ID   CATA2_ORYSI             Reviewed;         492 AA.
AC   A2YH64; P55309; Q4PJT9; Q5Z7P3; Q9SB22;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Catalase isozyme B;
DE            Short=CAT-B;
DE            EC=1.11.1.6;
GN   Name=CATB; ORFNames=OsI_023657;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ratna;
RA   Mandal S., Mondal P., Dash A.K., Kar M., Sabat S.C.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., 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).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Glyoxysome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; DQ078758; AAY59707.1; -; mRNA.
DR   EMBL; CM000131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A2YH64; -.
DR   SMR; A2YH64; -.
DR   STRING; 39946.A2YH64; -.
DR   PeroxiBase; 5145; OsKat02.
DR   EnsemblPlants; BGIOSGA023636-TA; BGIOSGA023636-PA; BGIOSGA023636.
DR   Gramene; BGIOSGA023636-TA; BGIOSGA023636-PA; BGIOSGA023636.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   OMA; HVWPQKQ; -.
DR   Proteomes; UP000007015; Chromosome 6.
DR   ExpressionAtlas; A2YH64; differential.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007623; P:circadian rhythm; IEA:EnsemblPlants.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:1900034; P:regulation of cellular response to heat; IEA:EnsemblPlants.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR   GO; GO:0009646; P:response to absence of light; IEA:EnsemblPlants.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblPlants.
DR   GO; GO:0009751; P:response to salicylic acid; IEA:EnsemblPlants.
DR   GO; GO:1902074; P:response to salt; IEA:EnsemblPlants.
DR   GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 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; Oxidoreductase;
KW   Peroxidase; Peroxisome; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme B"
FT                   /id="PRO_0000293084"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         348
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        113
FT                   /note="P -> S (in Ref. 1; AAY59707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="G -> R (in Ref. 1; AAY59707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   492 AA;  56587 MW;  9D012F374B1A8E3C 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
     VIDKENNFKQ AGERYRSFDP ARQDRFLQRW VDALSDPRIT HELRGIWISY WSQCDASLGQ
     KLASRLNLKP NM