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-MAY-2013, entry version 54.
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC -!- COFACTOR: Heme group (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the catalase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI80881.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ938182; CAI80881.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_416670.1; NC_007622.1.
DR HSSP; P77872; 2A9E.
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 ProtClustDB; CLSK885283; -.
DR BioCyc; SAUR273036:GJVS-1214-MONOMER; -.
DR GO; GO:0004096; F:catalase activity; IEA: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; Catalase_N; 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 By similarity.
FT ACT_SITE 129 129 By similarity.
FT METAL 339 339 Iron (heme axial ligand) (By similarity).
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
//
