CATA_STAAU
ID CATA_STAAU Reviewed; 505 AA.
AC Q9L4S1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12600 / DSM 20231 / IAM 12544 / NCDO 949 / NCTC 8532;
RX PubMed=10708385; DOI=10.1099/00221287-146-2-465;
RA Sanz R., Marin I., Ruiz-Santa-Quiteria J.A., Orden J.A., Cid D., Diez R.M.,
RA Silhadi K.S., Amils R., de la Fuente R.;
RT "Catalase deficiency in Staphylococcus aureus subsp. anaerobius is
RT associated with natural loss-of-function mutations within the structural
RT gene.";
RL Microbiology 146:465-475(2000).
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; AJ000472; CAB76839.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9L4S1; -.
DR SMR; Q9L4S1; -.
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..505
FT /note="Catalase"
FT /id="PRO_0000085002"
FT REGION 1..25
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 505 AA; 58324 MW; BEEB05FBB0AE172F 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
RNPDNYFTDV EQAAFAPTNI IPGLDFSPDK MLQGRLFSYG DAQRYRLGVN HWQIPVNQPK
GVGIENICPF SRDGQMRVVD NNQGGGTHHY PNNHGKFDSQ PEYKKPPFPT DGYGYEYNQR
QDDDNYFEQP GKLFRLQSED AKERIFTNTA NAMEGVTDDV KRRHIRHCYK ADPEYGKGVA
KALGIDINSI DLETENDETY ENFEK