ID   CATA_STAWA              Reviewed;         505 AA.
AC   Q9KW19;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA;
OS   Staphylococcus warneri.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ISK-1;
RX   AGRICOLA=IND23261977; DOI=10.3136/fstr.6.324;
RA   Mizuno K., Fukuda D., Kakihara M., Kohno M., Ha T.L., Sonomoto K.,
RA   Ishizaki A.;
RT   "Purification and gene cloning of catalase from Staphylococcus warneri ISK-
RT   1.";
RL   Food Sci. Technol. Res. 6:324-329(2000).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000250}.
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=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AB045340; BAA97560.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KW19; -.
DR   SMR; Q9KW19; -.
DR   STRING; 1194526.A284_06960; -.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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   CDD; cd08156; catalase_clade_3; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..505
FT                   /note="Catalase"
FT                   /id="PRO_0000085008"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         339
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"
SQ   SEQUENCE   505 AA;  58042 MW;  106AF448457EC1F6 CRC64;
     MSKQDGKLTG LFGAPVSDRE NSMTAGPRGP LLMQDIYFLE QMSHFDREVI PERRMHAKGS
     GAFGTFTVTN DITQYTSAKM FSEVGKQTEM FARFSTVSGE RGAADAERDI RGFALKFYTE
     DGNWDLVGNN TPVFFFRDPK LFVSLNRAVK RDPRTNMRSA QNNWDFWTGL PEALHQVTIL
     MSDRGIPKDL RHMHGFGSHT YSMYNDKGER VWVKYHFRTQ QGIENLTDEE AANVIATDRD
     SSQRDLFNAI ENGDYPKWKM YIQVMTEEQA RNHKDNPFDL TKVWYHGDYP LIEVGEFELN
     RNPNNYFQDV EQAAFAPTNI VPGLDYSPDK MLQGRLFPYG DAQRYRLGVN HWQIPVNQPK
     GVGIENLCPF SRDGQMRILD DNQGGGPHYY PNNQGVYDSQ PEFKKPPFPA DGDGYEYNQR
     QDDDNYFEQP GKLFRLQSDE AKERIFTNTA NAMDGVTEDV KRRHIRHCYK ADPDYGKGVA
     KALGIDINSI DLEGEQDETY ENFKN