ID   CATA1_ORYSI             Reviewed;         492 AA.
AC   P0C549; P29611; Q6Z7B2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=Catalase isozyme A;
DE            Short=CAT-A;
DE            EC=1.11.1.6;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Habataki; TISSUE=Immature seed;
RX   MEDLINE=92256818; PubMed=1581574; DOI=10.1007/BF00019211;
RA   Mori H., Higo K., Higo H., Minobe Y., Matsui H., Chiba S.;
RT   "Nucleotide and derived amino acid sequence of a catalase cDNA
RT   isolated from rice immature seeds.";
RL   Plant Mol. Biol. 18:973-976(1992).
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 (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; X61626; CAA43814.1; -; mRNA.
DR   HSSP; P46206; 1M7S.
DR   Gramene; P29611; -.
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    492       Catalase isozyme A.
FT                                /FTId=PRO_0000293083.
FT   ACT_SITE     65     65       By similarity.
FT   ACT_SITE    138    138       By similarity.
FT   METAL       348    348       Iron (heme axial ligand) (By similarity).
FT   CONFLICT    113    113       P -> Q (in Ref. 1; CAA43814).
FT   CONFLICT    448    454       RRFAGEL -> AVRRRV (in Ref. 1; CAA43814).
SQ   SEQUENCE   492 AA;  56698 MW;  CB72C63598262AEF CRC64;
     MDPCKFRPSS SFDTKTTTTN AGAPVWNDNE ALTVGPRGPI LLEDYHLIEK VAHFARERIP
     ERVVHARGAS AKGFFECTHD VTDITCADFL RSPGAQTPVI VRFSTVIHER GSPETIRDPR
     GFAVKFYTRE GNWDLLGNNF PVFFIRDGIK FPDVIHAFKP NPRSHVQEYW RVFDFLSHHP
     ESLHTFFFLF DDVGIPTDYR HMDGFGVNTY TFVTRDAKAR YVKFHWKPTC GVSCLMDDEA
     TLVGGKNHSH ATQDLYDSIA AGNFPEWKLF VQVIDPEEEE RFDFDPLDDT KTWPEDEVPL
     RPVGRLVLNR NVDNFFNENE QLAFGPGLVV PGIYYSDDKM LQCRVFAYAD TQRYRLGPNY
     LMLPVNAPKC AHHNNHYDGA MNFMHRDEEV DYYPSRHAPL RHAPPTPITP RPVVGRRQKA
     TIHKQNDFKQ PGERYRSWAP DRQERFIRRF AGELAHPKVS PELRAIWVNY LSQCDESLGV
     KIANRLNVKP SM
//