ID   CATA_HELAN              Reviewed;         492 AA.
AC   P45739;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Spanners Allzweck; TISSUE=Cotyledon;
RX   PubMed=7803505; DOI=10.1016/0167-4889(94)90284-4;
RA   Kleff S., Trelease R.N., Eising R.;
RT   "Nucleotide and deduced amino acid sequence of a putative higher molecular
RT   weight precursor for catalase in sunflower cotyledons.";
RL   Biochim. Biophys. Acta 1224:463-466(1994).
CC   -!- FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2))
CC       generated by peroxisomal oxidases to water and oxygen, thereby
CC       protecting cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000250|UniProtKB:P04040}.
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         Evidence={ECO:0000250|UniProtKB:P04040};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P25819}. Peroxisome matrix
CC       {ECO:0000250|UniProtKB:P25819}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; L28740; AAA69866.1; -; mRNA.
DR   PIR; S52079; S52079.
DR   RefSeq; NP_001415290.1; NM_001428361.1.
DR   AlphaFoldDB; P45739; -.
DR   SMR; P45739; -.
DR   PeroxiBase; 4087; HaKat01.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr08g0327621; mRNA:HanXRQr2_Chr08g0327621; HanXRQr2_Chr08g0327621.
DR   GeneID; 110872274; -.
DR   Gramene; mRNA:HanXRQr2_Chr08g0327621; mRNA:HanXRQr2_Chr08g0327621; HanXRQr2_Chr08g0327621.
DR   OMA; FYNQGAR; -.
DR   OrthoDB; 6880011at2759; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
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:SF23; CATALASE-2; 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   2: Evidence at transcript level;
KW   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Peroxisome.
FT   CHAIN           1..492
FT                   /note="Catalase"
FT                   /id="PRO_0000084940"
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|UniProtKB:P04040"
SQ   SEQUENCE   492 AA;  56755 MW;  4A5C596506F44961 CRC64;
     MDPYKYRSSS AYNAPFWTTN SGAPVYNNNN SLTVGSRGPI LLEDYHLVEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD ITALTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHSLKP NPKSHIQEDW RIMDFFSHHP
     ESLHMFTFLL DDIGVPQDYR HMDGSGVNTY TLINKAGKAY YVKFHWKPTC GVKSLLEEEA
     IKIGGANHSH ATQDLYDSIA AGNYPEWKLF IQTIDPDHED RLDFDPLDVT KTWPEDIFPL
     QPVGRLVLNK NIDNFFAENE QLAFCPAIIV PGIYYSDDKL LQTRIFSYSD TQRHRLGPNY
     LQLPANAPKC AHHNNHYDGF MNFMHRDEEI DYFPSRYDPA RHAEQYPIPP VRLSGKRDKC
     VIEKENNFKQ PGERYRSFSP DRQERFINRV VGGLSDPRVT HEVRSIWVSY WSQADKSLGQ
     KIASRLNVKP NY
//