ID   CATA2_GOSHI             Reviewed;         492 AA.
AC   P30567;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Catalase isozyme 2;
DE            EC=1.11.1.6;
GN   Name=CAT2; Synonyms=SU2;
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Deltapine 62; TISSUE=Cotyledon;
RX   PubMed=1898069; DOI=10.1016/0003-9861(91)90467-w;
RA   Ni W., Trelease R.N.;
RT   "Two genes encode the two subunits of cottonseed catalase.";
RL   Arch. Biochem. Biophys. 289:237-243(1991).
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   -!- MISCELLANEOUS: There are at least five isozymes of catalase in cotton.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; X56675; CAA39998.1; -; mRNA.
DR   PIR; S17493; S17493.
DR   RefSeq; NP_001314401.1; NM_001327472.1.
DR   AlphaFoldDB; P30567; -.
DR   SMR; P30567; -.
DR   STRING; 3635.P30567; -.
DR   PeroxiBase; 1803; GhKat02.
DR   GeneID; 107943729; -.
DR   KEGG; ghi:107943729; -.
DR   Proteomes; UP000189702; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; TAS:AgBase.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
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; IDA:AgBase.
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   GO; GO:0009845; P:seed germination; IDA:AgBase.
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; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme 2"
FT                   /id="PRO_0000084939"
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;  56935 MW;  589FD8DCA173AB12 CRC64;
     MDPYKFRPSS SFDSPFWTTN SGAPVWNNNS SLTVGARGPI LLEDYHLVEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD ISQLTCADFL RAPGVQTPLI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP
     ESLHMFTFLF DDIGVPQDYR HMDGSGVHTY TLINKAGKSH YVKFHWKPTC GVKSLLEDEA
     IRVGGANHSH ATQDLYDSIA AGNYPEWKLF IQIMDPLHED RFDFDPLDVT KTWPEDIFPL
     QPMGRMVLNK NIDNFFAENE QLAFCPSLIV PGIYYSDDKL LQTRIFSYSD TQRHRLGPNY
     LQLPANAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRYDPV RHAEKHPIPS TVLSGKREKC
     IIGKENNFKQ PGERYRSFSA DRQERFINRW IDALSDPRVT HEIRSIWISY WSQADKSLGQ
     KIASRLNVRP SI