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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   05-DEC-2018, entry version 105.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
GN   Name=sodA; ORFNames=DDB_G0267420;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
RT   acid 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.
CC       {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}.
DR   EMBL; AAFI02000003; EAL73162.1; -; Genomic_DNA.
DR   EMBL; AF092899; AAC62106.1; -; mRNA.
DR   RefSeq; XP_647129.1; XM_642037.1.
DR   ProteinModelPortal; Q55GQ5; -.
DR   SMR; Q55GQ5; -.
DR   STRING; 44689.DDB0191290; -.
DR   PaxDb; Q55GQ5; -.
DR   PRIDE; Q55GQ5; -.
DR   EnsemblProtists; EAL73162; EAL73162; DDB_G0267420.
DR   GeneID; 8615933; -.
DR   KEGG; ddi:DDB_G0267420; -.
DR   dictyBase; DDB_G0267420; sodA.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; Q55GQ5; -.
DR   KO; K04565; -.
DR   OMA; MAKAVCT; -.
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   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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; -; 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.
PE   2: Evidence at transcript level;
KW   Antioxidant; Complete proteome; Copper; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    153       Superoxide dismutase [Cu-Zn] 1.
FT                                /FTId=PRO_0000311820.
FT   METAL        46     46       Copper; catalytic. {ECO:0000250}.
FT   METAL        48     48       Copper; catalytic. {ECO:0000250}.
FT   METAL        63     63       Copper; catalytic. {ECO:0000250}.
FT   METAL        63     63       Zinc; structural. {ECO:0000250}.
FT   METAL        71     71       Zinc; structural. {ECO:0000250}.
FT   METAL        80     80       Zinc; structural. {ECO:0000250}.
FT   METAL        83     83       Zinc; structural. {ECO:0000250}.
FT   METAL       120    120       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     57    146       {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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