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Chlorite dismutase (EC 1.13.11.49) (Chlorite O(2)-lyase)

 CLD_DECAR               Reviewed;         282 AA.
Q47CX0;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 1.
30-AUG-2017, entry version 65.
RecName: Full=Chlorite dismutase;
EC=1.13.11.49;
AltName: Full=Chlorite O(2)-lyase;
Flags: Precursor;
OrderedLocusNames=Daro_2580;
Dechloromonas aromatica (strain RCB).
Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
Azonexaceae; Dechloromonas.
NCBI_TaxID=159087;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RCB;
PubMed=19650930; DOI=10.1186/1471-2164-10-351;
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
Lapidus A.;
"Metabolic analysis of the soil microbe Dechloromonas aromatica str.
RCB: indications of a surprisingly complex life-style and cryptic
anaerobic pathways for aromatic degradation.";
BMC Genomics 10:351-351(2009).
[2]
CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18422344; DOI=10.1021/bi800163x;
Streit B.R., DuBois J.L.;
"Chemical and steady-state kinetic analyses of a heterologously
expressed heme dependent chlorite dismutase.";
Biochemistry 47:5271-5280(2008).
[3]
CATALYTIC ACTIVITY.
PubMed=18840691; DOI=10.1073/pnas.0804279105;
Lee A.Q., Streit B.R., Zdilla M.J., Abu-Omar M.M., DuBois J.L.;
"Mechanism of and exquisite selectivity for O-O bond formation by the
heme-dependent chlorite dismutase.";
Proc. Natl. Acad. Sci. U.S.A. 105:15654-15659(2008).
[4]
BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
PubMed=20356038; DOI=10.1021/ja9082182;
Streit B.R., Blanc B., Lukat-Rodgers G.S., Rodgers K.R., DuBois J.L.;
"How active-site protonation state influences the reactivity and
ligation of the heme in chlorite dismutase.";
J. Am. Chem. Soc. 132:5711-5724(2010).
[5]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 35-282 IN COMPLEX WITH
CALCIUM AND HEME, AND SUBUNIT.
STRAIN=RCB;
PubMed=20386942; DOI=10.1007/s00775-010-0651-0;
Goblirsch B.R., Streit B.R., Dubois J.L., Wilmot C.M.;
"Structural features promoting dioxygen production by Dechloromonas
aromatica chlorite dismutase.";
J. Biol. Inorg. Chem. 15:879-888(2010).
-!- 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:18422344}.
-!- CATALYTIC ACTIVITY: Chloride + O(2) = chlorite.
{ECO:0000269|PubMed:18422344, ECO:0000269|PubMed:18840691}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:18422344};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
monomer. {ECO:0000269|PubMed:18422344};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=620 uM for chlorite (at 4 degrees Celsius and pH 5.2)
{ECO:0000269|PubMed:18422344, ECO:0000269|PubMed:20356038};
KM=215 uM for chlorite (at 4 degrees Celsius and pH 6.8)
{ECO:0000269|PubMed:18422344, ECO:0000269|PubMed:20356038};
KM=430 uM for chlorite (at 4 degrees Celsius and pH 7.6)
{ECO:0000269|PubMed:18422344, ECO:0000269|PubMed:20356038};
Note=kcat is 4.53 min(-1) with chlorite as substrate.;
-!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:20386942}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the chlorite dismutase family.
{ECO:0000305}.
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EMBL; CP000089; AAZ47311.1; -; Genomic_DNA.
RefSeq; WP_011288310.1; NC_007298.1.
PDB; 3Q08; X-ray; 3.05 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=35-282.
PDB; 3Q09; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=35-282.
PDBsum; 3Q08; -.
PDBsum; 3Q09; -.
ProteinModelPortal; Q47CX0; -.
SMR; Q47CX0; -.
STRING; 159087.Daro_2580; -.
EnsemblBacteria; AAZ47311; AAZ47311; Daro_2580.
KEGG; dar:Daro_2580; -.
HOGENOM; HOG000068200; -.
KO; K09162; -.
OMA; EMEVHTT; -.
OrthoDB; POG091H0A5D; -.
BioCyc; DARO159087:GI5B-2619-MONOMER; -.
Proteomes; UP000000550; Chromosome.
GO; GO:0042597; C:periplasmic space; ISS: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.
Pfam; PF06778; Chlor_dismutase; 1.
SUPFAM; SSF54909; SSF54909; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Heme; Iron; Metal-binding;
Oxidoreductase; Periplasm; Reference proteome; Signal.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 282 Chlorite dismutase.
/FTId=PRO_5000100107.
ACT_SITE 217 217 Proton acceptor.
{ECO:0000269|PubMed:20356038}.
METAL 104 104 Calcium. {ECO:0000269|PubMed:20386942}.
METAL 204 204 Iron (heme axial ligand); via tele
nitrogen.
METAL 226 226 Calcium. {ECO:0000269|PubMed:20386942}.
METAL 265 265 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:20386942}.
HELIX 45 48 {ECO:0000244|PDB:3Q09}.
STRAND 51 53 {ECO:0000244|PDB:3Q08}.
STRAND 55 63 {ECO:0000244|PDB:3Q09}.
HELIX 65 69 {ECO:0000244|PDB:3Q09}.
TURN 72 77 {ECO:0000244|PDB:3Q09}.
HELIX 78 88 {ECO:0000244|PDB:3Q09}.
TURN 89 92 {ECO:0000244|PDB:3Q09}.
STRAND 93 99 {ECO:0000244|PDB:3Q09}.
TURN 101 103 {ECO:0000244|PDB:3Q09}.
STRAND 108 116 {ECO:0000244|PDB:3Q09}.
HELIX 118 128 {ECO:0000244|PDB:3Q09}.
HELIX 132 135 {ECO:0000244|PDB:3Q09}.
STRAND 137 146 {ECO:0000244|PDB:3Q09}.
STRAND 151 154 {ECO:0000244|PDB:3Q09}.
TURN 155 157 {ECO:0000244|PDB:3Q09}.
HELIX 159 166 {ECO:0000244|PDB:3Q09}.
STRAND 177 185 {ECO:0000244|PDB:3Q09}.
HELIX 187 190 {ECO:0000244|PDB:3Q09}.
HELIX 194 208 {ECO:0000244|PDB:3Q09}.
HELIX 209 213 {ECO:0000244|PDB:3Q09}.
STRAND 215 221 {ECO:0000244|PDB:3Q09}.
STRAND 226 237 {ECO:0000244|PDB:3Q09}.
HELIX 239 250 {ECO:0000244|PDB:3Q09}.
HELIX 253 257 {ECO:0000244|PDB:3Q09}.
STRAND 258 261 {ECO:0000244|PDB:3Q09}.
STRAND 266 270 {ECO:0000244|PDB:3Q09}.
HELIX 273 281 {ECO:0000244|PDB:3Q09}.
SEQUENCE 282 AA; 31613 MW; 61499C27EAE5AEF5 CRC64;
MTNLSIHNFK LSLVAAVIGS AMVMTSSPVA AQQAMQPMQS MKIERGTILT QPGVFGVFTM
FKLRPDWNKV PVAERKGAAE EVKKLIEKHK DNVLVDLYLT RGLETNSDFF FRINAYDLAK
AQTFMREFRS TTVGKNADVF ETLVGVTKPL NYISKDKSPG LNAGLSSATY SGPAPRYVIV
IPVKKNAEWW NMSPEERLKE MEVHTTPTLA YLVNVKRKLY HSTGLDDTDF ITYFETDDLT
AFNNLMLSLA QVKENKFHVR WGSPTTLGTI HSPEDVIKAL AD


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