ID   CATA1_HORVU             Reviewed;         492 AA.
AC   P55307; Q43761;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Catalase isozyme 1;
DE            EC=1.11.1.6;
GN   Name=CAT1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Morex;
RX   PubMed=8555444; DOI=10.1007/bf00014973;
RA   Skadsen R.W., Schulze-Lefert P., Herbst J.M.;
RT   "Molecular cloning, characterization and expression analysis of two
RT   catalase isozyme genes in barley.";
RL   Plant Mol. Biol. 29:1005-1014(1995).
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   -!- TISSUE SPECIFICITY: In whole endosperms (aleurones plus starchy
CC       endosperm), in isolated aleurones and in developing seeds.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U20777; AAA96947.1; -; mRNA.
DR   EMBL; U16132; AAA62306.1; -; mRNA.
DR   PIR; S62696; S62696.
DR   AlphaFoldDB; P55307; -.
DR   SMR; P55307; -.
DR   PRIDE; P55307; -.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0623480.1; HORVU.MOREX.r2.7HG0623480.1; HORVU.MOREX.r2.7HG0623480.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0623480.1.mrna1; HORVU.MOREX.r2.7HG0623480.1.mrna1; HORVU.MOREX.r2.7HG0623480.1.
DR   Gramene; HORVU.MOREX.r2.7HG0623480.1; HORVU.MOREX.r2.7HG0623480.1; HORVU.MOREX.r2.7HG0623480.
DR   Gramene; HORVU.MOREX.r2.7HG0623480.1.mrna1; HORVU.MOREX.r2.7HG0623480.1.mrna1; HORVU.MOREX.r2.7HG0623480.1.
DR   ExpressionAtlas; P55307; baseline and differential.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
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:0007623; P:circadian rhythm; IEA:EnsemblPlants.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:1900034; P:regulation of cellular response to heat; IEA:EnsemblPlants.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR   GO; GO:0009646; P:response to absence of light; IEA:EnsemblPlants.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblPlants.
DR   GO; GO:0009751; P:response to salicylic acid; IEA:EnsemblPlants.
DR   GO; GO:1902074; P:response to salt; IEA:EnsemblPlants.
DR   GO; GO:0009414; P:response to water deprivation; 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.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme 1"
FT                   /id="PRO_0000084941"
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;  56586 MW;  5917F285FD75D725 CRC64;
     MDPYKHRPTS GANSAYWTTN SGAPVWNNNN ALTVGHRGPI LLEDYHLIEK LAQFDRERIP
     ERVVHARGAS AKGFFEVTHD VSQLTCADFL RAPGVQTPVI VRFSTVVHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNM PVFFIRDGMK FPDMVHAFKP SPKTNMQENW RVVDFFSHHP
     ESLHMFTFLF DDVGIPLNYR HMDGFGVNTY TLISRDGKAH LVKFHWKPTC GVKCLLDDEA
     VTVGGTCHTH ATKDLTDSIA AGNYPEWKLF IQTIDADHED RFDFDPLDVT KTWPEDIIPL
     QPVGRMVLNK NIDNFFAENE QLAFCPAVTV PGIHYSDDKL LQTRIFSYAD TQRHRLGPNY
     LMLPVNAPKC AHHNNHHDGL MNFIHRDEEV NYFPSRFDPT RHAEKYPMPP RVLSGCREKC
     IIDKENNFKQ AGERYRSFDP ARQDRFLQRW VDALTDARVT HEIQSIWVSY WSQCDASLGQ
     KLASRLKIKP NM