ID   CATA1_RICCO             Reviewed;         492 AA.
AC   Q01297;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Catalase isozyme 1;
DE            EC=1.11.1.6;
GN   Name=CAT1;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Hypocotyl;
RX   PubMed=8049373; DOI=10.1007/bf00043878;
RA   Suzuki M., Ario T., Hattori T., Nakamura K., Asahi T.;
RT   "Isolation and characterization of two tightly linked catalase genes from
RT   castor bean that are differentially regulated.";
RL   Plant Mol. Biol. 25:507-516(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 404-492.
RC   STRAIN=cv. Hale;
RX   PubMed=1712298; DOI=10.1111/j.1432-1033.1991.tb16111.x;
RA   Gonzalez E.;
RT   "The C-terminal domain of plant catalases. Implications for a glyoxysomal
RT   targeting sequence.";
RL   Eur. J. Biochem. 199:211-215(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. Glyoxysome
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Abundant in endosperms and cotyledons. Only in
CC       small amount in root.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; D21161; BAA04697.1; -; Genomic_DNA.
DR   EMBL; X59694; CAA42215.1; -; mRNA.
DR   PIR; S46297; S46297.
DR   AlphaFoldDB; Q01297; -.
DR   SMR; Q01297; -.
DR   PRIDE; Q01297; -.
DR   InParanoid; Q01297; -.
DR   GO; GO:0009514; C:glyoxysome; 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   Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Peroxisome.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme 1"
FT                   /id="PRO_0000084956"
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"
FT   CONFLICT        439
FT                   /note="A -> P (in Ref. 2; CAA42215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="F -> S (in Ref. 2; CAA42215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="L -> F (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="D -> E (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="H -> Q (in Ref. 2; CAA42215)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   492 AA;  56464 MW;  B5E28A425088BF63 CRC64;
     MDPYRNRPSS GFNTPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLIEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDVVHAFKP NPKSHLQENW RIFDFLSHVP
     ESLHMLTFLL DDLGIPQDYR HMEGSGVNTY TLINKAGKVH YVKFHWKPTC GVKCLLENEA
     IKVGGSNHSH ATQDLYDSIS AGNYPEWKLY IQIMDPAHED KFDFDPLDVT KTWPEDILPL
     QPVGRLVLNK NIDNFFAENE QLAFCPGIVV PGVSYSEDKL LQTRIFSYSD TQRHRLGPNY
     LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRCDPA RNAESFPVPS AICSGKREKC
     VIEKENNFKQ PGERYRSWAP DRQERFLNRL VGGLSDPRIT HELRTIWISY WIQCDKSLGQ
     KLATRLNVKP SI