ID   CATA_STAEP              Reviewed;         504 AA.
AC   Q2PUJ9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CH;
RA   Calderon I.L., Arenas F.A., Pichuantes S.E., Vasquez C.C.;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; DQ301862; ABC17637.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2PUJ9; -.
DR   SMR; Q2PUJ9; -.
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..504
FT                   /note="Catalase"
FT                   /id="PRO_0000278275"
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   504 AA;  58269 MW;  2E7663576E96229F CRC64;
     MSKQDGKLTG LFGAPVSDRE NSMTAGRRGP LLMQDVYYLE QISHFDREVI PERRMHAKGS
     GAFGTFTVTN DITQYTNAKI FSEVGKQTEM FARFSTVSGE RGAADLERDI RGFALKFYTE
     DGNWDLVGNN TPVFFFRDPK LFISLNRAVK RDPRTNMRSA QNNWDFWTGL PEALHQVTIL
     MSDRGMPKGF RNMHGFGSHT YSMYNDKGER VWVKYHFRTQ QGIENYTDEE AAKIVGMDRD
     SSQRDLYNAI ENGDYPKWKM YIQVMTEEQA KNHPDNPFDL TKVWYKKDYP LIEVGEFELN
     RNPENYFLDV EQAAFAPTNI VPGLDYSPDK MLQGRLFSYG DAQRYRLGVN HWQIPVNQPK
     GVGVENLCPF SRDGQMRFLD NNQGGGPHYY PNNQGIYESQ PEHKKPPFPT DGDGYEYNYR
     QDDDNYFEQP GKLFRLQSED AKERIFTNTA NAMDGVSKDV KVRHIRHCYK ADPEYGKGVA
     KALDIDINQI DLETNQDETY ENFK