ID   CATA1_SOLTU             Reviewed;         492 AA.
AC   P49284;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Catalase isozyme 1;
DE            EC=1.11.1.6;
GN   Name=CAT1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Russet Burbank-0; TISSUE=Root;
RA   Wu G., Shah D.M.;
RT   "Isolation and characterization of a potato catalase cDNA.";
RL   (er) Plant Gene Register PGR95-037(1995).
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}. Glyoxysome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U27082; AAA80650.1; -; mRNA.
DR   AlphaFoldDB; P49284; -.
DR   SMR; P49284; -.
DR   PRIDE; P49284; -.
DR   ProMEX; P49284; -.
DR   InParanoid; P49284; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P49284; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
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   Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Peroxisome; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme 1"
FT                   /id="PRO_0000084961"
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;  56370 MW;  D55F0581ADF9E77B CRC64;
     MDPSKYRPSS AYDTPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYYLIEK LATFDREKIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGAQTPVI CRFSTVVHER GSPESIRDIR
     GFGVKFYNRG GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQEDW RTLDFFSFLP
     ESLHTFAFFY DDVCLPTDYR HMEGFGVHAY QLINKEGKAH YVKFHWKPTC GVKCMSEEEA
     IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQTMDPEDVD KFDFDPLDVT KTWPEDLLPL
     IPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGIYYSEDKL LQTRIFAYAD TQRHRIGPNY
     MQLPVNAPKC GHHNNHRDGA MNMTHRDEEV DYFPSRFDPC RPAEQYPIPA CVLNGRRTNC
     VIPKENNSKQ AGERYRSWES DRQDRYINKW VESLSDPRVT HEIRSIWISY LSQADKSCGQ
     KVASRLTVKP TM