCUG 30977;
RX PubMed=12359335; DOI=10.1016/s0167-4781(02)00446-3;
RA Danielsson Thorell H., Karlsson J., Portelius E., Nilsson T.;
RT "Cloning, characterisation, and expression of a novel gene encoding
RT chlorite dismutase from Ideonella dechloratans.";
RL Biochim. Biophys. Acta 1577:445-451(2002).
RN [2]
RP PROTEIN SEQUENCE OF 39-60, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 51718 / CCUG 30977;
RX PubMed=11472023; DOI=10.1007/s007750100237;
RA Stenklo K., Danielsson Thorell H., Bergius H., Aasa R., Nilsson T.;
RT "Chlorite dismutase from Ideonella dechloratans.";
RL J. Biol. Inorg. Chem. 6:601-607(2001).
RN [3]
RP PROTEIN SEQUENCE OF 281-285, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51718 / CCUG 30977;
RX PubMed=15317589; DOI=10.1111/j.0014-2956.2004.04290.x;
RA Danielsson Thorell H., Beyer N.H., Heegaard N.H., Oehman M., Nilsson T.;
RT "Comparison of native and recombinant chlorite dismutase from Ideonella
RT dechloratans.";
RL Eur. J. Biochem. 271:3539-3546(2004).
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 51718 / CCUG 30977;
RX PubMed=22492460; DOI=10.1128/aem.07303-11;
RA Lindqvist M.H., Johansson N., Nilsson T., Rova M.;
RT "Expression of chlorite dismutase and chlorate reductase in the presence of
RT oxygen and/or chlorate as the terminal electron acceptor in Ideonella
RT dechloratans.";
RL Appl. Environ. Microbiol. 78:4380-4385(2012).
CC -!- FUNCTION: Catalyzes the heme-dependent decomposition of chlorite to
CC O(2) and chloride with high efficiency and specificity. Used to
CC detoxify chlorite, a by-product of the reduction of perchlorate, a
CC primarily anthropogenic pollutant, in perchlorate-respiring bacteria.
CC {ECO:0000269|PubMed:11472023, ECO:0000269|PubMed:22492460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride + O2 = chlorite; Xref=Rhea:RHEA:21404,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17441, ChEBI:CHEBI:17996;
CC EC=1.13.11.49; Evidence={ECO:0000269|PubMed:11472023};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:11472023, ECO:0000269|PubMed:12359335};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000269|PubMed:11472023, ECO:0000269|PubMed:12359335};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for chlorite {ECO:0000269|PubMed:11472023};
CC Vmax=4.3 mmol/min/mg enzyme {ECO:0000269|PubMed:11472023};
CC -!- SUBUNIT: Homopentamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11472023}.
CC -!- INDUCTION: Expressed under aerobic conditions. Significantly increased
CC upon shift to anaerobic conditions. {ECO:0000269|PubMed:22492460}.
CC -!- SIMILARITY: Belongs to the chlorite dismutase family. {ECO:0000305}.
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DR EMBL; AJ296077; CAC14884.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F437; -.
DR SMR; Q9F437; -.
DR KEGG; ag:CAC14884; -.
DR SABIO-RK; Q9F437; -.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0050587; F:chlorite O2-lyase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR010644; ChdC/CLD.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR PANTHER; PTHR36843; PTHR36843; 1.
DR Pfam; PF06778; Chlor_dismutase; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000269|PubMed:11472023,
FT ECO:0000269|PubMed:12359335"
FT CHAIN 39..285
FT /note="Chlorite dismutase"
FT /id="PRO_5000066624"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CONFLICT 59
FT /note="F -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
