ID   CATB_STAXY              Reviewed;         495 AA.
AC   Q66V81;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Catalase B;
DE            EC=1.11.1.6;
GN   Name=katB;
OS   Staphylococcus xylosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29971 / CIP 81.66 / DSM 20266 / JCM 2418 / LMG 20217 / NCTC
RC   11043 / CCM 2738;
RA   Blaiotta G., Fusco V., Ercolini D., Coppola S.;
RT   "Sequence polymorphism of Staphylococcus xylosus katA and sodA genes:
RT   detection of some atypical Staphylococcus xylosus strains.";
RL   Submitted (JUN-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; AY702101; AAU07935.2; -; Genomic_DNA.
DR   RefSeq; WP_029377399.1; NZ_UHEI01000002.1.
DR   AlphaFoldDB; Q66V81; -.
DR   SMR; Q66V81; -.
DR   STRING; 1288.SXYLSMQ121_1465; -.
DR   PATRIC; fig|1288.89.peg.1248; -.
DR   eggNOG; COG0753; Bacteria.
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..495
FT                   /note="Catalase B"
FT                   /id="PRO_0000085010"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         338
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   495 AA;  57127 MW;  356F11C5CB6AC9C4 CRC64;
     MSNNKKLTSL FGAPVSDREN SMTAGPRGPL VMQDWYFLEQ MAHFDREVIP ERRMHAKGSG
     AFGTFTVTND ITQYTSASIF SEVGKQTEMF ARFSTVAGER GAADAERDIR GFALKFYTDE
     GNWDLVGNNT PVFFFRDPKL FASLNHAVKR DPRTNMRSAQ NNWDFWTSLP EALHQVTILM
     SDRGIPKGYR NMHGFGSHTY SMYNDKGERV WVKFHHRTQQ GIENLQPDEA AKIIADDRES
     SQRDLFEAIE NKDYPKWKTY IQVMTEEQAR NHKDNPFDLT KVWYKGDYPL IEVGEWELNR
     NPDNYFQDVE QAAFAPTNIV PGIDFSPDKM LQGRLFSYGD AQRYRLGVNH WQIPVNQPKG
     VGVENICPFS RDGQMRILDN NQGGGTHYYP NSDGSFEDQP EFKKPGLKVE GEAYEYDFRQ
     DDDNYFEQPG RLFRLQSKEQ QERIFENTAN EMQGTTLEVQ HRHIRHCYKA DSEYGKGVAR
     ALGVDINDVD LEIKD