CATA1_ORYSJ
ID CATA1_ORYSJ Reviewed; 492 AA.
AC Q0E4K1; A3A2F1; P29611; Q6Z7B2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Catalase isozyme A;
DE Short=CAT-A;
DE EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:21979082};
GN Name=CATA; OrderedLocusNames=Os02g0115700, LOC_Os02g02400;
GN ORFNames=OJ1442_E05.8-1, OsJ_004973, P0036E06.27-1;
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 [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=8605302; DOI=10.1007/bf00049328;
RA Higo K., Higo H.;
RT "Cloning and characterization of the rice CatA catalase gene, a homologue
RT of the maize Cat3 gene.";
RL Plant Mol. Biol. 30:505-521(1996).
RN [2]
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 [3]
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 [4]
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 [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., 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 [6]
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 [7]
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 [8]
RP INHIBITION BY WATER STRESS, SUBCELLULAR 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 [9]
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 [10]
RP FUNCTION, INDUCTION BY LIGHT, REPRESSION BY 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 [11]
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 [12]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [13]
RP INDUCTION BY XANTHOMONAS ORYZAE.
RX PubMed=27185545; DOI=10.1038/srep26104;
RA Jiang G., Yin D., Zhao J., Chen H., Guo L., Zhu L., Zhai W.;
RT "The rice thylakoid membrane-bound ascorbate peroxidase OsAPX8 functions in
RT tolerance to bacterial blight.";
RL Sci. Rep. 6:26104-26104(2016).
RN [14]
RP TISSUE SPECIFICITY.
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 INDUCTION BY HEAT STRESS, AND 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). Involved in environmental stress response. Promotes
CC drought stress tolerance and recovery (Ref.10).
CC {ECO:0000250|UniProtKB:Q55DH8, ECO:0000269|Ref.10}.
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 and MgCl(2), and, to a lower extent, of
CC LiCl. {ECO:0000269|PubMed:21979082}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 mM for H(2)O(2) (at pH 7.5) {ECO:0000269|PubMed:21979082};
CC Vmax=0.33 umol/min/g enzyme (at pH 7.5)
CC {ECO:0000269|PubMed:21979082};
CC Note=kcat is 6.6 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 8. {ECO:0000269|PubMed:21979082};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:21979082};
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with STRK1 at the
CC plasma membrane (PubMed:29581216). {ECO:0000250|UniProtKB:Q9C168,
CC ECO:0000269|PubMed:29581216}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26900141,
CC ECO:0000305|PubMed:21398647}. Cell membrane
CC {ECO:0000269|PubMed:29581216}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in young leaves (blades and
CC sheaths) and seeds (Ref.10, PubMed:21979082, PubMed:21398647,
CC PubMed:22106097, PubMed:26900141, PubMed:28969789, PubMed:29464319).
CC Abundant in leaf sheath and moderately expressed in leaf blade and root
CC (PubMed:21398647, PubMed:22106097, PubMed:29464319). Also present at a
CC high levels in panicles, but barely in culms (PubMed:22106097, Ref.10).
CC Observed in stems and anthers (PubMed:29464319).
CC {ECO:0000269|PubMed:21398647, ECO:0000269|PubMed:21979082,
CC ECO:0000269|PubMed:22106097, ECO:0000269|PubMed:26900141,
CC ECO:0000269|PubMed:28969789, ECO:0000269|PubMed:29464319,
CC ECO:0000269|Ref.10}.
CC -!- INDUCTION: Abundance in leaves follows a photoperiod-dependent
CC circadian rhythm with an oscillating expression pattern peaking late in
CC the light period (PubMed:21398647, Ref.10). Inhibited by water stress
CC (PubMed:21398647). Repressed by abscisic acid (ABA), drought, high
CC salinity (NaCl) and hydrogen peroxide (H(2)O(2)) treatments (Ref.10).
CC Triggered by zinc oxide nanoparticles (ZnO NPs); this induction is
CC reversed by sodium nitroprusside (SNP, a NO donor) (PubMed:25958266).
CC Accumulates upon infection by the bacterial blight agent X.oryzae pv.
CC Oryzae (Xoo) strain PXO99 (PubMed:27185545). Influenced by heat stress
CC (HS); up-regulated in conditons 35 degrees Celsius day / 27 degrees
CC Celsius night, but repressed in conditions 38 degrees Celsius day / 30
CC degrees Celsius night (PubMed:29464319). {ECO:0000269|PubMed:21398647,
CC ECO:0000269|PubMed:25958266, ECO:0000269|PubMed:27185545,
CC ECO:0000269|PubMed:29464319, ECO:0000269|Ref.10}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAZ21490.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D29966; BAA06232.1; -; Genomic_DNA.
DR EMBL; AP004121; BAD07711.1; -; Genomic_DNA.
DR EMBL; AP004867; BAD07936.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07587.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76647.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ21490.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK065094; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK099923; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015625395.1; XM_015769909.1.
DR AlphaFoldDB; Q0E4K1; -.
DR SMR; Q0E4K1; -.
DR STRING; 4530.OS02T0115700-01; -.
DR PeroxiBase; 5146; OsKat01.
DR PaxDb; Q0E4K1; -.
DR PRIDE; Q0E4K1; -.
DR EnsemblPlants; Os02t0115700-01; Os02t0115700-01; Os02g0115700.
DR GeneID; 4328073; -.
DR Gramene; Os02t0115700-01; Os02t0115700-01; Os02g0115700.
DR KEGG; osa:4328073; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_4_0_1; -.
DR InParanoid; Q0E4K1; -.
DR OMA; QERMVWH; -.
DR OrthoDB; 507937at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q0E4K1; baseline and differential.
DR Genevisible; Q0E4K1; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
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:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; 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:0009416; P:response to light stimulus; 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; Cytoplasm; Heme; Hydrogen peroxide; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Peroxidase; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..492
FT /note="Catalase isozyme A"
FT /id="PRO_0000084952"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
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: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 CONFLICT 448..454
FT /note="RRFAGEL -> PLRRRV (in Ref. 1; BAA06232)"
FT /evidence="ECO:0000305"
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
