ID   CATA2_SOLLC             Reviewed;         492 AA.
AC   Q9XHH3;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Catalase isozyme 2;
DE            EC=1.11.1.6;
GN   Name=CAT2;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kerdnaimongkol K., Woodson W.R.;
RT   "Cloning of a cDNA encoding catalase from tomato.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AF112368; AAD41256.1; -; mRNA.
DR   AlphaFoldDB; Q9XHH3; -.
DR   SMR; Q9XHH3; -.
DR   STRING; 4081.Solyc02g082760.2.1; -.
DR   PaxDb; Q9XHH3; -.
DR   PRIDE; Q9XHH3; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   InParanoid; Q9XHH3; -.
DR   BRENDA; 1.11.1.6; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q9XHH3; baseline and differential.
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; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme 2"
FT                   /id="PRO_0000084945"
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   492 AA;  56778 MW;  E43B4773BD5229F6 CRC64;
     MDPYKYRPSS AFNSPFCTTN SGAPVFNNNS SLTVGARGPV LLEDYHLVEK LANFDRERIA
     ERVVHARGAS AKGFFEVTHD IAHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHALKP NPKSHIQENW RVLDFFSHHP
     ESLHMFTFLF DDIGIPQDYR HMDGSGVHTF TLINRAGKST YVKFHWKPTC GVKSLLEEKA
     IRVGGANHSH ATQDLYDSIA AGNYPEWKPS IQIMGPEHED KFDFDPLDVT KTWPEDILPL
     QPVGRLVLNK NIDNFLYMNE QLAFCPSIVV PGVYYSDDKM LQTRIFSYSD TQRYRLGPNY
     LQLPANAPKC AHHNNHYDGS MNFMHRDEEI DYFPSRYDQV RHAEVYPIPS TVCSGKREKC
     IIQKENNFKQ PGERYRSFTP DRQERFIRRW VEALSDPRIT YEIRSIWITY WSQADKSLGQ
     KLASRLNVRP SI