ID   CATA1_SOLLC             Reviewed;         492 AA.
AC   P30264;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Catalase isozyme 1;
DE            EC=1.11.1.6;
GN   Name=CAT1;
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].
RX   PubMed=16653169; DOI=10.1104/pp.100.3.1605;
RA   Drory A., Woodson W.R.;
RT   "Molecular cloning and nucleotide sequence of a cDNA encoding catalase from
RT   tomato.";
RL   Plant Physiol. 100:1605-1606(1992).
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; M93719; AAA34145.1; -; mRNA.
DR   RefSeq; NP_001234827.1; NM_001247898.1.
DR   AlphaFoldDB; P30264; -.
DR   SMR; P30264; -.
DR   STRING; 4081.Solyc12g094620.1.1; -.
DR   PaxDb; P30264; -.
DR   PRIDE; P30264; -.
DR   GeneID; 543990; -.
DR   KEGG; sly:543990; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   InParanoid; P30264; -.
DR   OrthoDB; 507937at2759; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P30264; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; 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   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 1"
FT                   /id="PRO_0000084944"
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;  56506 MW;  1D84FA6B7F7B4F97 CRC64;
     MDPSKYRPSS AYDTPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYYLIEK LATFDREKIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGAQTPVI CRFSTVVHER GSPESIRDIR
     GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQENW RILDFFSFLP
     ESLHTFAFFY DDVCLPTDYR HMEGFGVHAY QLINKEGKAH YVKFHWKPTC GVKCMSEEEA
     IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQTMDPEDVD KFDFDPLDVT KTWPEDLLPL
     IPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGIYYSEDKL LQTRIFAYAD TQRHRIGPNY
     MQLPVNAPKC GHHNNHRDGA MNMTHRDEEV DYLPSRFDPC RPAEQYPIPS CVLNGRRTNC
     VIPKENNFKQ AGERYRSWEP DRQDRYINKW VESLSDPRVT HEIRSIWISY LSQADKSCGQ
     KVASRLTVKP TM