ID   CATA_CAPAN              Reviewed;         492 AA.
AC   Q9M5L6;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
DE   AltName: Full=CaCat1;
GN   Name=CAT;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11297793; DOI=10.1016/s0168-9452(01)00332-6;
RA   Kwon S.-I., An C.-S.;
RT   "Molecular cloning, characterization and expression analysis of a catalase
RT   cDNA from hot pepper (Capsicum annuum L.).";
RL   Plant Sci. 160:961-969(2001).
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}.
CC   -!- TISSUE SPECIFICITY: In stems, leaves, roots and developing fruits.
CC   -!- INDUCTION: In roots, by aluminum and salt. Expressed with a circadian
CC       rhythm reaching a maximum at late in the dark period or early in the
CC       light period.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AF227952; AAF34718.1; -; mRNA.
DR   PIR; JE0126; JE0126.
DR   AlphaFoldDB; Q9M5L6; -.
DR   SMR; Q9M5L6; -.
DR   Proteomes; UP000189700; Genome assembly.
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_0000084934"
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;  56480 MW;  5D987B637FCDD4E7 CRC64;
     MDLSKYRPSS AYDSPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYHLIEK LATFVRERIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI CRFSTVVHER GSPESIRDIR
     GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQENW RILDFFSFLP
     ESLHTFAFFY DDVCLPTDYR HMEGFGVHAY QLINKAGKAH YVKFHWKPTC GVKSMTEEEA
     IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQIMNPEDVD KFDFDPLDVT KTWPEDILPL
     MPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGVYYSEDKL LQTRIFAYAD TQRHRIGPNY
     MQLPVNAPKC AHHNNHRDGA MNFMHRDEEV DYLPSRFDPC RPAEQYPIPS CVLTGRREKC
     VIPKENNFKQ AGERYRSWAP DRQDRYINKW VESLSDPRAT HEIRSIWISY LSQADKSCGQ
     KVASRLTVKP TM