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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}.
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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
 
 
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