CATA1_WHEAT
ID CATA1_WHEAT Reviewed; 492 AA.
AC Q43206;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Catalase-1;
DE EC=1.11.1.6;
GN Name=CAT1;
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 Saruyama H., Matsumura T.;
RL Submitted (JUL-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; Evidence={ECO:0000250};
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; D86327; BAA13068.1; -; mRNA.
DR PIR; T06478; T06478.
DR AlphaFoldDB; Q43206; -.
DR SMR; Q43206; -.
DR STRING; 4565.Traes_4DL_4FC0D4B27.1; -.
DR PRIDE; Q43206; -.
DR eggNOG; KOG0047; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q43206; 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 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-1"
FT /id="PRO_0000084967"
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; 56808 MW; 52899174D5BA2EAB CRC64;
MDPYKYRPSS SFNAPMWSTN SGAPVWNNDN SLTVGSRGPI LLEDYHLVEK IADFDRERIP
ERVVHARGAT AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
GFAIKFYTRE GNWDLVGNNF PVFFIRDGMK FPDMVHALKP NPKTHIQENW RILDFFSHHP
ESLHMFTFLF DDIGVPADYR HMDGSGVNTY TLVNRAGKAH YVKFHWKPTC GVKSLLEEEA
VTVGGTNHSH ATKDLTDSIA AGNYPEWTFY IQTIDPDYEE RFDFDPLDVT KTWPEDVVPL
QPVGRLVLNR NIDNFFSENE QLAFCPGIIV PGVYYSDDKL LQTRIFSYSD TQRHRLGPNY
LLLPANAPKC SHHNNHYDGL MNFMHRDEEV DYFPSRFDPA KHAPRYPIPS RTLNGRREKM
VIEKENNFKQ PGERYRSMDP ARQERFINRW IDALSDPRLT HEIKAIWLSY WSQADKSLGQ
KLASRLSSKP SM