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Database: UniProt
Entry: J1K8X0_BARTA
LinkDB: J1K8X0_BARTA
Original site: J1K8X0_BARTA 
ID   J1K8X0_BARTA            Unreviewed;       178 AA.
AC   J1K8X0;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   10-APR-2019, entry version 30.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=ME9_01068 {ECO:0000313|EMBL:EJF94147.1};
OS   Bartonella taylorii 8TBB.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094560 {ECO:0000313|EMBL:EJF94147.1, ECO:0000313|Proteomes:UP000002648};
RN   [1] {ECO:0000313|EMBL:EJF94147.1, ECO:0000313|Proteomes:UP000002648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8TBB {ECO:0000313|EMBL:EJF94147.1,
RC   ECO:0000313|Proteomes:UP000002648};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Kirby J., Kosoy M., Birtles R., Probert W.S.,
RA   Chiaraviglio L., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA   Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bartonella taylorii 8TBB.";
RL   Submitted (MAR-2012) 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:EJF94147.1}.
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DR   EMBL; AIMD01000035; EJF94147.1; -; Genomic_DNA.
DR   STRING; 1094560.ME9_01068; -.
DR   EnsemblBacteria; EJF94147; EJF94147; ME9_01068.
DR   PATRIC; fig|1094560.3.peg.1163; -.
DR   Proteomes; UP000002648; 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; 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:UP000002648};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       41    176       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   178 AA;  19229 MW;  E92A65CE87D337F7 CRC64;
     MFCMNKTVLP ILFSLAFLNY NTIVLAKSMK VAIYKLENKN TKKPIGTIEI EENIHGLIFV
     PNLSTLPEGL HGFHVHINPS CDTKDGVIGG AAGGHYDPEH TNKHLGPYNV NGHFGDLPAL
     YVDDKGHSTM SVLAPRIKKL SEIKGHSLMI HLGGDNQSDK PLPLGGGGAR LACGIIEE
//
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