ID   CATA2_HORVU             Reviewed;         494 AA.
AC   P55308;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Catalase isozyme 2;
DE            EC=1.11.1.6;
GN   Name=CAT2;
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   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U20778; AAA96948.1; -; mRNA.
DR   PIR; S62697; S62697.
DR   AlphaFoldDB; P55308; -.
DR   SMR; P55308; -.
DR   PRIDE; P55308; -.
DR   ExpressionAtlas; P55308; baseline and differential.
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; 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..494
FT                   /note="Catalase isozyme 2"
FT                   /id="PRO_0000084942"
FT   REGION          1..29
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        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   494 AA;  56913 MW;  67E3CF2AD02E542E CRC64;
     MDPCKFRPSS SFDTKTTTTN AGQPVWNDNE ALTVGPRGPI LLEDYHLLEK IAHFARERIP
     ERVVHARGAS AKGFFECTHD VTGLTCADFL RAPGARTPVI VRFSTVIHER GSPETIRDPR
     GFAVKFYTRE GNWDLLGNNF PVFFIRDGIK FPDVIHAFKP NPKSHVQEYW RVFDFLSHHP
     ESLHTFFFLF DDVGIPTDYR HMDGFGVNTY TFVSRAGKSH YVKFHWRPTC GVSCLMDDEA
     TLVGGKNHSH ATQDLYDSID AGNFPEWKLF VQVIDPDEED RFDFDPLDDT KTWPEDLVPL
     QPVGRLVLDR NVDNFFNENE QLAFGPGLVV PGIYYSDDKM LQCRVFAYAD TQRYRLGPNY
     LMLPVNAPKC GFKNNHYDGA MNFMHRDEEV DYYPSRHAPL RHAEPASFPV PTRPVVGKRE
     KTRIKKENDF VQPGERYRSW APDRQDRFVR RFSDALAHPK VSHELRVIWI DFLSKCDKSC
     GMKVANRLNV KPSM