ID   CATA_LISMO              Reviewed;         488 AA.
AC   Q8Y3P9;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=kat; OrderedLocusNames=lmo2785;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591984; CAD00998.1; -; Genomic_DNA.
DR   PIR; AH1422; AH1422.
DR   RefSeq; NP_466307.1; NC_003210.1.
DR   RefSeq; WP_010990069.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y3P9; -.
DR   SMR; Q8Y3P9; -.
DR   STRING; 169963.lmo2785; -.
DR   PaxDb; Q8Y3P9; -.
DR   PRIDE; Q8Y3P9; -.
DR   EnsemblBacteria; CAD00998; CAD00998; CAD00998.
DR   GeneID; 984948; -.
DR   KEGG; lmo:lmo2785; -.
DR   PATRIC; fig|169963.11.peg.2855; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_4_0_9; -.
DR   OMA; HVWPQKQ; -.
DR   PhylomeDB; Q8Y3P9; -.
DR   BioCyc; LMON169963:LMO2785-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..488
FT                   /note="Catalase"
FT                   /id="PRO_0000085016"
FT   REGION          1..26
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;  55888 MW;  95EB6097F5591734 CRC64;
     MTDRKNLTTN QGVPVGDNQN SMTAGRKGPT LIEDYVLIEK LAHFDRERVP ERVVHARGAG
     AHGKFVTKKS MKKYTMAKFL QEEGTETEVF ARFSTVIHGQ HSPETLRDPR GFSVKFYTEE
     GNYDFVGNNL PVFFIRDAIK FPDVIHSLKP DPRTNIQDGN RYWDFFSLTP EATTMIMYLF
     SDEGTPASYR EVRGSSVHAF KWINEEGKTV YVKLRWVPKA GIVNLSTEQA SQIQAKEFNH
     ASRDLYEAIE NGDYPEWDLY VQVLDPKDLD SFDFNPLDAT KDWFEDVFPY EHVGTMTLDR
     NPDNIFAETE SVGFNPGVLV RGMLPSEDRL LQGRLFSYSD TQRHRVGPNY LQLPINSPKA
     PVANNQRDGH MPFKQQTSSI NYEPNSYDTE PKENPAFIEP EQEIRGDISG RLIAEKPNNF
     GHAKEVWDRY SNAERAALVK NIVDDWSQVR EDIKIRNLRN FYQVDPEFAS RVAAGTGINL
     EEHVTDLK