ID   CATA2_SOLTU             Reviewed;         492 AA.
AC   P55312;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 115.
DE   RecName: Full=Catalase isozyme 2;
DE            EC=1.11.1.6;
GN   Name=CAT2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-492.
RC   STRAIN=cv. Datura; TISSUE=Leaf;
RX   PubMed=7655060; DOI=10.1094/mpmi-8-0371;
RA   Niebel A., Heungens K., Barthels N., Inze D., van Montagu M., Gheysen G.;
RT   "Characterization of a pathogen-induced potato catalase and its systemic
RT   expression upon nematode and bacterial infection.";
RL   Mol. Plant Microbe Interact. 8:371-378(1995).
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 = O2 + 2 H2O; 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; Z37106; CAA85470.1; -; Genomic_DNA.
DR   AlphaFoldDB; P55312; -.
DR   SMR; P55312; -.
DR   IntAct; P55312; 1.
DR   STRING; 4113.P55312; -.
DR   PaxDb; 4113-P55312; -.
DR   ProMEX; P55312; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   InParanoid; P55312; -.
DR   OrthoDB; 6880011at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08154; catalase_clade_1; 1.
DR   FunFam; 2.40.180.10:FF:000002; Catalase; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
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; CATALASE; 1.
DR   PANTHER; PTHR11465:SF64; CATALASE ISOZYME 1; 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; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Peroxisome; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme 2"
FT                   /id="PRO_0000084962"
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;  56451 MW;  5C84E2C381F2C140 CRC64;
     MDPSKYRPSS AYDTPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYYLIEK LATFDREKIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGAQTPVI CRFSTVVHER GSPESIRDIR
     GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQENW RILDFFSFLP
     ESLHTFAFFY DDVCLPTDYR HMEGFGVHAY QLINKEGKAH YVKFHWKPTC GVKSMSEEEA
     IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQTMDPEDVD KFDFDPLDVT KTWPEDLLPL
     IPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGIYYSEDKL LQTRIFAYAD TQRHRIGPNY
     MQLPVNAPKC GHHNNHRDGA MNMTHRDEEV DYLPSRFDPC RPAEQYPIPA CVLNGRRTNC
     VIPKENNFKQ AGERYRSWES DRQDRYITKW VESLSDPRVT HEIRSIWISY LSQADKSCGQ
     KVASRLTVKP TM
//