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 03-AUG-2022, entry version 120.
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; 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.DDB0191290; -.
DR PaxDb; 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 HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; Q55GQ5; -.
DR OMA; DITYTDP; -.
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; -; 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; 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
