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   16-JUN-2009, entry version 52.
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Morex;
RX   MEDLINE=96145511; 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
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). Glyoxysome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; U20778; AAA96948.1; -; mRNA.
DR   PIR; S62697; S62697.
DR   HSSP; P46206; 1M7S.
DR   Gramene; P55308; -.
DR   BRENDA; 1.11.1.6; 283.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 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;
KW   Oxidoreductase; Peroxidase; Peroxisome.
FT   CHAIN         1    494       Catalase isozyme 2.
FT                                /FTId=PRO_0000084942.
FT   ACT_SITE     65     65       By similarity.
FT   ACT_SITE    138    138       By similarity.
FT   METAL       348    348       Iron (heme axial ligand) (By similarity).
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
//