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 24-JAN-2024, entry version 104.
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.P55313; -.
DR PaxDb; 4565-Traes_7DL_44F6042FE-1; -.
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:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0009628; P:response to abiotic stimulus; IEA:UniProt.
DR GO; GO:0009725; P:response to hormone; IEA:UniProt.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR CDD; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
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; CATALASE; 1.
DR PANTHER; PTHR11465:SF60; CATALASE ISOZYME B; 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; Heme-dependent catalase-like; 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
//
