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Database: UniProt/TrEMBL
Entry: A4VMM2_PSEU5
LinkDB: A4VMM2_PSEU5
Original site: A4VMM2_PSEU5 
ID   A4VMM2_PSEU5            Unreviewed;       173 AA.
AC   A4VMM2;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   25-OCT-2017, entry version 68.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC {ECO:0000313|EMBL:ABP80223.1};
GN   OrderedLocusNames=PST_2573 {ECO:0000313|EMBL:ABP80223.1};
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731 {ECO:0000313|EMBL:ABP80223.1, ECO:0000313|Proteomes:UP000000233};
RN   [1] {ECO:0000313|EMBL:ABP80223.1, ECO:0000313|Proteomes:UP000000233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501 {ECO:0000313|EMBL:ABP80223.1,
RC   ECO:0000313|Proteomes:UP000000233};
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H.,
RA   Zhan Y., Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the
RT   genome of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP000304; ABP80223.1; -; Genomic_DNA.
DR   RefSeq; WP_011913684.1; NC_009434.1.
DR   ProteinModelPortal; A4VMM2; -.
DR   STRING; 379731.PST_2573; -.
DR   EnsemblBacteria; ABP80223; ABP80223; PST_2573.
DR   KEGG; psa:PST_2573; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
DR   Proteomes; UP000000233; 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:UP000000233};
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:UP000000233};
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_5002675329.
FT   DOMAIN       35    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   173 AA;  17625 MW;  8447A0CD8C679D68 CRC64;
     MKQWIIAALA GCTALAAQAE TLSVKVNAVT AQGIGESVGS VKIESSEYGL VFRPELTGLQ
     AGLHGFHIHA KGSCEPAEVD GKPTAAGAAA GHWDPKNTGK HGEPWGDGHM GDLPALYVDS
     DGKASQPVLA PRLKSLGDIK GLALMVHQGG DNHSDHPQPL GGGGARVACG VIE
//
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