ID   CATA2_WHEAT             Reviewed;         492 AA.
AC   P55313;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=CATA;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Song Z., Zhu Y., Huiliu G.J.;
RL   Submitted (JAN-1996) 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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
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; X94352; CAA64077.1; -; mRNA.
DR   AlphaFoldDB; P55313; -.
DR   SMR; P55313; -.
DR   STRING; 4565.Traes_7DL_44F6042FE.1; -.
DR   PRIDE; P55313; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P55313; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblPlants.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IEA:EnsemblPlants.
DR   GO; GO:0009970; P:cellular response to sulfate starvation; IEA:EnsemblPlants.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR   GO; GO:0009416; P:response to light stimulus; IEA:EnsemblPlants.
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; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase"
FT                   /id="PRO_0000084968"
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"
SQ   SEQUENCE   492 AA;  56480 MW;  CFAED23345ED3C94 CRC64;
     MDPYKHRPTS GANSAYWTTN SGAPVWNNNN ALTVGHRGPI LLEDYHLIEK LAQFDRERIP
     ERVVHARGAS AKGFFEVTHD VSQLTCADFL RAPGVQTPVI VRFSTVVHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNM PVFFIRDGMK FPDMVHAFKP SSKTNMQENW RVVDFFSHHP
     ESLHMFTFLF DDVGIPLNYR HMDGFGVNTY TLISRDGKAH LVKFHWKPTC GVKCLLDDEA
     VTVGGTCHTH ATKDLTDSIA AGNYPEWKLF IQTIDADHED RFDFDPLDVT KTWPEDIIPL
     QPVGRMVLNK NIDNFFAENE QLAFCPAVTV PGIHYSDDKL LQTRIFSYAD TQRHRLGPNY
     LMLPVNAPKC AHHNNHHDGL MNFIHRDEEV NYFPSRVDPT RHAEKDPMPP RVLSGCREKC
     IIDKENNFKQ AGERYRSFDP ARQDRFLQRW VDALTDARVT HEIQSIWVSY WSQCDASLGQ
     KLASRLKIKP NM