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 27-MAR-2024, entry version 139.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=SOD;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; 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 cytosolic
RT Cu/Zn superoxide dismutase and high-yield expression of the enzymatically
RT 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., Tanaka M.,
RA Garratt R.C.;
RT "Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma
RT 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}.
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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 AlphaFoldDB; Q01137; -.
DR SMR; Q01137; -.
DR STRING; 6183.Q01137; -.
DR EnsemblMetazoa; Smp_176200.1; Smp_176200.1; Smp_176200.
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 HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; Q01137; -.
DR OrthoDB; 3470597at2759; -.
DR EvolutionaryTrace; Q01137; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF71; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 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; Copper; Cytoplasm; Disulfide bond;
KW Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..153
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164105"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:15333927"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:15333927"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:15333927"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:15333927"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT DISULFID 56..145
FT CONFLICT 115
FT /note="T -> S (in Ref. 2; AAA29935)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="I -> V (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:1TO4"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1TO4"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1TO5"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1TO4"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1TO4"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1TO4"
FT STRAND 141..147
FT /evidence="ECO:0007829|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
//
