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   25-NOV-2008, entry version 51.
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; 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   -!- TISSUE SPECIFICITY: In whole endosperms (aleurones plus starchy
CC       endosperm), in isolated aleurones and in developing seeds.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; U20777; AAA96947.1; -; mRNA.
DR   EMBL; U16132; AAA62306.1; -; mRNA.
DR   PIR; S62696; S62696.
DR   HSSP; P46206; 1M7S.
DR   Gramene; P55307; -.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-KW.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
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; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 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    492       Catalase isozyme 1.
FT                                /FTId=PRO_0000084941.
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   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
//