ID   CATA1_SOYBN             Reviewed;         492 AA.
AC   P29756;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Catalase-1/2;
DE            EC=1.11.1.6;
GN   Name=CAT1;
GN   and
GN   Name=CAT2;
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Corsoy 79;
RA   Su H., Hardy K.A., Hermsmeier D., Baum T.J.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; Z12021; CAA78056.1; -; Genomic_DNA.
DR   EMBL; AF035252; AAB88169.1; -; mRNA.
DR   EMBL; AF035253; AAB88170.1; -; mRNA.
DR   PIR; S20999; CSSY.
DR   RefSeq; NP_001237556.1; NM_001250627.1.
DR   AlphaFoldDB; P29756; -.
DR   SMR; P29756; -.
DR   STRING; 3847.GLYMA17G38140.1; -.
DR   PeroxiBase; 6260; GmKat01.
DR   PRIDE; P29756; -.
DR   EnsemblPlants; KRH06008; KRH06008; GLYMA_17G261700.
DR   GeneID; 547510; -.
DR   Gramene; KRH06008; KRH06008; GLYMA_17G261700.
DR   KEGG; gmx:547510; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_4_0_1; -.
DR   InParanoid; P29756; -.
DR   OMA; PIRDGAK; -.
DR   OrthoDB; 507937at2759; -.
DR   Proteomes; UP000008827; Chromosome 17.
DR   Genevisible; P29756; GM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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-1/2"
FT                   /id="PRO_0000084963"
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;  56847 MW;  CE8AFE8BEEA483C6 CRC64;
     MDPYKNRPSS AFNSPFWTTN SGAPIWNNNS SLTVGSRGPI LLEDYHLVEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPLI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFVRDGLK FPDMVHALKP NPKSHIQENW RILDFFSHHP
     ESLHMFSFLF DDVGIPQDYR HMDGFGVNTY TLINKAGKAL YVKFHWKTTS GEKSLLDDEA
     IRVGGSNHSH ATQDLYDSIA AGNYPEWKLY IQTLDPENED RLDFDPLDVT KTWPEDVLPL
     QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGVYYSDDKL LQTRVFSYAD TQRHRLGPNY
     LQLPANAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRYDPV RHAEKVPVPP RILGGKREKC
     MIEKENNFKQ PGERYRSWPS DRQERFVRRW VDALSDPRVT HEIRSIWISY WSQADRSLGQ
     KIASHLNLKP SI