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Database: UniProt
Entry: W8R0Q9_PSEST
LinkDB: W8R0Q9_PSEST
Original site: W8R0Q9_PSEST 
ID   W8R0Q9_PSEST            Unreviewed;       173 AA.
AC   W8R0Q9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   16-JAN-2019, entry version 26.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=CH92_14210 {ECO:0000313|EMBL:AHL76184.1};
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316 {ECO:0000313|EMBL:AHL76184.1, ECO:0000313|Proteomes:UP000019522};
RN   [1] {ECO:0000313|Proteomes:UP000019522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28a24 {ECO:0000313|Proteomes:UP000019522};
RX   PubMed=24903873;
RA   Smith B.A., Dougherty K.M., Baltrus D.A.;
RT   "Complete Genome Sequence of the Highly Transformable Pseudomonas
RT   stutzeri Strain 28a24.";
RL   Genome Announc. 2:e00543-14(2014).
RN   [2] {ECO:0000313|EMBL:AHL76184.1, ECO:0000313|Proteomes:UP000019522}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=28a24 {ECO:0000313|EMBL:AHL76184.1,
RC   ECO:0000313|Proteomes:UP000019522};
RA   Baltrus D., Dougherty K.;
RL   Submitted (MAR-2014) 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}.
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DR   EMBL; CP007441; AHL76184.1; -; Genomic_DNA.
DR   RefSeq; WP_025242384.1; NZ_CP007441.1.
DR   EnsemblBacteria; AHL76184; AHL76184; CH92_14210.
DR   KEGG; pstt:CH92_14210; -.
DR   PATRIC; fig|316.77.peg.2838; -.
DR   KO; K04565; -.
DR   OrthoDB; 2015673at2; -.
DR   Proteomes; UP000019522; Chromosome.
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; 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:UP000019522};
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     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    173       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004912416.
FT   DOMAIN       33    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   173 AA;  17621 MW;  203740DDCB66C103 CRC64;
     MKQWIIAALA GCTAMSLQAE TLSVPMKAVT AKGVGESVGT VKIESSPYGL VFRPELSGLD
     SGAHGFHIHA KGSCDPADKD GETIAAGAAG GHWDPKNAGK HGEPWGEGHM GDLPALMVDG
     EGHANQPVLA PRLKSLGDIK GLALMVHKGG DNHSDHPQPL GGGGARVACG LIE
//
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