ID   CATA2_RICCO             Reviewed;         492 AA.
AC   P49318;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-NOV-2008, entry version 49.
DE   RecName: Full=Catalase isozyme 2;
DE            EC=1.11.1.6;
GN   Name=CAT2;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Malpighiales; Euphorbiaceae; Acalyphoideae;
OC   Acalypheae; Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Hypocotyl;
RX   MEDLINE=94325474; PubMed=8049373; DOI=10.1007/BF00043878;
RA   Suzuki M., Ario T., Hattori T., Nakamura K., Asahi T.;
RT   "Isolation and characterization of two tightly linked catalase genes
RT   from castor bean that are differentially regulated.";
RL   Plant Mol. Biol. 25:507-516(1994).
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.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome (Potential). Glyoxysome
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Abundant in hypocotyls and roots. Low levels
CC       are seen in the endosperms and cotyledons.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; D21162; BAA04698.1; -; Genomic_DNA.
DR   PIR; S46298; S46298.
DR   HSSP; P46206; 1M7S.
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; FALSE_NEG.
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 2.
FT                                /FTId=PRO_0000084957.
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;  57172 MW;  DDB84B8FC652B202 CRC64;
     MDPYKFRPSS SNDTPFWTTN AGDPVSNNNS SMTVGPRGPI LLEDYHMIEK LANFTRERIP
     ERVVHARGMS AKGFFEVTHD VTDLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFATKFYTRE GNFDIVGNNF PVFFIRDGIK FPDVVHAFKP NPKSHIQEYW RIFDFCSHHP
     ESLSTFAWFF DDVGIPQDYR HMEGFGVHTY CLINKAGKVT YVKFHWKPTC GVKCLMDDEA
     IKVGGANHSH ATQDLYDSIA AGNFPEWKLM IQTMDPADED KFSFDPLDMT KIWPEDMFPL
     HPVGRLVLNR NIDNWFAENE MLAFNPAHVV PGVYYSNDKL FQLRLFAYSD TQRHRLGTNY
     LQLPVNAPKC PYHNNHYDGF MNFMHRDEEV DYFQSRYDPV RHAEKVPIPN AICSGRREKC
     VIEKEDNFRQ PGDRYRSWAP DRQERFLCRL VNALSEPRIT HEIRSIWVSW WTQCDKSLGQ
     KLASRLNVRP NI
//