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Database: UniProt/SWISS-PROT
Entry: SODC_SCHMA
LinkDB: SODC_SCHMA
Original site: SODC_SCHMA 
ID   SODC_SCHMA              Reviewed;         153 AA.
AC   Q01137;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   10-APR-2019, entry version 119.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1620165; DOI=10.1016/0166-6851(92)90060-W;
RA   da Silva A., Lepresle T., Capron A., Pierce R.J.;
RT   "Molecular cloning of a 16-kilodalton Cu/Zn superoxide dismutase from
RT   Schistosoma mansoni.";
RL   Mol. Biochem. Parasitol. 52:275-278(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1426133; DOI=10.1016/0014-4894(92)90216-W;
RA   Hong Z., Loverde P.T., Hammarskjold M.L., Rekosh D.;
RT   "Schistosoma mansoni: cloning of a complementary DNA encoding a
RT   cytosolic Cu/Zn superoxide dismutase and high-yield expression of the
RT   enzymatically active gene product in Escherichia coli.";
RL   Exp. Parasitol. 75:308-322(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NMRI;
RX   PubMed=7895835; DOI=10.1006/expr.1995.1031;
RA   Mei H., Hirai H., Tanaka M., Hong Z., Rekosh D., Loverde P.T.;
RT   "Schistosoma mansoni: cloning and characterization of a gene encoding
RT   cytosolic Cu/Zn superoxide dismutase.";
RL   Exp. Parasitol. 80:250-259(1995).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ZINC AND COPPER
RP   IONS, AND SUBUNIT.
RX   PubMed=15333927; DOI=10.1107/S0907444904016798;
RA   Cardoso R.M.F., Silva C.H.T.P., Ulian de Araujo A.P., Tanaka T.,
RA   Tanaka M., Garratt R.C.;
RT   "Structure of the cytosolic Cu,Zn superoxide dismutase from
RT   Schistosoma mansoni.";
RL   Acta Crystallogr. D 60:1569-1578(2004).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       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=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds 1 copper ion per subunit.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15333927}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; M86867; AAA29936.1; -; mRNA.
DR   EMBL; M97298; AAA29935.1; -; mRNA.
DR   EMBL; L12159; AAC14467.1; -; Genomic_DNA.
DR   EMBL; L12008; AAC14467.1; JOINED; Genomic_DNA.
DR   EMBL; L12158; AAC14467.1; JOINED; Genomic_DNA.
DR   PIR; A49241; A49241.
DR   RefSeq; XP_018646947.1; XM_018795564.1.
DR   PDB; 1TO4; X-ray; 1.55 A; A/B/C/D=1-153.
DR   PDB; 1TO5; X-ray; 2.20 A; A/B/C/D=1-153.
DR   PDBsum; 1TO4; -.
DR   PDBsum; 1TO5; -.
DR   ProteinModelPortal; Q01137; -.
DR   SMR; Q01137; -.
DR   STRING; 6183.Smp_176200.2; -.
DR   PRIDE; Q01137; -.
DR   GeneDB; Smp_176200.1:pep; -.
DR   GeneID; 8341912; -.
DR   KEGG; smm:Smp_176200.1; -.
DR   WBParaSite; Smp_176200.1; Smp_176200.1; Smp_176200.
DR   CTD; 8341912; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   EvolutionaryTrace; Q01137; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antioxidant; Complete proteome; Copper; Cytoplasm;
KW   Disulfide bond; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN         1    153       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164105.
FT   METAL        45     45       Copper; catalytic.
FT   METAL        47     47       Copper; catalytic.
FT   METAL        62     62       Copper; catalytic.
FT   METAL        62     62       Zinc; structural.
FT                                {ECO:0000269|PubMed:15333927}.
FT   METAL        70     70       Zinc; structural.
FT                                {ECO:0000269|PubMed:15333927}.
FT   METAL        79     79       Zinc; structural.
FT                                {ECO:0000269|PubMed:15333927}.
FT   METAL        82     82       Zinc; structural.
FT                                {ECO:0000269|PubMed:15333927}.
FT   METAL       119    119       Copper; catalytic.
FT   DISULFID     56    145
FT   CONFLICT    115    115       T -> S (in Ref. 2; AAA29935).
FT                                {ECO:0000305}.
FT   CONFLICT    148    148       I -> V (in Ref. 2 and 3). {ECO:0000305}.
FT   STRAND        2      8       {ECO:0000244|PDB:1TO4}.
FT   STRAND       10     12       {ECO:0000244|PDB:1TO4}.
FT   STRAND       14     23       {ECO:0000244|PDB:1TO4}.
FT   STRAND       28     36       {ECO:0000244|PDB:1TO4}.
FT   STRAND       39     48       {ECO:0000244|PDB:1TO4}.
FT   TURN         53     56       {ECO:0000244|PDB:1TO4}.
FT   HELIX        57     59       {ECO:0000244|PDB:1TO4}.
FT   STRAND       76     78       {ECO:0000244|PDB:1TO5}.
FT   STRAND       82     88       {ECO:0000244|PDB:1TO4}.
FT   STRAND       94    102       {ECO:0000244|PDB:1TO4}.
FT   STRAND      104    106       {ECO:0000244|PDB:1TO4}.
FT   HELIX       107    109       {ECO:0000244|PDB:1TO4}.
FT   STRAND      114    121       {ECO:0000244|PDB:1TO4}.
FT   HELIX       133    136       {ECO:0000244|PDB:1TO4}.
FT   STRAND      141    147       {ECO:0000244|PDB:1TO4}.
SQ   SEQUENCE   153 AA;  15721 MW;  D30014FDBD34593A CRC64;
     MKAVCVMTGT AGVKGVVKFT QETDNGPVHV HAEFSGLKAG KHGFHVHEFG DTTNGCTSAG
     AHFNPTKQEH GAPEDSIRHV GDLGNVVAGA DGNAVYNATD KLISLNGSHS IIGRTMVIHE
     NEDDLGRGGH ELSKVTGNAG GRLACGVIGL AAE
//
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