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Database: UniProt
Entry: G3Y0L1_ASPNA
LinkDB: G3Y0L1_ASPNA
Original site: G3Y0L1_ASPNA 
ID   G3Y0L1_ASPNA            Unreviewed;       154 AA.
AC   G3Y0L1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   16-JAN-2019, entry version 36.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=ASPNIDRAFT_209716 {ECO:0000313|EMBL:EHA23922.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB
OS   Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA23922.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA23922.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R.,
RA   Albermann K., Berka R.M., Braus G.H., Braus-Stromeyer S.A.,
RA   Corrochano L.M., Dai Z., van Dijck P.W., Hofmann G., Lasure L.L.,
RA   Magnuson J.K., Menke H., Meijer M., Meijer S.L., Nielsen J.B.,
RA   Nielsen M.L., van Ooyen A.J., Pel H.J., Poulsen L., Samson R.A.,
RA   Stam H., Tsang A., van den Brink J.M., Atkins A., Aerts A.,
RA   Shapiro H., Pangilinan J., Salamov A., Lou Y., Lindquist E., Lucas S.,
RA   Grimwood J., Grigoriev I.V., Kubicek C.P., Martinez D., van Peij N.N.,
RA   Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC
RT   1015 versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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         Evidence={ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHA23922.1}.
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DR   EMBL; ACJE01000009; EHA23922.1; -; Genomic_DNA.
DR   ProteinModelPortal; G3Y0L1; -.
DR   SMR; G3Y0L1; -.
DR   EnsemblFungi; EHA23922; EHA23922; ASPNIDRAFT_209716.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   Complete proteome {ECO:0000313|Proteomes:UP000009038};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009038};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       11    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15960 MW;  C8679562F6FB52AF CRC64;
     MVKAVAVIRG DSKVSGTVTF EQANENTPTT ISWNITGHDA NAERGFHVHQ FGDNTNGCTS
     AGPHFNPFGK THGAPEDDER HVGDLGNFKT DAEGNAVGSK QDKLVKLIGA ESVLGRTLVV
     HAGTDDLGRG GNEESKKTGN AGPRPACGVI GIAA
//
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