ID   CATA2_ORYSJ             Reviewed;         492 AA.
AC   Q0D9C4; P55309; Q4PJT9; Q5Z7P3; Q9SB22;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Catalase isozyme B;
DE            Short=CAT-B;
DE            EC=1.11.1.6;
GN   Name=CATB; OrderedLocusNames=Os06g0727200, LOC_Os06g51150;
GN   ORFNames=P0017G10.17, OsJ_021830;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=94336766; PubMed=8058828; DOI=10.1104/pp.105.3.1015;
RA   Morita S., Tasaka M., Fujisawa H., Ushimaru T., Tsuji H.;
RT   "A cDNA clone encoding a rice catalase isozyme.";
RL   Plant Physiol. 105:1015-1016(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Seedling leaf;
RX   AGRICOLA=IND21967300; DOI=10.1007/s001220050861;
RA   Iwamoto M., Maekawa M., Saito A., Higo H., Higo K.;
RT   "Evolutionary relationship of plant catalase genes inferred from exon-
RT   intron structures: isozyme divergence after the separation of monocots
RT   and dicots.";
RL   Theor. Appl. Genet. 97:9-19(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=17210932; DOI=10.1101/gr.5509507;
RG   The rice annotation project (RAP);
RT   "Curated genome annotation of Oryza sativa ssp. japonica and
RT   comparative genome analysis with Arabidopsis thaliana.";
RL   Genome Res. 17:175-183(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=22752273; PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D26484; BAA05494.1; -; mRNA.
DR   EMBL; D64013; BAA34204.1; -; Genomic_DNA.
DR   EMBL; AP004685; BAD61813.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF20549.1; -; Genomic_DNA.
DR   EMBL; CM000143; EAZ38347.1; -; Genomic_DNA.
DR   EMBL; AK069446; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001058635.1; -.
DR   UniGene; Os.39055; -.
DR   HSSP; P46206; 1M7S.
DR   PeroxiBase; 5145; OsKat02.
DR   GeneID; 4342124; -.
DR   KEGG; osa:4342124; -.
DR   Gramene; P55309; -.
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 B.
FT                                /FTId=PRO_0000084953.
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      8      8       P -> A (in Ref. 1; BAA05494).
FT   CONFLICT    118    118       D -> E (in Ref. 2; BAA34204).
FT   CONFLICT    142    142       V -> G (in Ref. 1; BAA05494).
FT   CONFLICT    199    199       Y -> H (in Ref. 2; BAA34204).
SQ   SEQUENCE   492 AA;  56587 MW;  88E13AC2AB1A8E26 CRC64;
     MDPYKHRPSS GSNSTFWTTN SGAPVWNNNS ALTVGERGPI LLEDYHLIEK LAQFDRERIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVVHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNM PVFFIRDGMK FPDMVHAFKP SPKTNMQENW RIVDFFSHHP
     ESLHMFSFLF DDVGIPLNYR HMEGFGVNTY TLINKDGKPH LVKFHWKPTC GVKCLLDDEA
     VTVGGTCHSH ATKDLTDSIA AGNYPEWKLY IQTIDPDHED RFDFDPLDVT KTWPEDIIPL
     QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGIHYSDDKL LQTRIFSYAD TQRHRLGPNY
     LMLPVNAPKC AYHNNHHDGS MNFMHRDEEV NYFPSRFDAA RHAEKVPIPP RVLTGCREKC
     VIDKENNFQQ AGERYRSFDP ARQDRFLQRW VDALSDPRIT HELRGIWISY WSQCDASLGQ
     KLASRLNLKP NM
//