ID   CATA_LATSK              Reviewed;         478 AA.
AC   P30265;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA;
OS   Latilactobacillus sakei (Lactobacillus sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=1599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LTH677;
RX   PubMed=1575485; DOI=10.1128/aem.58.3.832-839.1992;
RA   Knauf H.J., Vogel R.F., Hammes W.P.;
RT   "Cloning, sequence, and phenotypic expression of katA, which encodes the
RT   catalase of Lactobacillus sake LTH677.";
RL   Appl. Environ. Microbiol. 58:832-839(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC   STRAIN=LTH677;
RX   PubMed=9546173; DOI=10.1128/aem.64.4.1359-1365.1998;
RA   Hertel C., Schmidt G., Fischer M., Oellers K., Hammes W.P.;
RT   "Oxygen-dependent regulation of the expression of the catalase gene katA of
RT   Lactobacillus sakei LTH677.";
RL   Appl. Environ. Microbiol. 64:1359-1365(1998).
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; M84015; AAC19139.1; -; Genomic_DNA.
DR   PIR; T09652; T09652.
DR   AlphaFoldDB; P30265; -.
DR   SMR; P30265; -.
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   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   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..478
FT                   /note="Catalase"
FT                   /id="PRO_0000084989"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         336
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   478 AA;  54076 MW;  85952A05DB16EF3D CRC64;
     MTNQLTTNEG QPWADNQHSQ TAGQRGPVLI QDYQLLEKLA HFNRERIPER VVHAKGAGAK
     GYFKVTKDMS AYTKAAVFSG VGKKTPLITR FSQVAGEAGY PDTYRDVRGF AVKFYTEEGN
     YDIVGNNTPV FFVNDPLKFP DFIHSQKRDP RTHARSQDMQ WDFWSLSPES VHQVTILMSD
     RGIPASYRMM HGFGSHTFKW VNAQGEQFWV KYHFKTNQGI HNLSNELADE LAGKDTDYLQ
     NDLFDAIETG DYPSWTVAVQ LVPYEDGLNY PQDIFDVTKV ISQKDYPLIE IGQMVLDENP
     TNNFEDIQEL AFSPANLVPG IEASPDKLLQ GRLFGYKDAE RYRLGANYEQ LPVNRPKVPV
     HNYERDGAMA QNQATGVNYE PNSQDGPTEV PAAKIHGDQL SGTTGNFSAD PDYYSAAGKL
     YRLLSADEQT RLIENIRMNL GQVTKPEIQI REVKQFYQAD PEYGRRVATS VKLRFSSV