ID CATA_STAAC Reviewed; 505 AA.
AC Q5HG86;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; OrderedLocusNames=SACOL1368;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW36617.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000046; AAW36617.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000082539.1; NC_002951.2.
DR AlphaFoldDB; Q5HG86; -.
DR SMR; Q5HG86; -.
DR KEGG; sac:SACOL1368; -.
DR HOGENOM; CLU_010645_2_0_9; -.
DR Proteomes; UP000000530; Chromosome.
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 Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1.
DR PANTHER; PTHR11465:SF61; CATALASE; 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; Heme-dependent catalase-like; 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_0000084997"
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; 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
//
