ID   CATA4_SOYBN             Reviewed;         492 AA.
AC   O48561;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Catalase-4;
DE            EC=1.11.1.6;
GN   Name=CAT4;
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 [MRNA].
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. {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; AF035255; AAB88172.1; -; mRNA.
DR   RefSeq; NP_001237571.1; NM_001250642.1.
DR   AlphaFoldDB; O48561; -.
DR   SMR; O48561; -.
DR   STRING; 3847.GLYMA04G01920.1; -.
DR   PeroxiBase; 6266; GmKat04.
DR   PRIDE; O48561; -.
DR   ProMEX; O48561; -.
DR   EnsemblPlants; KRH60933; KRH60933; GLYMA_04G017500.
DR   GeneID; 547511; -.
DR   Gramene; KRH60933; KRH60933; GLYMA_04G017500.
DR   KEGG; gmx:547511; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   InParanoid; O48561; -.
DR   OrthoDB; 507937at2759; -.
DR   Proteomes; UP000008827; Chromosome 4.
DR   Genevisible; O48561; 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-4"
FT                   /id="PRO_0000084965"
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;  56737 MW;  FEF3B4706A4FD669 CRC64;
     MDPYKHRPSS AFNSPFWTTN SGAPIWNNNS SLTVGARGPI LLEDYHLVEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNL PVFFVRDGMK FPDMVHALKP NPKNHIQENW RILDFFSHFP
     ESLHMFTFLF DDLGVPQDYR HMDGFGVNTY TLINKAGKAV YVKFHWKTTS GIKCLLEEEA
     IKVGGANHSH ATQDLHDSIA AGNYPEWKLF VQTIDPEHED KFDFDPLDVT KTWPEDIIPL
     QPVGRLVLNK NIDNFFAENE QLAFCPAIVV PGVYYSDDKM LQTRIFSYAD SQRHRLGPNY
     LQLPANAPKC AHHNNHHEGF MNFIHRDEEV NYFPSRYDPV RHAERFPIPP AICSGRREKC
     GIEKENNFKQ PGERYRSWAP DRQDRFARRW VDALSDPRVT HEIRSVWISY WSQADRSLGQ
     KIASHLSTRP NI