SODF_ENTHI
ID SODF_ENTHI Reviewed; 190 AA.
AC P34107;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=SODB;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS, and SAW 142;
RX PubMed=1775159; DOI=10.1016/0166-6851(91)90130-x;
RA Tannich E., Bruchhaus I., Walter R.D., Horstmann R.D.;
RT "Pathogenic and nonpathogenic Entamoeba histolytica: identification and
RT molecular cloning of an iron-containing superoxide dismutase.";
RL Mol. Biochem. Parasitol. 49:61-71(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8274224; DOI=10.1089/dna.1993.12.925;
RA Bruchhaus I., Leippe M., Lioutas C., Tannich E.;
RT "Unusual gene organization in the protozoan parasite Entamoeba
RT histolytica.";
RL DNA Cell Biol. 12:925-933(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
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 [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; M63815; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M63816; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X70852; CAA50204.1; -; Genomic_DNA.
DR EMBL; DS571167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A45552; A45552.
DR AlphaFoldDB; P34107; -.
DR SMR; P34107; -.
DR STRING; 5759.rna_EHI_159160-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_272690; -.
DR VEuPathDB; AmoebaDB:EHI_159160; -.
DR VEuPathDB; AmoebaDB:KM1_324680; -.
DR eggNOG; KOG0876; Eukaryota.
DR InParanoid; P34107; -.
DR OMA; KWGSFDK; -.
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; -; 1.
DR Gene3D; 3.55.40.20; -; 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 Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 2: Evidence at transcript level;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..190
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159965"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT VARIANT 94
FT /note="I -> T (in strain: SAW 142)"
FT VARIANT 142
FT /note="V -> I (in strain: SAW 142)"
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
