ID   Q85M64_TOXGO            Unreviewed;       258 AA.
AC   Q85M64; B6K9R2; B9PJB1; B9QAA3; S7VUX8; S8ETL1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=TGRH88_054910 {ECO:0000313|EMBL:KAF4639719.1};
OS   Toxoplasma gondii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811 {ECO:0000313|EMBL:AAO72229.2};
RN   [1] {ECO:0000313|EMBL:AAO72229.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Ding M., Kwok L.Y., Krauth-Siegel L., Schlueter D., Clayton C., Soldati D.;
RT   "Role of catalase and peroxiredoxins as defence mechanism against oxidative
RT   stress in Toxoplasma gondii.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF4639719.1, ECO:0000313|Proteomes:UP000557509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RH-88 {ECO:0000313|EMBL:KAF4639719.1,
RC   ECO:0000313|Proteomes:UP000557509};
RA   Lorenzi H.A., Venepally P., Rozenberg A., Sibley D.;
RT   "Genome sequence of Toxoplasma gondii RH-88 strain.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; AY254045; AAO72229.2; -; Genomic_DNA.
DR   EMBL; JAAUHK010000196; KAF4639719.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q85M64; -.
DR   SMR; Q85M64; -.
DR   VEuPathDB; ToxoDB:TGARI_316190; -.
DR   VEuPathDB; ToxoDB:TGCAST_316190; -.
DR   VEuPathDB; ToxoDB:TGCOUG_316190; -.
DR   VEuPathDB; ToxoDB:TGDOM2_316190; -.
DR   VEuPathDB; ToxoDB:TGFOU_316190; -.
DR   VEuPathDB; ToxoDB:TGGT1_316190; -.
DR   VEuPathDB; ToxoDB:TGMAS_316190; -.
DR   VEuPathDB; ToxoDB:TGME49_316190; -.
DR   VEuPathDB; ToxoDB:TGP89_316190; -.
DR   VEuPathDB; ToxoDB:TGPRC2_316190; -.
DR   VEuPathDB; ToxoDB:TGRH88_054910; -.
DR   VEuPathDB; ToxoDB:TGRUB_316190; -.
DR   VEuPathDB; ToxoDB:TGVAND_316190; -.
DR   VEuPathDB; ToxoDB:TGVEG_316190; -.
DR   OMA; HQTYVTA; -.
DR   Proteomes; UP000557509; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN          51..131
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          139..239
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
SQ   SEQUENCE   258 AA;  29678 MW;  A3D80D6F2B6EE5C5 CRC64;
     MFAAVARRTA TGTLPGAVTL FGRKSFEGYY RDYPLHPRNF GVMASLFSTG KFELPALPYD
     YNALEPYISA KTLKFHHDKH HATYVKNLNE LIKGTDYENQ KLEDIIRNAD GPTFNNAAQA
     WNHTFFWNSM KPNGGGEPTG LVKEQIDRCF SSFSKYKEEF SEKATKHFGS GWAWLVWCNE
     KRRLEVIETH DAGNPITMKK WPIITCDLWE HGYYLDRQND RGAYVKSWWS VVNWDFANEK
     LEKAMRGDPI DETVGGGQ
//