ID   CATA_IPOBA              Reviewed;         492 AA.
AC   P07145;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kokei No. 14;
RX   PubMed=2885193; DOI=10.1111/j.1432-1033.1987.tb11457.x;
RA   Sakajo S., Nakamura K., Asahi T.;
RT   "Molecular cloning and nucleotide sequence of full-length cDNA for sweet
RT   potato catalase mRNA.";
RL   Eur. J. Biochem. 165:437-442(1987).
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; X05549; CAA29063.1; -; mRNA.
DR   PIR; S07124; S07124.
DR   AlphaFoldDB; P07145; -.
DR   SMR; P07145; -.
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   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   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Peroxisome.
FT   CHAIN           1..492
FT                   /note="Catalase"
FT                   /id="PRO_0000084943"
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;  56985 MW;  7B3E59C6A2E3B45C CRC64;
     MDPSKYRPSS SFNTPFCTTN SGAPVWNNTC ALTVGSRGPI LLEDYHLVEK IQNFTRERIP
     ERVVHARGAS AKGFFEVTHD ITHLTCADFL RAPGVQTPLI VRFSTVIHER GSPETIRDPR
     GFAVKMYTRG GNWDLVGNNF PVFFIRDGTQ FPDVIHAFKP NPKSHIQENW RILDYLSHLP
     ESLNTFAWFY DDVGIPTDYR HMEGFGVHTF TMINKEGKAN YVKFHWKPTC GVKCLLEEEA
     IRIGGENHSH ATQDLYESIA AGNYPEWKLY IQVMDPDHED RFDFDPLDTT KIWPEELIPL
     QPVGRMVLNK NIDNFFAENE MLAMDPAHIV PGIYFSDDKM LQARVFAYAD THRHRLGPNY
     MLLPVNAPKC AHHNNSYDGY MNFVHRDEEV DYFPSKFDNT RNAERFPTPL RIVTGQRDKC
     VIEKENNFKQ PGDRYRSWAP DRQDRFINRW VKALSEPRVT HEIRSTWISY LTQADRSLGQ
     KVASRLNIRP TM