ID   CATA3_CUCPE             Reviewed;         492 AA.
AC   P48352;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Catalase isozyme 3;
DE            EC=1.11.1.6;
GN   Name=CAT3;
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:0000250}.
CC   -!- TISSUE SPECIFICITY: Abundant in green cotyledons, etiolated cotyledons,
CC       green hypocotyl and root, but not in young leaf.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; D55647; BAA09508.1; -; mRNA.
DR   PIR; T09756; T09756.
DR   AlphaFoldDB; P48352; -.
DR   SMR; P48352; -.
DR   PRIDE; P48352; -.
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 3"
FT                   /id="PRO_0000084937"
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;  57137 MW;  8FDBEC7751660A6A CRC64;
     MDPYKYRPSS AYNTPFCTTN SGAPIWNNTA VMSVGERGPI LLEDYQLIEK IATFTRERIP
     ERVVHRRGAS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFVRDAMQ FPDVIRAFKP NPKSHLQEPW RYLDFCSYHP
     ESLLSFAWFY DDVGIPINYR HMEGFGVQAY SLINKSGKAR LVKFHWKPTC GVKSMMEEEA
     IRIGGTNHSH ATQDLYESIA AGNFPEWRLY IQTIDYEDQN KYDFEPLDTT ITWPEDVVPL
     QPVGRLVLNK NIDNFFAENE MLAFSMSLVP GIHYSDDKML QARSFAYADT QRHRLGPNYL
     QLPVNAPKCP HHNNHHEGFM NFMHRDEEVN YFPSRYDPCR HAEKFPMPPN VLTGKRERCV
     IPKENNNFKQ AGDRYRSWAP DRQDRFVKRF VEALSDPRVT DEVRNIWISY WSQADRSLGQ
     KIASRLNVRP NI