ID   CATA_VIGRR              Reviewed;         492 AA.
AC   P32290;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8108520; DOI=10.1104/pp.102.2.691;
RA   Mori H., Imaseki H.;
RT   "cDNA for catalase from etiolated mung bean (Vigna radiata) hypocotyls.";
RL   Plant Physiol. 102:691-692(1993).
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 {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; D13557; BAA02755.1; -; mRNA.
DR   PIR; T10902; T10902.
DR   RefSeq; NP_001304079.1; NM_001317150.1.
DR   AlphaFoldDB; P32290; -.
DR   SMR; P32290; -.
DR   STRING; 3916.P32290; -.
DR   PeroxiBase; 6264; PauKat01.
DR   PRIDE; P32290; -.
DR   GeneID; 106762083; -.
DR   KEGG; vra:106762083; -.
DR   Proteomes; UP000087766; Chromosome 5.
DR   GO; GO:0009514; C:glyoxysome; 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   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; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase"
FT                   /id="PRO_0000084955"
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   492 AA;  56844 MW;  933E604D2611CE85 CRC64;
     MDPYKYRPSS AFNSPFWTTN SGAPVWNNNN SLTVGTRGPI LLEDYHLVEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNL PVFFVRDGMK FPDMVHALKP NPKNHIQENW RILDFFSHFP
     ESLHMFSFLF DDLGVPQDYR HMDGFGVNTY TLINKAGKAV YVKFHWKTTS GVKCLLEEEA
     IKVGGANHSH ATQDLHDSIA AGNYPEWKLF IQTIDPEHED KFDFDPLDVT KTWPEDIIPL
     QPVGRLVLNK NIDNFFAENE QLAFCPAIIV PGVYYSDDKM LQTRIFSYAD SQRHRLGPNY
     LLLPANAPKS AHHNNHHEGF MNFIHRDEEV NYFPSRYDPV RHAEKFPIPP AVFSGRREKI
     AIEKENNFKQ AGERFRSWAP DRQDRFIRRW VDALSDPRVT HEIRSVWISY WSQADRSLGQ
     KIASHLNMRP NI