CATA1_ORYSI
ID CATA1_ORYSI Reviewed; 492 AA.
AC P0C549; P29611; Q6Z7B2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Catalase isozyme A;
DE Short=CAT-A;
DE EC=1.11.1.6;
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 [MRNA].
RC STRAIN=cv. Habataki; TISSUE=Immature seed;
RX PubMed=1581574; DOI=10.1007/bf00019211;
RA Mori H., Higo K., Higo H., Minobe Y., Matsui H., Chiba S.;
RT "Nucleotide and derived amino acid sequence of a catalase cDNA isolated
RT from rice immature seeds.";
RL Plant Mol. Biol. 18:973-976(1992).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Glyoxysome
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61626; CAA43814.1; -; mRNA.
DR AlphaFoldDB; P0C549; -.
DR SMR; P0C549; -.
DR PRIDE; P0C549; -.
DR EnsemblPlants; BGIOSGA007252-TA; BGIOSGA007252-PA; BGIOSGA007252.
DR Gramene; BGIOSGA007252-TA; BGIOSGA007252-PA; BGIOSGA007252.
DR HOGENOM; CLU_010645_4_0_1; -.
DR OMA; QERMVWH; -.
DR ExpressionAtlas; P0C549; differential.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IEA:EnsemblPlants.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009617; P:response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblPlants.
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 2: Evidence at transcript level;
KW Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Peroxisome.
FT CHAIN 1..492
FT /note="Catalase isozyme A"
FT /id="PRO_0000293083"
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:0000255|PROSITE-ProRule:PRU10013"
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"
FT CONFLICT 113
FT /note="P -> Q (in Ref. 1; CAA43814)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..454
FT /note="RRFAGEL -> AVRRRV (in Ref. 1; CAA43814)"
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