KATG_BURPS
ID KATG_BURPS Reviewed; 728 AA.
AC Q939D2; Q63R09;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=BPSL2865;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12383513; DOI=10.1016/s0378-1119(02)00854-5;
RA Loprasert S., Sallabhan R., Whangsuk W., Mongkolsuk S.;
RT "The Burkholderia pseudomallei oxyR gene: expression analysis and mutant
RT characterization.";
RL Gene 296:161-169(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-5, AND COVALENT BOND.
RX PubMed=12832453; DOI=10.1074/jbc.m304053200;
RA Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T.,
RA Singh R., Switala J., Carpena X., Fita I., Loewen P.C.;
RT "Characterization of the catalase-peroxidase KatG from Burkholderia
RT pseudomallei by mass spectrometry.";
RL J. Biol. Chem. 278:35687-35692(2003).
RN [4]
RP FUNCTION.
RX PubMed=15280362; DOI=10.1074/jbc.m406374200;
RA Singh R., Wiseman B., Deemagarn T., Donald L.J., Duckworth H.W.,
RA Carpena X., Fita I., Loewen P.C.;
RT "Catalase-peroxidases (KatG) exhibit NADH oxidase activity.";
RL J. Biol. Chem. 279:43098-43106(2004).
RN [5]
RP CATALYTIC MECHANISM.
RX PubMed=17260948; DOI=10.1021/bi062266+;
RA Jakopitsch C., Vlasits J., Wiseman B., Loewen P.C., Obinger C.;
RT "Redox intermediates in the catalase cycle of catalase-peroxidases from
RT Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium
RT tuberculosis.";
RL Biochemistry 46:1183-1193(2007).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
RA Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
RT "Comparative study of catalase-peroxidases (KatGs).";
RL Arch. Biochem. Biophys. 471:207-214(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-728 IN COMPLEX WITH HEME, AND
RP SUBUNIT.
RX PubMed=12628252; DOI=10.1016/s0022-2836(03)00122-0;
RA Carpena X., Loprasert S., Mongkolsuk S., Switala J., Loewen P.C., Fita I.;
RT "Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A
RT resolution.";
RL J. Mol. Biol. 327:475-489(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-304 IN COMPLEX WITH
RP HEME, AND SUBUNIT.
RX PubMed=15567407; DOI=10.1016/j.jmb.2004.10.020;
RA Deemagarn T., Carpena X., Singh R., Wiseman B., Fita I., Loewen P.C.;
RT "Structural characterization of the Ser324Thr variant of the catalase-
RT peroxidase (KatG) from Burkholderia pseudomallei.";
RL J. Mol. Biol. 345:21-28(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16211084; DOI=10.1038/sj.embor.7400550;
RA Carpena X., Wiseman B., Deemagarn T., Singh R., Switala J., Ivancich A.,
RA Fita I., Loewen P.C.;
RT "A molecular switch and electronic circuit modulate catalase activity in
RT catalase-peroxidases.";
RL EMBO Rep. 6:1156-1162(2005).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Also displays NADH oxidase, isoniazid hydrazine
CC lyase and isonicotinoyl-NAD synthase activities. {ECO:0000255|HAMAP-
CC Rule:MF_01961, ECO:0000269|PubMed:15280362}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01961};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
CC {ECO:0000269|PubMed:16211084, ECO:0000269|PubMed:18178143};
CC KM=4.5 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC {ECO:0000269|PubMed:16211084, ECO:0000269|PubMed:18178143};
CC KM=700 uM for H(2)O(2) for the peroxidase reaction
CC {ECO:0000269|PubMed:16211084, ECO:0000269|PubMed:18178143};
CC KM=300 uM for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:16211084, ECO:0000269|PubMed:18178143};
CC KM=12.5 uM for NADH for the oxidase reaction
CC {ECO:0000269|PubMed:16211084, ECO:0000269|PubMed:18178143};
CC Vmax=11900 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 5.5-6.0) {ECO:0000269|PubMed:16211084,
CC ECO:0000269|PubMed:18178143};
CC Vmax=4300 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 7.0) {ECO:0000269|PubMed:16211084,
CC ECO:0000269|PubMed:18178143};
CC Vmax=6.0 umol/min/mg enzyme for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:16211084, ECO:0000269|PubMed:18178143};
CC pH dependence:
CC Optimum pH is 4.5 for the peroxidase reaction, 6.0 for the catalase
CC reaction, and 8.75 for the NADH oxidase reaction.
CC {ECO:0000269|PubMed:16211084, ECO:0000269|PubMed:18178143};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12628252,
CC ECO:0000269|PubMed:15567407, ECO:0000269|PubMed:16211084}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK72466.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH36875.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY040244; AAK72466.3; ALT_INIT; Genomic_DNA.
DR EMBL; BX571965; CAH36875.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004522123.1; NZ_CP009538.1.
DR RefSeq; YP_109459.1; NC_006350.1.
DR PDB; 5L02; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5L05; X-ray; 1.70 A; A/B=15-728.
DR PDB; 5SW4; X-ray; 1.90 A; A/B=15-728.
DR PDB; 5SW5; X-ray; 2.05 A; A/B=15-728.
DR PDB; 5SW6; X-ray; 1.90 A; A/B=15-728.
DR PDB; 5SX0; X-ray; 2.00 A; A/B=15-728.
DR PDB; 5SX1; X-ray; 1.80 A; A/B=1-728.
DR PDB; 5SX2; X-ray; 2.15 A; A/B=1-728.
DR PDB; 5SX3; X-ray; 2.00 A; A/B=1-728.
DR PDB; 5SX6; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5SX7; X-ray; 1.95 A; A/B=1-728.
DR PDB; 5SXQ; X-ray; 2.10 A; A/B=1-728.
