ID   CATA_PSEPU              Reviewed;         479 AA.
AC   Q59714;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; Synonyms=catA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Corvallis;
RX   PubMed=9358059; DOI=10.1016/s0378-1119(97)00370-3;
RA   Kim Y.C., Miller C.D., Anderson A.J.;
RT   "Identification of adjacent genes encoding the major catalase and a
RT   bacterioferritin from the plant-beneficial bacterium Pseudomonas putida.";
RL   Gene 199:219-224(1997).
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   -!- ACTIVITY REGULATION: Activated by peroxide.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U63511; AAB88219.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59714; -.
DR   SMR; Q59714; -.
DR   STRING; 1240350.AMZE01000022_gene1307; -.
DR   eggNOG; COG0753; Bacteria.
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   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..479
FT                   /note="Catalase"
FT                   /id="PRO_0000084995"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
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   479 AA;  53381 MW;  EFE3CBDE67778571 CRC64;
     MSKILTTASG APVADNQNSR SAGPRGPLLL DDFHLIEKLA HFNRENIPER RVHAKGSGAY
     GTFTVTRDIT GYTSAKLFEQ VGKQTETFLR FSTVGGERGS ADTERDPRGF AVKFYTEEGN
     WDIVGNNTPV FFIRDPLKFP DFIHTQKRHP QSNLKNAQIF WDSWSHSPEA LHQVTILFSD
     RGIPDGYRHM HGFGSHTYSL INAQGERTWV KWHFKTQQGI KNLAPADAAR LAGTDPDYAQ
     RDLFEAIERG DYPRWTVCIQ VMSEAEAASR DENPFDVTKT WSQKDYPLIE VGVLELNRNP
     LNYFAEVEQA AFGPSNMVPG VGLSPDRMLQ GRVFAYADAH RYRVGTNHQQ LPVNAPRCPV
     NSYQRDGSMA TGSYGSAPNY EPNSYAAAPK QSPRHAEPAL ALNGSADRYD HREDADYYSH
     AGALFRLMSD EQKALLISNI AGTMAGVSEN VIQRQLQYFF KADPAYGEGI AKGLGINLA