ID CATA_PEA Reviewed; 494 AA.
AC P25890;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
OS Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=1932700; DOI=10.1007/bf00028744;
RA Isin S.H., Allen R.D.;
RT "Isolation and characterization of a pea catalase cDNA.";
RL Plant Mol. Biol. 17:1263-1265(1991).
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.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; X60169; CAA42736.1; -; mRNA.
DR PIR; S18346; CSPM.
DR AlphaFoldDB; P25890; -.
DR SMR; P25890; -.
DR PeroxiBase; 398; PsKat01.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
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; CATALASE; 1.
DR PANTHER; PTHR11465:SF23; CATALASE-2; 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; Heme-dependent catalase-like; 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 Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Peroxisome.
FT CHAIN 1..494
FT /note="Catalase"
FT /id="PRO_0000084954"
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"
SQ SEQUENCE 494 AA; 57345 MW; B5FC08E66B13B266 CRC64;
MDPYKHRPSS AFNSPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLVEK LAQFDRERIP
ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
GFAVKFYTRE GNYDLVGNNF PVFFVHDGMN FPDMVHALKP NPQTHIQENW RILDFFYNFP
ESLHMFSFLF DDVGVPQDYR HMDGFGVNTY TLINKAGKSV YVKFHWKPTC GVKCLLEEEA
IQVGGSNHSH ATKDLYDSIA AGNYPEWKLY IQTIDPAHED RFEFDPLDVT KTWPEDIIPL
QPVGRMVLNK NIDNFFAENE QLAFCPAIML PGIYYSDDKM LQTRVFSYAD SQRHRLGPNY
LQLPVNAPKW SHHNNHHEGF MNAIHRDEEV NYFPSRHDTV RHAERVPIPT THLSARREKC
NIPKQNHFKQ AGERYRTWAP DRQERFLRRW VEALSDTDPR ITHEIRSIWV SYWSQADRSL
GQKLASHLNM RPSI
//
