CATA3_ORYSJ
ID CATA3_ORYSJ Reviewed; 492 AA.
AC Q10S82; Q7XAD9; Q9ZRI9;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Catalase isozyme C {ECO:0000303|PubMed:21979082};
DE Short=CAT-C {ECO:0000303|PubMed:21979082};
DE Short=OsCatC {ECO:0000303|PubMed:21979082};
DE EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:21979082, ECO:0000269|PubMed:29581216};
DE AltName: Full=Protein NITRIC OXIDE EXCESS 1 {ECO:0000303|PubMed:22106097};
GN Name=CATC {ECO:0000303|Ref.1};
GN Synonyms=CAT1 {ECO:0000303|Ref.2}, NOE1 {ECO:0000303|PubMed:22106097};
GN OrderedLocusNames=LOC_Os03g03910 {ECO:0000312|EMBL:ABF93810.1},
GN Os03g0131200 {ECO:0000312|EMBL:BAF10775.1};
GN ORFNames=OsJ_09293 {ECO:0000312|EMBL:EEE58275.1},
GN OSNPB_030131200 {ECO:0000312|EMBL:BAS82138.1};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Peng R., Yao Q., Xiong A.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP INHIBITION BY WATER STRESS AND ABSCISIC ACID, AND SUBCELLULAR LOCATION.
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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 [12]
RP REVIEW.
RX PubMed=23331502; DOI=10.1111/jipb.12032;
RA Wang Y., Lin A., Loake G.J., Chu C.;
RT "H2O2-induced leaf cell death and the crosstalk of reactive nitric/oxygen
RT species.";
RL J. Integr. Plant Biol. 55:202-208(2013).
RN [13]
RP FUNCTION, INDUCTION BY LIGHT AND ABIOTIC STRESSES, AND TISSUE 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 [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25912474; DOI=10.1111/jpi.12243;
RA Liang C., Zheng G., Li W., Wang Y., Hu B., Wang H., Wu H., Qian Y.,
RA Zhu X.G., Tan D.X., Chen S.Y., Chu C.;
RT "Melatonin delays leaf senescence and enhances salt stress tolerance in
RT rice.";
RL J. Pineal Res. 59:91-101(2015).
RN [16]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND INTERACTION WITH GLO1 AND 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 [17]
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 [18]
RP INHIBITION BY CADMIUM, AND 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 [19]
RP PHOSPHORYLATION AT TYR-210, MUTAGENESIS OF TYR-210 AND TYR-360, INTERACTION
RP WITH STRK1, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
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 [20]
RP TISSUE SPECIFICITY.
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.
CC Responsible for the redox homeostasis in leaves. Prevents nitric oxide
CC (NO) accumulation and subsequent NO-mediated leaf cell death as well as
CC the S-nitrosylation of specific proteins (e.g. glyceraldehyde 3-
CC phosphate dehydrogenase and thioredoxin) by degrading H(2)O(2)
CC (PubMed:22106097, PubMed:23331502). Involved in photorespiration.
CC Promotes drought stress tolerance and recovery (Ref.13). Involved in
CC NO-mediated enhanced tolerance to zinc oxide nanoparticles (ZnO NPs)-
CC induced phytotoxicity (PubMed:25958266). Participates in melatonin-
CC mediated detoxification (PubMed:25912474).
CC {ECO:0000269|PubMed:22106097, ECO:0000269|PubMed:25912474,
CC ECO:0000269|PubMed:25958266, ECO:0000269|Ref.13,
CC ECO:0000303|PubMed:23331502}.
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, ECO:0000269|PubMed:29581216};
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=43 mM for H(2)O(2) (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:26900141};
CC KM=40 mM for H(2)O(2) (at pH 7.5) {ECO:0000269|PubMed:21979082};
CC Vmax=251 mmol/min/mg enzyme (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:26900141};
CC Vmax=0.03 umol/min/g enzyme (at pH 7.5)
CC {ECO:0000269|PubMed:21979082};
CC Note=kcat is 0.5 min(-1) with H(2)O(2) as substrate (at pH 7.5)
CC (PubMed:21979082). kcat is 28 sec(-1) with H(2)O(2) as substrate (at
CC pH 7.4 and 30 degrees Celsius) (PubMed:26900141).
CC {ECO:0000269|PubMed:21979082, ECO:0000269|PubMed:26900141};
CC pH dependence:
CC Optimum pH is 7. {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 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: Highly expressed in mature leaves (PubMed:21979082,
CC PubMed:21398647, PubMed:22106097, PubMed:23331502, PubMed:26900141,
CC PubMed:28969789, PubMed:29464319). Mainly expressed in leaf blades,
CC stems, panicles, leaf sheaths, and culms, but barely in roots
CC (PubMed:22106097, PubMed:23331502, PubMed:29464319).
CC {ECO:0000269|PubMed:21398647, ECO:0000269|PubMed:21979082,
CC ECO:0000269|PubMed:22106097, ECO:0000269|PubMed:23331502,
CC ECO:0000269|PubMed:26900141, ECO:0000269|PubMed:28969789,
CC ECO:0000269|PubMed:29464319}.
