ID   CATA_PEA                Reviewed;         494 AA.
AC   P25890;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=1932700; DOI=10.1007/bf00028744;
RA   Isin S.H., Allen R.D.;
RT   "Isolation and characterization of a pea catalase cDNA.";
RL   Plant Mol. Biol. 17:1263-1265(1991).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to 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   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; X60169; CAA42736.1; -; mRNA.
DR   PIR; S18346; CSPM.
DR   AlphaFoldDB; P25890; -.
DR   SMR; P25890; -.
DR   PeroxiBase; 398; PsKat01.
DR   PRIDE; P25890; -.
DR   GO; GO:0005777; C:peroxisome; 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   2: Evidence at transcript level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Peroxisome.
FT   CHAIN           1..494
FT                   /note="Catalase"
FT                   /id="PRO_0000084954"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         348
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   494 AA;  57345 MW;  B5FC08E66B13B266 CRC64;
     MDPYKHRPSS AFNSPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLVEK LAQFDRERIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNYDLVGNNF PVFFVHDGMN FPDMVHALKP NPQTHIQENW RILDFFYNFP
     ESLHMFSFLF DDVGVPQDYR HMDGFGVNTY TLINKAGKSV YVKFHWKPTC GVKCLLEEEA
     IQVGGSNHSH ATKDLYDSIA AGNYPEWKLY IQTIDPAHED RFEFDPLDVT KTWPEDIIPL
     QPVGRMVLNK NIDNFFAENE QLAFCPAIML PGIYYSDDKM LQTRVFSYAD SQRHRLGPNY
     LQLPVNAPKW SHHNNHHEGF MNAIHRDEEV NYFPSRHDTV RHAERVPIPT THLSARREKC
     NIPKQNHFKQ AGERYRTWAP DRQERFLRRW VEALSDTDPR ITHEIRSIWV SYWSQADRSL
     GQKLASHLNM RPSI