ID   CATA1_GOSHI             Reviewed;         492 AA.
AC   P17598;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Catalase isozyme 1;
DE            EC=1.11.1.6;
GN   Name=CAT1; Synonyms=SU1;
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=2364113; DOI=10.1016/0167-4781(90)90044-3;
RA   Ni W., Turley R.B., Trelease R.N.;
RT   "Characterization of a cDNA encoding cottonseed catalase.";
RL   Biochim. Biophys. Acta 1049:219-222(1990).
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; X52135; CAA36380.1; -; mRNA.
DR   PIR; S10395; S10395.
DR   PIR; S10770; S10770.
DR   RefSeq; NP_001314123.1; NM_001327194.1.
DR   AlphaFoldDB; P17598; -.
DR   SMR; P17598; -.
DR   STRING; 3635.P17598; -.
DR   PeroxiBase; 437; GhKat01.
DR   PRIDE; P17598; -.
DR   GeneID; 107922122; -.
DR   KEGG; ghi:107922122; -.
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 1"
FT                   /id="PRO_0000084938"
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;  56855 MW;  64886966A095F261 CRC64;
     MDPYKHRPSS AFNSPFWTTN SGAPVWNNNS SLTVGPRGQY LLEDYHLVEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP
     ESLHMFTFLF DDLGVPQDYR HMEGSGVNTY TLINKAGKAH YVKFHWKPTC GVKCLLEDEA
     IKVGGANHSH ATQDLYDSIA AGNYPEWKLF IQTIDPDHED KFDFDPLDVT KTWPEDILPL
     QPVGRLVLNK NIDNFFAENE QLAFCPAIVV PGIYYSDDKL LQTRIFSYSD TQRHRLGPNY
     LQLPANAPKC AHHNNHHEGF MNFMHRDEEI NYFPSRYDPV RHAEMFPIPP AVCTGRREKC
     IIEKENNFKQ PGERYRSWAA DRQERFICRW VDALSDPRVT HEIRSIWISY WSQADKSVGQ
     KLASLLNVRP SI