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Database: UniProt
Entry: P34107
LinkDB: P34107
Original site: P34107 
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   05-DEC-2018, entry version 94.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=SODB;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Archamoebae; Entamoebidae; 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
RT   and 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;
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.,
RA   Amedeo P., Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T.,
RA   Suh B., Pop M., Duchene M., Ackers J., Tannich E., Leippe M.,
RA   Hofer M., Bruchhaus I., Willhoeft U., Bhattacharya A.,
RA   Chillingworth T., Churcher C.M., Hance Z., Harris B., Harris D.,
RA   Jagels K., Moule S., Mungall K.L., Ormond D., Squares R.,
RA   Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H., Price C.,
RA   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
CC       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
CC       family. {ECO:0000305}.
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   ProteinModelPortal; P34107; -.
DR   SMR; P34107; -.
DR   STRING; 5759.rna_EHI_159160-1; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
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; 2.40.500.20; -; 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   Complete proteome; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    190       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159965.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        75     75       Iron. {ECO:0000250}.
FT   METAL       156    156       Iron. {ECO:0000250}.
FT   METAL       160    160       Iron. {ECO:0000250}.
FT   VARIANT      94     94       I -> T (in strain: SAW 142).
FT   VARIANT     142    142       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
//
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