CATA_TOXGO
ID CATA_TOXGO Reviewed; 502 AA.
AC Q9XZD5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Peroxisomal catalase;
DE EC=1.11.1.6;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=RH;
RX PubMed=10625653; DOI=10.1074/jbc.275.2.1112;
RA Kaasch A.J., Joiner K.A.;
RT "Targeting and subcellular localization of Toxoplasma gondii catalase.
RT Identification of peroxisomes in an apicomplexan parasite.";
RL J. Biol. Chem. 275:1112-1118(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RH;
RX PubMed=10852820; DOI=10.1242/jcs.113.13.2409;
RA Ding M., Clayton C., Soldati D.;
RT "Toxoplasma gondii catalase: are there peroxisomes in toxoplasma?";
RL J. Cell Sci. 113:2409-2419(2000).
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; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AF136344; AAD30129.1; -; mRNA.
DR EMBL; AF161267; AAD45528.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9XZD5; -.
DR SMR; Q9XZD5; -.
DR PeroxiBase; 8428; TgKat01.
DR VEuPathDB; ToxoDB:TGARI_232250; -.
DR VEuPathDB; ToxoDB:TGCAST_232250; -.
DR VEuPathDB; ToxoDB:TGCOUG_232250; -.
DR VEuPathDB; ToxoDB:TGDOM2_232250; -.
DR VEuPathDB; ToxoDB:TGFOU_232250; -.
DR VEuPathDB; ToxoDB:TGGT1_232250; -.
DR VEuPathDB; ToxoDB:TGMAS_232250; -.
DR VEuPathDB; ToxoDB:TGME49_232250; -.
DR VEuPathDB; ToxoDB:TGP89_232250A; -.
DR VEuPathDB; ToxoDB:TGPRC2_232250; -.
DR VEuPathDB; ToxoDB:TGRH88_076380; -.
DR VEuPathDB; ToxoDB:TGRUB_232250; -.
DR VEuPathDB; ToxoDB:TGVAND_232250A; -.
DR VEuPathDB; ToxoDB:TGVEG_232250; -.
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 CDD; cd08156; catalase_clade_3; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
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..502
FT /note="Peroxisomal catalase"
FT /id="PRO_0000084913"
FT MOTIF 500..502
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 347
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 502 AA; 57270 MW; FBA8F0551434B74D CRC64;
MTQVPPVTFQ QYGPVITTSA GNPVDDNQNS VTAGPYGPAI LSNFHLIDKL AHFDRERIPE
RVVHAKGGGA FGYFEVTHDI TRFCKAKLFE KIGKRTPVFA RFSTVAGESG SADTRRDPRG
FALKFYTEEG NWDMVGNNTP IFFVRDAIKF PDFIHTQKRH PQTHLHDPNM VWDFFSLVPE
SVHQVTFLYT DRGTPDGFRH MNGYGSHTFK FINKDNEAFY VKWHFKTNQG IKNLNRQRAK
ELESEDPDYA VRDLFNAIAK REFPSWTFCI QVMPLKDAET YKWNVFDVTK VWPHGDYPLI
PVGKLVLDRN PENYFQDVEQ AAFAPAHMVP GIEPSEDRML QGRMFSYIDT HRHRLGANYH
QIPVNRPWNA RGGDYSVRDG PMCVDGNKGS QLNYEPNSVD GFPKEDRNAA VSGTTTVSGT
VACHPQEHPN SDFEQPGNFY RTVLSEPERE ALIGNIAEHL RQARRDIQER QVKIFYKCDP
EYGERVARAI GLPTAACYPA KM
