ID Q6PXW7_STAXY Unreviewed; 459 AA.
AC Q6PXW7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
DE Flags: Fragment;
GN Name=katA {ECO:0000313|EMBL:AAS78562.1};
OS Staphylococcus xylosus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288 {ECO:0000313|EMBL:AAS78562.1};
RN [1] {ECO:0000313|EMBL:AAS78562.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DS20 {ECO:0000313|EMBL:AAS78558.1}, S480
RC {ECO:0000313|EMBL:AAS78562.1}, and S878 {ECO:0000313|EMBL:AAS78564.1};
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 (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000720,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR EMBL; AY571731; AAS78558.1; -; Genomic_DNA.
DR EMBL; AY571735; AAS78562.1; -; Genomic_DNA.
DR EMBL; AY571737; AAS78564.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6PXW7; -.
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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|RuleBase:RU000498};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}.
FT DOMAIN 1..376
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 107
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 317
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:0000256|PIRSR:PIRSR038928-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAS78562.1"
FT NON_TER 459
FT /evidence="ECO:0000313|EMBL:AAS78562.1"
SQ SEQUENCE 459 AA; 53205 MW; EFE6721366135732 CRC64;
MTAGPRGPLL MQDIYFLEQM AHFDREVIPE RRMHAKGSGA FGTFTVTNDI TKYTCASIFA
EVGKQTEMFA RFSTVAGERG AGDAERDIRG FALKFYTDEG NWDLVGNNTP VFFFRDPKLF
PSLNHVVKRN PKTNMKDPQA NWDFWTLLPE ALHQITILMT DRGIPKGFRN MHGFGSHTYS
MYNDKGERFW VKFHHRTQQG IENYSAEEAE QVMAKDRDSS QRDLFNNIEQ GNFPKWKMYI
QVMTEEQARN HKDNPFDLTK VWYKDEYPLI EVGEFELNRN PENYFQDVEQ AAFAPTNIVP
GLDFSPDKML QGRLFSYGDT QRYRLGVNHW QIPVNQPKGV GMENICPFSR DGQMRILDNN
QGASTHYYPN SNGAFEDQPQ YKKPALDIQG QAYEYDFRED DDNYFEQPGK LFRLLSSEEQ
QILFNNTANE MSPVTDALKH RHIRHCYKAD PAYGQGVAE
//
