(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 102.
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 Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   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 Saccharomyces
RT   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:
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   -!- 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; ACGVIRV; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; 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:0019430; P:removal of superoxide radicals; 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;
DR   PRODOM; Q751L8.
DR   SWISS-2DPAGE; Q751L8.
KW   Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..154
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000164106"
FT   METAL           47
FT                   /note="Copper"
FT                   /evidence="ECO:0000250"
FT   METAL           49
FT                   /note="Copper"
FT                   /evidence="ECO:0000250"
FT   METAL           64
FT                   /note="Copper"
FT                   /evidence="ECO:0000250"
FT   METAL           64
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           72
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           81
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           84
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           121
FT                   /note="Copper"
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..147
FT                   /evidence="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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