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Database: UniProt
Entry: A0A0W7X223_9ACTN
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ID   A0A0W7X223_9ACTN        Unreviewed;       197 AA.
AC   A0A0W7X223;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   05-DEC-2018, entry version 9.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=AT728_23230 {ECO:0000313|EMBL:KUF16827.1};
OS   Streptomyces silvensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF16827.1, ECO:0000313|Proteomes:UP000054804};
RN   [1] {ECO:0000313|EMBL:KUF16827.1, ECO:0000313|Proteomes:UP000054804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF16827.1,
RC   ECO:0000313|Proteomes:UP000054804};
RA   Johnston C.W., Li Y., Magarvey N.A.;
RT   "Draft genome sequence of Streptomyces silvensis ATCC 53525, a
RT   producer of novel hormone antagonists.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF16827.1}.
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DR   EMBL; LOCL01000036; KUF16827.1; -; Genomic_DNA.
DR   RefSeq; WP_058849097.1; NZ_LOCL01000036.1.
DR   EnsemblBacteria; KUF16827; KUF16827; AT728_23230.
DR   Proteomes; UP000054804; 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   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054804};
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:UP000054804};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    197       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006936940.
FT   DOMAIN       78    186       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   197 AA;  20500 MW;  12B93278E63222E7 CRC64;
     MVPSALTSAV AAVVLSVTGI SAGSAGHTAG STSPHGSGNG KTDNVQVRAE GRFVPPGAPT
     PSSAITYVQE LVPAGSWVQV SQHSDQRGTR VDLRVKGLKP GYKYGVHVHQ KPCGQKPTDA
     GGHYQNKPST DPHDTNPDNE VWLDFAARKD GSGKASAYHT WGFRRGEAAA IVIHREQGGA
     GERLACFSVP FAPPPGS
//
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