ID   CATA2_RICCO             Reviewed;         492 AA.
AC   P49318;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Catalase isozyme 2;
DE            EC=1.11.1.6;
GN   Name=CAT2;
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).
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   -!- 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 hypocotyls and roots. Low levels are
CC       seen in the endosperms and cotyledons.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; D21162; BAA04698.1; -; Genomic_DNA.
DR   PIR; S46298; S46298.
DR   AlphaFoldDB; P49318; -.
DR   SMR; P49318; -.
DR   STRING; 3988.XP_002510677.1; -.
DR   PRIDE; P49318; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   InParanoid; P49318; -.
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; 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; 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 2"
FT                   /id="PRO_0000084957"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
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;  57172 MW;  DDB84B8FC652B202 CRC64;
     MDPYKFRPSS SNDTPFWTTN AGDPVSNNNS SMTVGPRGPI LLEDYHMIEK LANFTRERIP
     ERVVHARGMS AKGFFEVTHD VTDLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFATKFYTRE GNFDIVGNNF PVFFIRDGIK FPDVVHAFKP NPKSHIQEYW RIFDFCSHHP
     ESLSTFAWFF DDVGIPQDYR HMEGFGVHTY CLINKAGKVT YVKFHWKPTC GVKCLMDDEA
     IKVGGANHSH ATQDLYDSIA AGNFPEWKLM IQTMDPADED KFSFDPLDMT KIWPEDMFPL
     HPVGRLVLNR NIDNWFAENE MLAFNPAHVV PGVYYSNDKL FQLRLFAYSD TQRHRLGTNY
     LQLPVNAPKC PYHNNHYDGF MNFMHRDEEV DYFQSRYDPV RHAEKVPIPN AICSGRREKC
     VIEKEDNFRQ PGDRYRSWAP DRQERFLCRL VNALSEPRIT HEIRSIWVSW WTQCDKSLGQ
     KLASRLNVRP NI