CATA3_ORYSI
ID CATA3_ORYSI Reviewed; 492 AA.
AC B8AME2;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Catalase isozyme C {ECO:0000255|PROSITE-ProRule:PRU10013};
DE EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013};
GN ORFNames=OsI_09857 {ECO:0000312|EMBL:EEC74449.1};
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 [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 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 Involved in photorespiration. Promotes drought stress tolerance and
CC recovery. Involved in NO-mediated enhanced tolerance to zinc oxide
CC nanoparticles (ZnO NPs)-induced phytotoxicity. Participates in
CC melatonin-mediated detoxification. {ECO:0000250|UniProtKB:Q10S82}.
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 Evidence={ECO:0000250|UniProtKB:Q9C168};
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). Interacts
CC with STRK1 at the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q10S82, ECO:0000250|UniProtKB:Q9C168}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q10S82}.
CC Glyoxysome {ECO:0000250|UniProtKB:Q10S82}. Cell membrane
CC {ECO:0000250|UniProtKB:Q10S82}.
CC -!- PTM: Activated by STRK1-mediated phosphorylation at Tyr-210 upon salt
CC and oxidative stress. {ECO:0000250|UniProtKB:Q10S82}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; CM000128; EEC74449.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AME2; -.
DR SMR; B8AME2; -.
DR STRING; 39946.B8AME2; -.
DR PRIDE; B8AME2; -.
DR EnsemblPlants; BGIOSGA011520-TA; BGIOSGA011520-PA; BGIOSGA011520.
DR Gramene; BGIOSGA011520-TA; BGIOSGA011520-PA; BGIOSGA011520.
DR HOGENOM; CLU_010645_4_0_1; -.
DR OMA; WTCYVQV; -.
DR Proteomes; UP000007015; Chromosome 3.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004096; F:catalase activity; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEA:EnsemblPlants.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0033484; P:nitric oxide homeostasis; ISS:UniProtKB.
DR GO; GO:0017014; P:protein nitrosylation; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009617; P:response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; 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 3: Inferred from homology;
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_0000445625"
FT MOTIF 484..492
FT /note="Peroxisome targeting signal"
FT /evidence="ECO:0000305"
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:0000250|UniProtKB:Q10S82"
FT CROSSLNK 325..348
FT /note="3-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:Q9C168"
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
