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Database: UniProt/SWISS-PROT
Entry: SODC1_DICDI
LinkDB: SODC1_DICDI
Original site: SODC1_DICDI 
ID   SODC1_DICDI             Reviewed;         153 AA.
AC   Q55GQ5; O77243;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
GN   Name=sodA; ORFNames=DDB_G0267420;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-153.
RC   STRAIN=AX3-1;
RX   PubMed=11004503; DOI=10.1016/s0167-4781(00)00063-4;
RA   Garcia M.X.U., Foote C., van Es S., Devreotes P.N., Alexander S.,
RA   Alexander H.;
RT   "Differential developmental expression and cell type specificity of
RT   Dictyostelium catalases and their response to oxidative stress and UV-
RT   light.";
RL   Biochim. Biophys. Acta 1492:295-310(2000).
RN   [3]
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=12186757; DOI=10.1080/10258140290018711;
RA   Tsuji A., Akaza Y., Kodaira K., Yasukawa H.;
RT   "Copper/zinc superoxide dismutases in Dictyostelium discoideum: amino acid
RT   sequences and expression kinetics.";
RL   J. Biochem. Mol. Biol. Biophys. 6:215-220(2002).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- DEVELOPMENTAL STAGE: Expressed in cells in the growth phase and
CC       throughout the developmental phases. {ECO:0000269|PubMed:12186757}.
CC   -!- INDUCTION: By H(2)O(2) exposure but not by UV irradiation.
CC       {ECO:0000269|PubMed:12186757}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000003; EAL73162.1; -; Genomic_DNA.
DR   EMBL; AF092899; AAC62106.1; -; mRNA.
DR   RefSeq; XP_647129.1; XM_642037.1.
DR   AlphaFoldDB; Q55GQ5; -.
DR   SMR; Q55GQ5; -.
DR   STRING; 44689.Q55GQ5; -.
DR   PaxDb; 44689-DDB0191290; -.
DR   EnsemblProtists; EAL73162; EAL73162; DDB_G0267420.
DR   GeneID; 8615933; -.
DR   KEGG; ddi:DDB_G0267420; -.
DR   dictyBase; DDB_G0267420; sodA.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   InParanoid; Q55GQ5; -.
DR   OMA; NSGDRWA; -.
DR   PhylomeDB; Q55GQ5; -.
DR   Reactome; R-DDI-114608; Platelet degranulation.
DR   Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:Q55GQ5; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IMP:dictyBase.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR   GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:dictyBase.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:dictyBase.
DR   GO; GO:0006801; P:superoxide metabolic process; IMP:dictyBase.
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 [CU-ZN]; 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.
PE   2: Evidence at transcript level;
KW   Antioxidant; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..153
FT                   /note="Superoxide dismutase [Cu-Zn] 1"
FT                   /id="PRO_0000311820"
FT   BINDING         46
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..146
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   153 AA;  15856 MW;  8DA20D942E832098 CRC64;
     MSKTAVCVIK GEKVNGVVKF TQENKDSPVT VNYDITGLEK GEHGFHVHAF GDTTNGCVSA
     GPHFNPFGKN HGAPSDEDRH VGDLGNIVAD GESNTKGTIS DKIISLFGEH TIVGRTMVVH
     ADQDDLGKGG KPDSLTTGAA GARLGCGVIG VSQ
//
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