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Chlorite dismutase (EC 1.13.11.49) (Chlorite O(2)-lyase)
CLD_IDEDE Reviewed; 285 AA.
Q9F437;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 35.
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; -.
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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Pathways :
WP1030: Selenium metabolism Selenoproteins
WP108: Selenium metabolism/Selenoproteins
WP1149: Selenium metabolism Selenoproteins
WP1293: Selenium metabolism Selenoproteins
WP1358: Selenium metabolism Selenoproteins
WP1640: Cysteine and methionine metabolism
WP1700: Selenoamino acid metabolism
WP1705: Sulfur metabolism
WP1718: Vitamin B6 metabolism
WP28: Selenium Metabolism and Selenoproteins
WP390: Serine-isocitrate lyase pathway
WP668: Octadecanoid Pathway
Related Genes :
[Daro_2580] Chlorite dismutase (EC 1.13.11.49) (Chlorite O(2)-lyase)
[cld] Chlorite dismutase (EC 1.13.11.49) (Chlorite O(2)-lyase)
[msrP yedY2 Dsui_1300] Protein-methionine-sulfoxide reductase catalytic subunit MsrP (EC 1.8.5.-)
[pcrA Daro_2584] Perchlorate reductase subunit alpha (EC 1.97.1.-) (Perchlorate reductase molybdenum subunit)
[sigF Dsui_0155] ECF RNA polymerase sigma factor SigF (ECF sigma factor SigF)
[nrsf Dsui_0154] Probable anti-sigma-F factor NrsF (Negative regulator of sigma F) (Regulator of SigF) (Sigma-F anti-sigma factor NrsF)
[mrpX Dsui_0158] Methionine-rich peptide X
[TTHA1714] Putative heme-dependent peroxidase TTHA1714 (EC 1.11.1.-) (UPF0447 protein TTHA1714)
[clrA] Chlorate reductase subunit alpha (EC 1.97.1.1) (Chlorate reductase molybdenum subunit)
[cld cld1 NIDE1387] Chlorite dismutase (EC 1.13.11.49)
[yedZ1 Dsui_0156] Putative protein-methionine-sulfoxide reductase subunit YedZ1
[purL NIDE1392] Phosphoribosylformylglycinamidine synthase subunit PurL (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit II) (FGAR amidotransferase II) (FGAR-AT II) (Glutamine amidotransferase PurL) (Phosphoribosylformylglycinamidine synthase subunit II)
[guaB NIDE1421] Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)
[aspS NIDE1425] Aspartate--tRNA(Asp/Asn) ligase (EC 6.1.1.23) (Aspartyl-tRNA synthetase) (AspRS) (Non-discriminating aspartyl-tRNA synthetase) (ND-AspRS)
[] Chlorate reductase subunit alpha (EC 1.97.1.1) (Fragment)
[purQ NIDE1391] Phosphoribosylformylglycinamidine synthase subunit PurQ (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit I) (FGAR amidotransferase I) (FGAR-AT I) (Glutaminase PurQ) (EC 3.5.1.2) (Phosphoribosylformylglycinamidine synthase subunit I)
[dxr NIDE1511] 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXP reductoisomerase) (EC 1.1.1.267) (1-deoxyxylulose-5-phosphate reductoisomerase) (2-C-methyl-D-erythritol 4-phosphate synthase)
[purF NIDE1393] Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPATase)
[msrQ yedZ2 Dsui_1299] Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ (Flavocytochrome MsrQ)
[yedY1 Dsui_0157] Putative protein-methionine-sulfoxide reductase subunit YedZ1
[guaA NIDE1422] GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase)
[pcrB Daro_2583] Perchlorate reductase subunit beta (Perchlorate reductase iron-sulfur subunit)
[aroC NIDE1426] Chorismate synthase (CS) (EC 4.2.3.5) (5-enolpyruvylshikimate-3-phosphate phospholyase)
[pcrC Daro_2582] Perchlorate reductase subunit gamma (Perchlorate reductase heme subunit)
[purS NIDE1390] Phosphoribosylformylglycinamidine synthase subunit PurS (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit III) (FGAR amidotransferase III) (FGAR-AT III) (Phosphoribosylformylglycinamidine synthase subunit III)
[cld1 NITMOv2_1301] Chlorite dismutase (EC 1.13.11.49)
[ispU uppS NIDE1513] Isoprenyl transferase (EC 2.5.1.-)
[rnhA NIDE1427] Ribonuclease H (RNase H) (EC 3.1.26.4)
[proS NIDE1509] Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)
[] Chlorite dismutase (EC 1.13.11.49)
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