ID   CATA_STAES              Reviewed;         504 AA.
AC   Q8CPD0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=SE_1016;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04613.1; -; Genomic_DNA.
DR   RefSeq; NP_764571.1; NC_004461.1.
DR   RefSeq; WP_001831169.1; NZ_WBME01000057.1.
DR   AlphaFoldDB; Q8CPD0; -.
DR   SMR; Q8CPD0; -.
DR   STRING; 176280.SE_1016; -.
DR   EnsemblBacteria; AAO04613; AAO04613; SE_1016.
DR   GeneID; 50018856; -.
DR   KEGG; sep:SE_1016; -.
DR   PATRIC; fig|176280.10.peg.991; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_9; -.
DR   OMA; WTCYVQV; -.
DR   Proteomes; UP000001411; Chromosome.
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_0000085005"
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   504 AA;  58213 MW;  10A1D718AF5A6DBD CRC64;
     MSKQDGKLTG LFGAPVSDRE NSMTAGQRGP 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 EQAAFTPTNI VPGLDYSPDK MLQGRLFSYG DAQRYRLGVN HWQIPVNQPK
     GVGVENLCPF SRDGQMRFLD NNQGGGPHYY PNNQGIYESQ PEHKKPPFPT DGDGYEYNYR
     QDDDNYFEQP GKLFRLQSED AKERIFTNTA NAMDGVSKDV KVRHIRHCYK ADPEYGKGVA
     KALGIDINQI DLETNQDETY ENFK