ID   CATA_STAHJ              Reviewed;         503 AA.
AC   Q4L643;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=SH1573;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04882.1; -; Genomic_DNA.
DR   RefSeq; WP_011275863.1; NC_007168.1.
DR   AlphaFoldDB; Q4L643; -.
DR   SMR; Q4L643; -.
DR   STRING; 279808.SH1573; -.
DR   EnsemblBacteria; BAE04882; BAE04882; SH1573.
DR   KEGG; sha:SH1573; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_9; -.
DR   OMA; WTCYVQV; -.
DR   OrthoDB; 1584770at2; -.
DR   Proteomes; UP000000543; 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..503
FT                   /note="Catalase"
FT                   /id="PRO_0000085006"
FT   REGION          1..26
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   503 AA;  58053 MW;  ACE7272241A12DBD CRC64;
     MAKDDKRLTG LFGHPVSDRE NSMTAGPRGP LLMQDAYFLE QMSHFDREVI PERRMHAKGS
     GAFGTFTVTN DITKYTNAKI FSEVGKQTEM FARFSTVAGE RGAADLERDI RGFALKFYTE
     DGNWDLVGNN TPVFFFRDSK LFVSLNRAVK RDPRTNMRSP QNNWDFWTGV PEALHQVTIL
     MSDRGMPKDF RHMHGFGSHT YSMYNDEGER VWVKYHFRTQ QGIENYTDDE AAEIVGQDRE
     SSQRDLYDAI ENGDYPKWKM YIQVMTEEQA KNHPDNPFDL TKVWYKGDYP LIEVGEFELN
     RNPENYFMDV EQAAFAPTNI IPGLDFSPDK MLQGRLFSYG DAQRYRLGVN HWQIPVNQPK
     GVGIENMCPF SRDGQMRFLD GNQGGGPHYY PNNKGVYQSQ PEYKKPAFPV DGDGYEYNQR
     QDDDNYFEQP GKLFRLQSDD AKERIFTNTA NAMDGVSEDV KHRHIRHCYK ADPEYGKGVA
     KALEIDINDV DLEGTNDETY ENF