ID   CATA_LISSE              Reviewed;         488 AA.
AC   P24168;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=kat;
OS   Listeria seeligeri.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1860824; DOI=10.1128/jb.173.16.5159-5167.1991;
RA   Haas A., Brehm K., Kreft J., Goebel W.;
RT   "Cloning, characterization, and expression in Escherichia coli of a gene
RT   encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous
RT   to mammalian catalases.";
RL   J. Bacteriol. 173:5159-5167(1991).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; M75944; AAB53655.1; -; Genomic_DNA.
DR   PIR; A40367; A40367.
DR   AlphaFoldDB; P24168; -.
DR   SMR; P24168; -.
DR   STRING; 683837.lse_2685; -.
DR   eggNOG; COG0753; Bacteria.
DR   SABIO-RK; P24168; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   InterPro; IPR018028; Catalase.
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   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..488
FT                   /note="Catalase"
FT                   /id="PRO_0000085017"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         338
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   488 AA;  55869 MW;  F0A3251469681EBB CRC64;
     MTDRRNLTTN QGVPIGDNQN SMTAGLKGPT LLEDYVLIEK LAHFDRERVP ERVVHARGAG
     AHGKFVTKKS MKKYTKAQFL QEEGTETEVF ARFSTVIHGQ HSPETLRDPR GFSVKFYTEE
     GNYDFVGNNL PVFFIRDAIK FPDVIHSLKP DPRTNIQDGN RYWDFFSLTP EATTMITYLF
     SDEGTPASYR EIRGSSVHAF KWINEEGKTV YVKLRWVPKA GIVNLSTDQA AQIQAKEFNH
     ASRDLYEAIE NGDYPEWDLY VQVLDPKDLD NYDFNPLDAT KDWFEDVFPY EHVGTMTLNR
     NPDNIFAETE SVGFNPGVLV PGMLPSEDRV LQGRLFSYSD TQRHRVGPNY LQLPINSPKT
     PVDNNQRDGQ MPFKQQTSSI NYEPNSYDTE PKENPAYIEP EQEIRGDISG RLVAEKPNNF
     GHAKEVWKRY SDAERAALVK NIVDDWEGVR EDIKIRNLRN FYQVEPEFAE RVAAGTGINL
     AEHVIDLK