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Database: UniProt/TrEMBL
Entry: A0A0H3LTP4_BARQU
LinkDB: A0A0H3LTP4_BARQU
Original site: A0A0H3LTP4_BARQU 
ID   A0A0H3LTP4_BARQU        Unreviewed;       200 AA.
AC   A0A0H3LTP4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:CAF25882.1};
GN   OrderedLocusNames=BQ03820 {ECO:0000313|EMBL:CAF25882.1};
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165 {ECO:0000313|EMBL:CAF25882.1, ECO:0000313|Proteomes:UP000000597};
RN   [1] {ECO:0000313|EMBL:CAF25882.1, ECO:0000313|Proteomes:UP000000597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse {ECO:0000313|EMBL:CAF25882.1,
RC   ECO:0000313|Proteomes:UP000000597};
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; BX897700; CAF25882.1; -; Genomic_DNA.
DR   RefSeq; WP_011179172.1; NC_005955.1.
DR   ProteinModelPortal; A0A0H3LTP4; -.
DR   STRING; 283165.BQ03820; -.
DR   EnsemblBacteria; CAF25882; CAF25882; BQ03820.
DR   GeneID; 13563242; -.
DR   KEGG; bqr:RM11_0367; -.
DR   KEGG; bqu:BQ03820; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000000597; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000597};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    191       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  23102 MW;  85AA5BC5601F994D CRC64;
     MAFELAKLPY DYDALSPYMS RETLEYHHDK HHLAYLTNTN NFVKDLGLEN ESLEHIVKKS
     FGQNIGLFNN AAQYYNHNHF WHWMKKGGGG QKLPEKLAKA IESDLGGYNK FRADFIAAAV
     AQFGSGWAWV AVKDGKLEIM KTSNSENPLV HDAQPILGVD VWEHSYYIDY RNARPKYLEA
     FVDNLINWDY VLKLYEDCGF
//
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