CLD_DECAR
ID CLD_DECAR Reviewed; 282 AA.
AC Q47CX0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Chlorite dismutase;
DE EC=1.13.11.49;
DE AltName: Full=Chlorite O(2)-lyase;
DE Flags: Precursor;
GN OrderedLocusNames=Daro_2580;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
RN [2]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18422344; DOI=10.1021/bi800163x;
RA Streit B.R., DuBois J.L.;
RT "Chemical and steady-state kinetic analyses of a heterologously expressed
RT heme dependent chlorite dismutase.";
RL Biochemistry 47:5271-5280(2008).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=18840691; DOI=10.1073/pnas.0804279105;
RA Lee A.Q., Streit B.R., Zdilla M.J., Abu-Omar M.M., DuBois J.L.;
RT "Mechanism of and exquisite selectivity for O-O bond formation by the heme-
RT dependent chlorite dismutase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15654-15659(2008).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
RX PubMed=20356038; DOI=10.1021/ja9082182;
RA Streit B.R., Blanc B., Lukat-Rodgers G.S., Rodgers K.R., DuBois J.L.;
RT "How active-site protonation state influences the reactivity and ligation
RT of the heme in chlorite dismutase.";
RL J. Am. Chem. Soc. 132:5711-5724(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 35-282 IN COMPLEX WITH CALCIUM
RP AND HEME, AND SUBUNIT.
RC STRAIN=RCB;
RX PubMed=20386942; DOI=10.1007/s00775-010-0651-0;
RA Goblirsch B.R., Streit B.R., Dubois J.L., Wilmot C.M.;
RT "Structural features promoting dioxygen production by Dechloromonas
RT aromatica chlorite dismutase.";
RL J. Biol. Inorg. Chem. 15:879-888(2010).
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:18422344}.
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:18422344,
CC ECO:0000269|PubMed:18840691};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:18422344};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000269|PubMed:18422344};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=620 uM for chlorite (at 4 degrees Celsius and pH 5.2)
CC {ECO:0000269|PubMed:18422344, ECO:0000269|PubMed:20356038};
CC KM=215 uM for chlorite (at 4 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:18422344, ECO:0000269|PubMed:20356038};
CC KM=430 uM for chlorite (at 4 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:18422344, ECO:0000269|PubMed:20356038};
CC Note=kcat is 4.53 min(-1) with chlorite as substrate.;
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:20386942}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chlorite dismutase family. {ECO:0000305}.
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DR EMBL; CP000089; AAZ47311.1; -; Genomic_DNA.
DR RefSeq; WP_011288310.1; NC_007298.1.
DR 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.
DR 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.
DR PDBsum; 3Q08; -.
DR PDBsum; 3Q09; -.
DR AlphaFoldDB; Q47CX0; -.
DR SMR; Q47CX0; -.
DR STRING; 159087.Daro_2580; -.
DR EnsemblBacteria; AAZ47311; AAZ47311; Daro_2580.
DR KEGG; dar:Daro_2580; -.
DR eggNOG; COG3253; Bacteria.
DR HOGENOM; CLU_1052467_0_0_4; -.
DR OMA; FMREFRS; -.
DR OrthoDB; 1420788at2; -.
DR BRENDA; 1.13.11.49; 10828.
DR GO; GO:0042597; C:periplasmic space; ISS: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 3D-structure; Calcium; Heme; Iron; Metal-binding; Oxidoreductase;
KW Periplasm; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..282
FT /note="Chlorite dismutase"
FT /id="PRO_5000100107"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:20356038"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20386942"
FT BINDING 204
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 BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20386942"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20386942"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3Q08"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:3Q09"
FT TURN 72..77
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:3Q09"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:3Q09"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3Q09"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 226..237
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3Q09"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:3Q09"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:3Q09"
SQ 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
