ID   CATA_STAXY              Reviewed;         493 AA.
AC   Q9EV50;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Catalase A;
DE            EC=1.11.1.6;
GN   Name=katA;
OS   Staphylococcus xylosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12435514; DOI=10.1016/s0378-1097(02)01030-3;
RA   Barriere C., Bruckner R., Centeno D., Talon R.;
RT   "Characterisation of the katA gene encoding a catalase and evidence for at
RT   least a second catalase activity in Staphylococcus xylosus, bacteria used
RT   in food fermentation.";
RL   FEMS Microbiol. Lett. 216:277-283(2002).
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; AJ295151; CAC14836.1; -; Genomic_DNA.
DR   RefSeq; WP_042363380.1; NZ_QXUH01000007.1.
DR   AlphaFoldDB; Q9EV50; -.
DR   SMR; Q9EV50; -.
DR   STRING; 1288.SXYLSMQ121_2340; -.
DR   PRIDE; Q9EV50; -.
DR   GeneID; 45498001; -.
DR   KEGG; sxl:SXYLSMQ121_2340; -.
DR   KEGG; sxo:SXYL_02505; -.
DR   eggNOG; COG0753; Bacteria.
DR   OrthoDB; 1584770at2; -.
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..493
FT                   /note="Catalase A"
FT                   /id="PRO_0000085009"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         336
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   493 AA;  56875 MW;  900B959518A9404B CRC64;
     MKRKLTGLFG APVSDRENSM TAGPRGPLLM QDIYFLEQMA HFDREVIPER RMHAKGSGAF
     GTFTVTNDIT KYTCASIFAE VGKQTEMFAR FSTVAGERGA GDAERDIRGF ALKFYTDEGN
     WDLVGNNTPV FFFRDPKLFP SLNHVVKRNP KTNMKDPQAN WDFWTLLPEA LHQITILMTD
     RGIPKGFRNM HGFGSHTYSM YNDKGERFWV KFHHRTQQGI ENYSAEEAEQ VMAKDRDSSQ
     RDLFNNIEQG NFPKWKMYIQ VMTEEQARNH KDNPFDLTKV WYKDEYPLIE VGEFELNRNP
     ENYFQDVEQA AFAPTNIVPG LDFSPDKMLQ GRLFSYGDTQ RYRLGVNHWQ IPVNQPKGVG
     MENICPFSRD GHMRILDNNQ GASTHYYPNS NGAFEDQPQY KKPALDIQGQ AYEYDFREDD
     DNYFEQPGKL FRLLSSEEQQ ILFNNTANEM SPVTDALKHR HIRHCYKADP AYGQGVAEAM
     GIDINEVDLD VAD