DR PDB; 5SXR; X-ray; 1.69 A; A/B=1-728.
DR PDB; 5SXS; X-ray; 1.89 A; A/B=1-728.
DR PDB; 5SXT; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5SXW; X-ray; 1.60 A; A/B=1-728.
DR PDB; 5SXX; X-ray; 1.70 A; A/B=1-728.
DR PDB; 5SYH; X-ray; 1.65 A; A/B=15-728.
DR PDB; 5SYI; X-ray; 1.70 A; A/B=15-728.
DR PDB; 5SYK; X-ray; 1.80 A; A/B=1-728.
DR PDB; 5SYL; X-ray; 1.95 A; A/B=1-728.
DR PDB; 5SYV; X-ray; 1.75 A; A/B=1-728.
DR PDB; 5SYX; X-ray; 1.77 A; A/B=1-728.
DR PDB; 6CFQ; X-ray; 1.72 A; A/B=1-728.
DR PDB; 6MPY; X-ray; 2.00 A; A/B=1-728.
DR PDB; 6MQ0; X-ray; 1.90 A; A/B=1-728.
DR PDB; 6MQ1; X-ray; 2.50 A; A/B=1-728.
DR PDBsum; 5L02; -.
DR PDBsum; 5L05; -.
DR PDBsum; 5SW4; -.
DR PDBsum; 5SW5; -.
DR PDBsum; 5SW6; -.
DR PDBsum; 5SX0; -.
DR PDBsum; 5SX1; -.
DR PDBsum; 5SX2; -.
DR PDBsum; 5SX3; -.
DR PDBsum; 5SX6; -.
DR PDBsum; 5SX7; -.
DR PDBsum; 5SXQ; -.
DR PDBsum; 5SXR; -.
DR PDBsum; 5SXS; -.
DR PDBsum; 5SXT; -.
DR PDBsum; 5SXW; -.
DR PDBsum; 5SXX; -.
DR PDBsum; 5SYH; -.
DR PDBsum; 5SYI; -.
DR PDBsum; 5SYK; -.
DR PDBsum; 5SYL; -.
DR PDBsum; 5SYV; -.
DR PDBsum; 5SYX; -.
DR PDBsum; 6CFQ; -.
DR PDBsum; 6MPY; -.
DR PDBsum; 6MQ0; -.
DR PDBsum; 6MQ1; -.
DR AlphaFoldDB; Q939D2; -.
DR SMR; Q939D2; -.
DR STRING; 272560.BPSL2865; -.
DR DrugBank; DB08638; 1-hydroperoxy-L-tryptophan.
DR PeroxiBase; 2303; BpCP01_K96243.
DR EnsemblBacteria; CAH36875; CAH36875; BPSL2865.
DR KEGG; bps:BPSL2865; -.
DR PATRIC; fig|272560.51.peg.2433; -.
DR eggNOG; COG0376; Bacteria.
DR OMA; MILAGNC; -.
DR BRENDA; 1.11.1.21; 1031.
DR SABIO-RK; Q939D2; -.
DR EvolutionaryTrace; Q939D2; -.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12832453"
FT CHAIN 2..728
FT /note="Catalase-peroxidase"
FT /id="PRO_0000345092"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT BINDING 259
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT SITE 88
FT /note="Transition state stabilizer"
FT CROSSLNK 91..218
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 244)"
FT CROSSLNK 218..244
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:6CFQ"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6MQ1"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6MPY"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6CFQ"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6MQ1"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:6CFQ"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6MQ1"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 376..387
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 389..405
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:6CFQ"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 498..517
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 527..545
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 608..621
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 643..648
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:6CFQ"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:6CFQ"
FT STRAND 675..680
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 690..699
FT /evidence="ECO:0007829|PDB:6CFQ"
FT HELIX 705..720
FT /evidence="ECO:0007829|PDB:6CFQ"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:6CFQ"
SQ SEQUENCE 728 AA; 79446 MW; FB6EC6E5261F6740 CRC64;
MSNEAKCPFH QAAGNGTSNR DWWPNQLDLS ILHRHSSLSD PMGKDFNYAQ AFEKLDLAAV
KRDLHALMTT SQDWWPADFG HYGGLFIRMA WHSAGTYRTA DGRGGAGEGQ QRFAPLNSWP
DNANLDKARR LLWPIKQKYG RAISWADLLI LTGNVALESM GFKTFGFAGG RADTWEPEDV
YWGSEKIWLE LSGGPNSRYS GDRQLENPLA AVQMGLIYVN PEGPDGNPDP VAAARDIRDT
FARMAMNDEE TVALIAGGHT FGKTHGAGPA SNVGAEPEAA GIEAQGLGWK SAYRTGKGAD
AITSGLEVTW TTTPTQWSHN FFENLFGYEW ELTKSPAGAH QWVAKGADAV IPDAFDPSKK
HRPTMLTTDL SLRFDPAYEK ISRRFHENPE QFADAFARAW FKLTHRDMGP RARYLGPEVP
AEVLLWQDPI PAVDHPLIDA ADAAELKAKV LASGLTVSQL VSTAWAAAST FRGSDKRGGA
NGARIRLAPQ KDWEANQPEQ LAAVLETLEA IRTAFNGAQR GGKQVSLADL IVLAGCAGVE
QAAKNAGHAV TVPFAPGRAD ASQEQTDVES MAVLEPVADG FRNYLKGKYR VPAEVLLVDK
AQLLTLSAPE MTVLLGGLRV LGANVGQSRH GVFTAREQAL TNDFFVNLLD MGTEWKPTAA
DADVFEGRDR ATGELKWTGT RVDLVFGSHS QLRALAEVYG SADAQEKFVR DFVAVWNKVM
NLDRFDLA
