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Database: UniProt
Entry: Q2YXT2
LinkDB: Q2YXT2
Original site: Q2YXT2 
ID   CATA_STAAB              Reviewed;         505 AA.
AC   Q2YXT2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   01-OCT-2014, entry version 59.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=SAB1192;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen;
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000255|PROSITE-ProRule:PRU10013}.
CC   -!- COFACTOR: Heme group. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI80881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ938182; CAI80881.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_416670.1; NC_007622.1.
DR   ProteinModelPortal; Q2YXT2; -.
DR   SMR; Q2YXT2; 6-488.
DR   STRING; 273036.SAB1192; -.
DR   PRIDE; Q2YXT2; -.
DR   EnsemblBacteria; CAI80881; CAI80881; SAB1192.
DR   GeneID; 3794552; -.
DR   KEGG; sab:SAB1192; -.
DR   PATRIC; 19523249; VBIStaAur92441_1273.
DR   eggNOG; COG0753; -.
DR   HOGENOM; HOG000087852; -.
DR   KO; K03781; -.
DR   OrthoDB; EOG6P5Z9F; -.
DR   BioCyc; SAUR273036:GJVS-1214-MONOMER; -.
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   Gene3D; 2.40.180.10; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR020835; Catalase-like_dom.
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   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   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN         1    505       Catalase.
FT                                /FTId=PRO_0000278272.
FT   ACT_SITE     56     56       {ECO:0000255|PROSITE-ProRule:PRU10013}.
FT   ACT_SITE    129    129       {ECO:0000255|PROSITE-ProRule:PRU10013}.
FT   METAL       339    339       Iron (heme axial ligand). {ECO:0000250}.
SQ   SEQUENCE   505 AA;  58380 MW;  F6A17136A32DCBCC CRC64;
     MSQQDKKLTG VFGHPVSDRE NSMTAGPRGP LLMQDIYFLE QMSQFDREVI PERRMHAKGS
     GAFGTFTVTK DITKYTNAKI FSEIGKQTEM FARFSTVAGE RGAADAERDI RGFALKFYTE
     EGNWDLVGNN TPVFFFRDPK LFVSLNRAVK RDPRTNMRDA QNNWDFWTGL PEALHQVTIL
     MSDRGIPKDL RHMHGFGSHT YSMYNDSGER VWVKFHFRTQ QGIENLTDEE AAEIIATDRD
     SSQRDLFEAI EKGDYPKWTM YIQVMTEEQA KNHKDNPFDL TKVWYHDEYP LIEVGEFELN
     RNPDNYFMDV EQAAFAPTNI IPGLDFSPDK MLQGRLFSYG DAQRYRLGVN HWQIPVNQPK
     GVGIENICPF SRDGQMRVVD NNQGGGTHYY PNNHGKFDSQ PEYKKPPFPT DGYGYEYNQR
     QDDDNYFEQP GKLFRLQSED AKERIFTNTA NAMEGVTDDV KRRHIRHCYK ADPEYGKGVA
     KALGIDINSI DLETENDETY ENFEK
//
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