ID   CATA_SECCE              Reviewed;         492 AA.
AC   P55310;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
OS   Secale cereale (Rye).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
OX   NCBI_TaxID=4550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Halo; TISSUE=Leaf;
RA   Schmidt M.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
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. {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; Z54143; CAA90858.1; -; mRNA.
DR   AlphaFoldDB; P55310; -.
DR   SMR; P55310; -.
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:0009628; P:response to abiotic stimulus; IEA:UniProt.
DR   GO; GO:0009725; P:response to hormone; IEA:UniProt.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:UniProt.
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"
FT                   /id="PRO_0000084958"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000250"
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;  56600 MW;  D725C042259AE494 CRC64;
     MDPCKFRPSS SFDTKTTTTN PGQPVWNDNE ALTVGPRGPI LLEDYHLLEK IAHFARDIPE
     PFVHAGRASA KGFFECTHDV TGLTCADFLP SPGAGTPVIV RFSTVIHERG SPETIRDPRG
     FAVKFYTREG NWDLLGNNFP VFFIRDGIKF PDVIHAFKPN PKSHVQEYWR VFDFLPHHPE
     SLHTFFFLFD DVGIPTDYRH MDGFGVNTYT FVTRAGKSHY IKFHWRPTCG VSCLMDDEAT
     LVGGKNHSHA TQDLYDSIDA GNFPEWKLFV QVIDPEQQDR FDFDPLDDTK TWPEDLVPLQ
     PVGRLVLDRN VDNFFNENEQ LAFGPGLVVP GIYYSDDKML QCRVFAYADT QRYRLGPNYL
     MLPVNAPKCG FKKNHYDGAM NFMHRDEEVD YYPSRHAPLR HAEPASFPVP TRPVVGKREK
     TRIKKENDFV QPGERYRSWA PDRQDRFVAL RRRLAHPKVS HELRVIWIDF LSKCDKSCGM
     KVANRLNVKP SM