CATA2_ORYSJ
ID CATA2_ORYSJ Reviewed; 492 AA.
AC Q0D9C4; B7EGE0; P55309; Q4PJT9; Q5Z7P3; Q9SB22;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Catalase isozyme B;
DE Short=CAT-B;
DE EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:21979082};
GN Name=CATB; OrderedLocusNames=Os06g0727200, LOC_Os06g51150;
GN ORFNames=OsJ_021830, P0017G10.17;
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare;
RX 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 and
RT 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=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
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., 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).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX 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).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=21979082; DOI=10.1271/bbb.110214;
RA Wutipraditkul N., Boonkomrat S., Buaboocha T.;
RT "Cloning and characterization of catalases from rice, Oryza sativa L.";
RL Biosci. Biotechnol. Biochem. 75:1900-1906(2011).
RN [9]
RP FUNCTION, INDUCTION BY WATER STRESS AND ABSCISIC ACID, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Yangdao 6;
RX PubMed=21398647; DOI=10.1093/pcp/pcr028;
RA Ye N., Zhu G., Liu Y., Li Y., Zhang J.;
RT "ABA controls H(2)O(2) accumulation through the induction of OsCATB in rice
RT leaves under water stress.";
RL Plant Cell Physiol. 52:689-698(2011).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=22106097; DOI=10.1104/pp.111.184531;
RA Lin A., Wang Y., Tang J., Xue P., Li C., Liu L., Hu B., Yang F.,
RA Loake G.J., Chu C.;
RT "Nitric oxide and protein S-nitrosylation are integral to hydrogen
RT peroxide-induced leaf cell death in rice.";
RL Plant Physiol. 158:451-464(2012).
RN [11]
RP FUNCTION, INDUCTION BY DARKNESS AND ABIOTIC STRESSES, AND TISSUE
RP SPECIFICITY.
RX DOI=10.1007/s12374-014-0383-8;
RA Joo J., Lee Y.H., Song S.I.;
RT "Rice CatA, CatB, and CatC are involved in environmental stress response,
RT root growth, and photorespiration, respectively.";
RL J. Plant Biol. 57:375-382(2014).
RN [12]
RP INDUCTION BY ZINC OXIDE NANOPARTICLES.
RC STRAIN=cv. Jiafuzhan;
RX PubMed=25958266; DOI=10.1016/j.jhazmat.2015.04.077;
RA Chen J., Liu X., Wang C., Yin S.-S., Li X.-L., Hu W.-J., Simon M.,
RA Shen Z.-J., Xiao Q., Chu C.-C., Peng X.-X., Zheng H.-L.;
RT "Nitric oxide ameliorates zinc oxide nanoparticles-induced phytotoxicity in
RT rice seedlings.";
RL J. Hazard. Mater. 297:173-182(2015).
RN [13]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH GLO1 AND
RP GLO4.
RC STRAIN=cv. Zhonghua 11;
RX PubMed=26900141; DOI=10.1016/j.molp.2016.02.002;
RA Zhang Z., Xu Y., Xie Z., Li X., He Z.-H., Peng X.-X.;
RT "Association-dissociation of glycolate oxidase with catalase in rice: a
RT potential switch to modulate intracellular H2O2 levels.";
RL Mol. Plant 9:737-748(2016).
RN [14]
RP INHIBITION BY CADMIUM.
RX PubMed=28969789; DOI=10.1016/j.plantsci.2017.08.002;
RA Hu S., Yu Y., Chen Q., Mu G., Shen Z., Zheng L.;
RT "OsMYB45 plays an important role in rice resistance to cadmium stress.";
RL Plant Sci. 264:1-8(2017).
RN [15]
RP INTERACTION WITH STRK1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Kitaake;
RX PubMed=29581216; DOI=10.1105/tpc.17.01000;
RA Zhou Y.-B., Liu C., Tang D.-Y., Yan L., Wang D., Yang Y.-Z., Gui J.-S.,
RA Zhao X.-Y., Li L.-G., Tang X.-D., Yu F., Li J.-L., Liu L.-L., Zhu Y.-H.,
RA Lin J.-Z., Liu X.-M.;
RT "The receptor-like cytoplasmic kinase STRK1 phosphorylates and activates
RT CatC, thereby regulating H2O2 homeostasis and improving salt tolerance in
RT rice.";
RL Plant Cell 30:1100-1118(2018).
RN [16]
RP FUNCTION, REPRESSION BY HEAT STRESS, INDUCTION BY SALICYLIC ACID, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Qianjiang3, and cv. Xieqingzao;
RX PubMed=29464319; DOI=10.1007/s00299-018-2264-y;
RA Zhao Q., Zhou L., Liu J., Cao Z., Du X., Huang F., Pan G., Cheng F.;
RT "Involvement of CAT in the detoxification of HT-induced ROS burst in rice
RT anther and its relation to pollen fertility.";
RL Plant Cell Rep. 37:741-757(2018).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide (By
CC similarity). May prevent the excessive accumulation of H(2)O(2) during
CC water stress in response to the accumulation of abscisic acid (ABA)
CC (PubMed:21398647). Involved in the modulation of ROS levels related to
CC root growth regulation (Ref.11). Required for pollen viability and
CC floret fertility upon heat stress (HS) by detoxifying reactive oxygen
CC species (ROS) and malondialdehyde (MDA) accumulation in developing
CC anthers exposed to HS (PubMed:29464319). {ECO:0000250|UniProtKB:Q55DH8,
CC ECO:0000269|PubMed:21398647, ECO:0000269|PubMed:29464319,
CC ECO:0000269|Ref.11}.
