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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
 
 
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