ID   CATA2_CUCPE             Reviewed;         492 AA.
AC   P48351;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Catalase isozyme 2;
DE            EC=1.11.1.6;
GN   Name=CAT2;
OS   Cucurbita pepo (Vegetable marrow) (Summer squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=9037166; DOI=10.1023/a:1005742916292;
RA   Esaka M., Yamada N., Kitabayashi M., Setoguchi Y., Tsugeki R., Kondo M.,
RA   Nishimura M.;
RT   "cDNA cloning and differential gene expression of three catalases in
RT   pumpkin.";
RL   Plant Mol. Biol. 33:141-155(1997).
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; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: High levels in green cotyledons, mature leaf, stem
CC       and green hypocotyl.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; D55646; BAA09507.1; -; mRNA.
DR   PIR; T09754; T09754.
DR   AlphaFoldDB; P48351; -.
DR   SMR; P48351; -.
DR   PRIDE; P48351; -.
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..492
FT                   /note="Catalase isozyme 2"
FT                   /id="PRO_0000084936"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         347
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;  56953 MW;  1D3C97F8E026D600 CRC64;
     MDPYKYRPSS AYNTPFCTTN SGAPIWNNTA VMSVGERGPI LLEDYQLIEK IATFTRERIP
     ERVVHARGAS AKGFFEVTHD VSDLSCADFL RAPGVQTPVI VRFSTVIHER VSPETVRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFVRDAMQ FPDVIRAFKP NPKSHLQESW RFLDFCSYHP
     ESLLSFAWFY DDVGIPINYR HMEGFGVQAY SLINKAGKAR LVKFHWKPTC GVKSMLEEEA
     IRVGGSNHSH ATQDLYESIA AGNFPEWRLY IQTIDYEDQN NYDFEPLDTT IAWPEDVVPL
     RPVGRLVLNK NIDNFFAENE MLAFSMSLVP GIHYSDDKML QARSFAYADT QRHRLGPNYL
     QLPVNAPKCP HHNNHHEGFM NFMHRDEEVN YFPSRYDACR HAEKYPMPPN VLSGKRERCV
     IPKENHNFKQ AGDRYRSWAP DRQERFVNRF VEALSDSKVT HEVRNIWISY WTQADRSLGQ
     KIASRMNARP NM