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Database: UniProt/SWISS-PROT
Entry: SODC_ASHGO
LinkDB: SODC_ASHGO
Original site: SODC_ASHGO 
ID   SODC_ASHGO              Reviewed;         154 AA.
AC   Q751L8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 4.
DT   20-DEC-2017, entry version 96.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD1; OrderedLocusNames=AGL321W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 5.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; AE016820; AAS54170.2; -; Genomic_DNA.
DR   RefSeq; NP_986346.2; NM_211408.2.
DR   SMR; Q751L8; -.
DR   STRING; 33169.AAS54170; -.
DR   EnsemblFungi; AAS54170; AAS54170; AGOS_AGL321W.
DR   GeneID; 4622639; -.
DR   KEGG; ago:AGOS_AGL321W; -.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; Q751L8; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG092C578I; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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   3: Inferred from homology;
KW   Antioxidant; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164106.
FT   METAL        47     47       Copper. {ECO:0000250}.
FT   METAL        49     49       Copper. {ECO:0000250}.
FT   METAL        64     64       Copper. {ECO:0000250}.
FT   METAL        64     64       Zinc. {ECO:0000250}.
FT   METAL        72     72       Zinc. {ECO:0000250}.
FT   METAL        81     81       Zinc. {ECO:0000250}.
FT   METAL        84     84       Zinc. {ECO:0000250}.
FT   METAL       121    121       Copper. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
SQ   SEQUENCE   154 AA;  15884 MW;  E9F7821A879FD83D CRC64;
     MVKAIAVLKG DAGVSGVVHF EQEADAAVTT ISWNITGFEP NTEHGFHIHE FGDVTNGCTS
     SGSHFNPFKK THGSPEDENR HVGDMGNVLA DANGVAVGSA KDPLIKIFGP TSILGRTVVV
     HAGKDDLGRG GNEESLKTGN AGPRPACGVI GIAN
//
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