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Database: UniProt/TrEMBL
Entry: A9I3N3_BORPD
LinkDB: A9I3N3_BORPD
Original site: A9I3N3_BORPD 
ID   A9I3N3_BORPD            Unreviewed;       176 AA.
AC   A9I3N3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   25-OCT-2017, entry version 63.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=Bpet3851 {ECO:0000313|EMBL:CAP44196.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44196.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP44196.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A.,
RA   Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J.,
RA   Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N.,
RA   Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D.,
RA   Rueckert C., Schneiker-Bekel S., Schulze K., Vorhoelter F.J.,
RA   Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B.,
RA   Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the
RT   metabolic versatility of environmental bacteria and virulence traits
RT   of pathogenic Bordetellae.";
RL   BMC Genomics 9:449-449(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; AM902716; CAP44196.1; -; Genomic_DNA.
DR   ProteinModelPortal; A9I3N3; -.
DR   STRING; 340100.Bpet3851; -.
DR   EnsemblBacteria; CAP44196; CAP44196; Bpet3851.
DR   KEGG; bpt:Bpet3851; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
DR   Proteomes; UP000001225; 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; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001225};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CAP44196.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001225};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    176       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002736323.
FT   DOMAIN       37    174       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   176 AA;  17623 MW;  06AC0F323170BE1A CRC64;
     MQHCLKLVLL AGALGLAAAA RADVTVPMHL AGDKGPGSEI GSVSLADSKY GLVLTPALKG
     LPPGVHGFHV HENASCDAKQ QDGKAVPAGA AGGHYDPDGA KKHGAPWSDD SHRGDLPALY
     VGADGSAATP VLAPRLKLAD VRGRALMVHA GGDNHSDHPK PLGGGGGRIA CGVIPK
//
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