CC -!- INDUCTION: Abundance in leaves follows a light-dependent rhythm with an
CC oscillating expression pattern peaking early in the light period
CC (PubMed:21398647, PubMed:23331502). Inhibited by water stress and
CC abscisic acid (ABA) in a concentration-dependent manner
CC (PubMed:21398647, PubMed:23331502). Enhanced by ABA biosynthesis
CC inhibitors nordihydroguaiaretic acid and tungstate under water stress
CC (PubMed:21398647). Slightly affected by high salinity and hydrogen
CC peroxide (H(2)O(2)) treatments (PubMed:23331502). Accumulates upon
CC infection by the bacterial blight agent X.oryzae pv. Oryzae (Xoo)
CC strain PXO99 (PubMed:27185545). Repressed by cadmium (Cd)
CC (PubMed:28969789). {ECO:0000269|PubMed:21398647,
CC ECO:0000269|PubMed:23331502, ECO:0000269|PubMed:27185545,
CC ECO:0000269|PubMed:28969789}.
CC -!- PTM: Activated by STRK1-mediated phosphorylation at Tyr-210 upon salt
CC and oxidative stress. {ECO:0000269|PubMed:29581216}.
CC -!- DISRUPTION PHENOTYPE: Impaired catalase activity in leaves.
CC Accumulation of hydrogen peroxide (H(2)O(2)) in leaves, which
CC consequently promotes nitric oxide (NO) production via the activation
CC of nitrate reductase, thus leading to subsequent NO-mediated leaf cell
CC death, as well as increased S-nitrosylation of specific proteins
CC including glyceraldehyde 3-phosphate dehydrogenase and thioredoxin
CC (PubMed:22106097, PubMed:23331502). Leaf bleaching and cell death;
CC these phenotypes are reversed by melatonin treatment (PubMed:25912474).
CC Increased tolerance to zinc oxide nanoparticles (ZnO NPs)
CC (PubMed:25958266). {ECO:0000269|PubMed:22106097,
CC ECO:0000269|PubMed:25912474, ECO:0000269|PubMed:25958266,
CC ECO:0000303|PubMed:23331502}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; D86611; BAA34205.1; -; Genomic_DNA.
DR EMBL; AY339372; AAQ19030.1; -; mRNA.
DR EMBL; DP000009; ABF93810.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF10775.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82138.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE58275.1; -; Genomic_DNA.
DR EMBL; AK062174; BAG88238.1; -; mRNA.
DR EMBL; AK066378; BAG89941.1; -; mRNA.
DR RefSeq; XP_015629749.1; XM_015774263.1.
DR AlphaFoldDB; Q10S82; -.
DR SMR; Q10S82; -.
DR STRING; 4530.OS03T0131200-01; -.
DR PeroxiBase; 5144; OsKat03.
DR iPTMnet; Q10S82; -.
DR PaxDb; Q10S82; -.
DR PRIDE; Q10S82; -.
DR EnsemblPlants; Os03t0131200-01; Os03t0131200-01; Os03g0131200.
DR EnsemblPlants; Os03t0131200-02; Os03t0131200-02; Os03g0131200.
DR GeneID; 4331509; -.
DR Gramene; Os03t0131200-01; Os03t0131200-01; Os03g0131200.
DR Gramene; Os03t0131200-02; Os03t0131200-02; Os03g0131200.
DR KEGG; osa:4331509; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_4_0_1; -.
DR InParanoid; Q10S82; -.
DR OMA; WTCYVQV; -.
DR OrthoDB; 507937at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
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:0045454; P:cell redox homeostasis; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0033484; P:nitric oxide homeostasis; IMP:UniProtKB.
DR GO; GO:0017014; P:protein nitrosylation; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; 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; 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 C"
FT /id="PRO_0000445626"
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; by STRK1"
FT /evidence="ECO:0000269|PubMed:29581216"
FT CROSSLNK 325..348
FT /note="3-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
FT MUTAGEN 210
FT /note="Y->D: Phosphorylation mimic exhibits higher catalase
FT activity. Impaired STRK1-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:29581216"
FT MUTAGEN 210
FT /note="Y->F: Non-phosphorylation mimic exhibits loss of
FT catalase activity. Impaired STRK1-mediated
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:29581216"
FT MUTAGEN 360
FT /note="Y->D,F: Normal STRK1-mediated phosphorylation and
FT subsequent catalase activity enhancement."
FT /evidence="ECO:0000269|PubMed:29581216"
FT CONFLICT 121
FT /note="G -> V (in Ref. 1; BAA34205 and 2; AAQ19030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56764 MW; 4443434F3485C8AA CRC64;
MDPYKHRPSS SFNGPLWSTN SGAPVWNNNN SLTVGSRGPI LLEDYHLVEK LANFDRERIP
ERVVHARGAS AKGFFEVTHD ITHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
GFAIKFYTRE GNWDLVGNNF PVFFIRDGMK FPDMVHSLKP NPKSHVQENW RILDFFSHHP
ESLHMFTFLF DDIGIPADYR HMDGSGVNTY TLVNRAGKSH YVKFHWKPTC GVKSLLDDEA
VTVGGTNHSH ATQDLYDSIA AGNFPEWKLF IQTIDPDHED RFDFDPLDVT KTWPEDIVPL
QPVGRMVLNR NIDNFFSENE QLAFCPGIIV PGIYYSDDKL LQTRIFSYSD TQRHRLGPNY
LLLPPNAPKC AHHNNHYDGF MNFMHRDEEV DYFPSRYDPA KHAPRYPIPS ATLTGRREKV
VIAKENNFKQ PGERYRSWDP ARQDRFIKRW IDALSDPRLT HEIRSIWLSY WSQADRSLGQ
KLASRLSAKP SM
