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Entry: A0A0F6AC17_9GAMM
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ID   A0A0F6AC17_9GAMM        Unreviewed;       182 AA.
AC   A0A0F6AC17;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   05-DEC-2018, entry version 15.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=N479_14535 {ECO:0000313|EMBL:KKE83356.1};
OS   Pseudoalteromonas luteoviolacea S4054.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE83356.1, ECO:0000313|Proteomes:UP000033434};
RN   [1] {ECO:0000313|EMBL:KKE83356.1, ECO:0000313|Proteomes:UP000033434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4054 {ECO:0000313|EMBL:KKE83356.1,
RC   ECO:0000313|Proteomes:UP000033434};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-
RT   negative bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KKE83356.1}.
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DR   EMBL; AUXW01000148; KKE83356.1; -; Genomic_DNA.
DR   RefSeq; WP_052960981.1; NZ_AUXW01000148.1.
DR   EnsemblBacteria; KKE83356; KKE83356; N479_14535.
DR   GeneID; 31723559; -.
DR   PATRIC; fig|1129367.4.peg.2739; -.
DR   Proteomes; UP000033434; 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   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000033434};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    182       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002499454.
FT   DOMAIN       40    178       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   182 AA;  19445 MW;  9977FA5F93A0B75A CRC64;
     MKKAFLAAGI TAFFCAAIST HVQATHQIGE MAHSKIINNQ GKQVGTAHYT QGNEGVVIEI
     IAQQLPAGKH GMHFHEVGTC VDKHHFKKAK GHIMPSGKPH GYYHPEGPHE GNLPNLIVRE
     DGTVHVELYT ELVSISGRGN KPALLDDNGS VLMIHANEDD HLTQPIGGSG SRIGCGLVVS
     GK
//
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