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 ECO:0000269|PubMed:21979082};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q9C168};
CC -!- ACTIVITY REGULATION: Strongly inhibited by beta-mercaptoethanol, sodium
CC azide and potassium cyanide. Slightly repressed by 3-amino-1,2,4-
CC triazole (3-AT). Activity is repressed proportionally to increased
CC concentration of NaCl, KCl, LiCl and MgCl(2).
CC {ECO:0000269|PubMed:21979082}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=66.7 mM for H(2)O(2) (at pH 7.5) {ECO:0000269|PubMed:21979082};
CC Vmax=1 umol/min/g enzyme (at pH 7.5) {ECO:0000269|PubMed:21979082};
CC Note=kcat is 20 min(-1) with H(2)O(2) as substrate (at pH 7.5).
CC {ECO:0000269|PubMed:21979082};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:21979082};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:21979082};
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with GLO1 and GLO4;
CC these interactions are disturbed by alpha-hydroxy-2-
CC pyridinemethanesulfonic acid (HPMS) and salicylic acid (SA)
CC (PubMed:26900141). Interacts with STRK1 at the plasma membrane
CC (PubMed:29581216). {ECO:0000250|UniProtKB:Q9C168,
CC ECO:0000269|PubMed:26900141, ECO:0000269|PubMed:29581216}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:26900141,
CC ECO:0000305|PubMed:21398647}. Glyoxysome {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:29581216}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots and, at low
CC levels, in leaves (e.g. sheaths) (PubMed:21398647, Ref.11,
CC PubMed:26900141, PubMed:29464319). Detected in seeds (PubMed:21979082,
CC PubMed:21398647, Ref.11, PubMed:29464319). Also present in panicles and
CC culms (PubMed:22106097, Ref.11). Observed in stems and anthers
CC (PubMed:29464319). {ECO:0000269|PubMed:21398647,
CC ECO:0000269|PubMed:21979082, ECO:0000269|PubMed:22106097,
CC ECO:0000269|PubMed:26900141, ECO:0000269|PubMed:29464319,
CC ECO:0000269|Ref.11}.
CC -!- INDUCTION: Abundance in roots follows a diurnal oscillating expression
CC pattern peaking during the night period (Ref.11). Induced by water
CC stress and abscisic acid (ABA) in a concentration-dependent manner
CC (PubMed:21398647, Ref.11). Activated by salicylic acid (SA)
CC (PubMed:29464319). Repressed by ABA biosynthesis inhibitors
CC nordihydroguaiaretic acid and tungstate under water stress
CC (PubMed:21398647). Induced by high salinity (NaCl) and hydrogen
CC peroxide (H(2)O(2)) treatments (Ref.11). Triggered by zinc oxide
CC nanoparticles (ZnO NPs); this induction is reversed by sodium
CC nitroprusside (SNP, a NO donor) (PubMed:25958266). Repressed by cadmium
CC (Cd) (PubMed:28969789). Inhibited by heat stress (HS) (e.g. 35 degrees
CC Celsius day/27 degrees Celsius night, 38 degrees Celsius day/30 degrees
CC Celsius night) (PubMed:29464319). {ECO:0000269|PubMed:21398647,
CC ECO:0000269|PubMed:25958266, ECO:0000269|PubMed:28969789,
CC ECO:0000269|PubMed:29464319, ECO:0000269|Ref.11}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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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; AP014962; BAS99609.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ38347.1; -; Genomic_DNA.
DR EMBL; AK069446; BAG91437.1; -; mRNA.
DR EMBL; AK100019; BAG94401.1; -; mRNA.
DR RefSeq; XP_015643077.1; XM_015787591.1.
DR AlphaFoldDB; Q0D9C4; -.
DR SMR; Q0D9C4; -.
DR STRING; 4530.OS06T0727200-02; -.
DR PeroxiBase; 5145; OsKat02.
DR PaxDb; Q0D9C4; -.
DR PRIDE; Q0D9C4; -.
DR EnsemblPlants; Os06t0727200-01; Os06t0727200-01; Os06g0727200.
DR EnsemblPlants; Os06t0727200-02; Os06t0727200-02; Os06g0727200.
DR GeneID; 4342124; -.
DR Gramene; Os06t0727200-01; Os06t0727200-01; Os06g0727200.
DR Gramene; Os06t0727200-02; Os06t0727200-02; Os06g0727200.
DR KEGG; osa:4342124; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; Q0D9C4; -.
DR OMA; HVWPQKQ; -.
DR OrthoDB; 507937at2759; -.
DR BRENDA; 1.11.1.6; 4460.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q0D9C4; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004096; F:catalase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:1900034; P:regulation of cellular response to heat; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
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 1: Evidence at protein level;
KW Cell membrane; Glyoxysome; Heme; Hydrogen peroxide; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein;
KW Reference proteome; Stress response; Thioether bond.
FT CHAIN 1..492
FT /note="Catalase isozyme B"
FT /id="PRO_0000084953"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 484..492
FT /note="Peroxisome targeting signal"
FT /evidence="ECO:0000305|PubMed:21398647"
FT ACT_SITE 65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 138
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
FT BINDING 62
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
FT BINDING 102
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
FT BINDING 151
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
FT BINDING 344
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
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|UniProtKB:Q9C168"
FT BINDING 355
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
FT MOD_RES 210
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q10S82"
FT CROSSLNK 325..348
FT /note="3-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
FT CONFLICT 8
FT /note="P -> A (in Ref. 1; BAA05494)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="D -> E (in Ref. 2; BAA34204)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="V -> G (in Ref. 1; BAA05494)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="Y -> H (in Ref. 2; BAA34204)"
FT /evidence="ECO:0000305"
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
