ID   C4LX20_ENTH1            Unreviewed;       190 AA.
AC   C4LX20; A0A175JIL5;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN   ORFNames=EHI_159160 {ECO:0000313|EMBL:EAL43440.1};
OS   Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=294381 {ECO:0000313|EMBL:EAL43440.1, ECO:0000313|Proteomes:UP000001926};
RN   [1] {ECO:0000313|EMBL:EAL43440.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM-1:IMSS {ECO:0000313|EMBL:EAL43440.1};
RX   PubMed=15729342; DOI=10.1038/nature03291;
RA   Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA   Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA   Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA   Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA   Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA   Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA   Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA   Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA   Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA   Barrell B.G., Fraser C.M., Hall N.;
RT   "The genome of the protist parasite Entamoeba histolytica.";
RL   Nature 433:865-868(2005).
RN   [2] {ECO:0000313|EMBL:EAL43440.1}
RP   GENOME REANNOTATION.
RC   STRAIN=HM-1:IMSS {ECO:0000313|EMBL:EAL43440.1};
RA   Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL   Submitted (MAR-2007) 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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; DS571167; EAL43440.1; -; Genomic_DNA.
DR   RefSeq; XP_648827.1; XM_643735.2.
DR   AlphaFoldDB; C4LX20; -.
DR   SMR; C4LX20; -.
DR   STRING; 5759.C4LX20; -.
DR   EnsemblProtists; GAT93272; GAT93272; CL6EHI_159160.
DR   EnsemblProtists; rna_EHI_159160-1; rna_EHI_159160-1; EHI_159160.
DR   GeneID; 3403104; -.
DR   KEGG; ehi:EHI_159160; -.
DR   VEuPathDB; AmoebaDB:EHI5A_272690; -.
DR   VEuPathDB; AmoebaDB:EHI_159160; -.
DR   VEuPathDB; AmoebaDB:KM1_324680; -.
DR   HOGENOM; CLU_031625_0_0_1; -.
DR   InParanoid; C4LX20; -.
DR   OMA; DSLINWD; -.
DR   OrthoDB; 4839at2759; -.
DR   Proteomes; UP000001926; Partially assembled 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; IPR019833; Mn/Fe_SOD_BS.
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   PIRSF; PIRSF000349; SODismutase; 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.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001926}.
FT   DOMAIN          2..83
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          89..188
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         156
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   190 AA;  22060 MW;  5C761B81C2F0539B CRC64;
     MSFQLPQLPY AYNALEPHIS KETLEFHHDK HHATYVNKLN GLVKGTEQEH KTLEELIKQK
     PTQAIYNNAA QAWNHAFYWK CMCGCGVKPS EQLIAKLTAA FGGLEEFKKK FTEKAVGHFG
     SGWCWLVEHD GKLEIIDTHD AVNPMTNGMK PLLTCDVWEH AYYIDTRNNR AAYLEHWWNV
     VNWKFVEEQL
//