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Database: UniProt/TrEMBL
Entry: A0A097AQH1_THEKI
LinkDB: A0A097AQH1_THEKI
Original site: A0A097AQH1_THEKI 
ID   A0A097AQH1_THEKI        Unreviewed;       198 AA.
AC   A0A097AQH1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
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:AIS52060.1};
GN   ORFNames=TKV_c08790 {ECO:0000313|EMBL:AIS52060.1};
OS   Thermoanaerobacter kivui (Acetogenium kivui).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=2325 {ECO:0000313|EMBL:AIS52060.1, ECO:0000313|Proteomes:UP000029669};
RN   [1] {ECO:0000313|Proteomes:UP000029669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25676747;
RA   Johnson S.L., Baker A.L., Chain P.S., Currie B.J., Daligault H.E.,
RA   Davenport K.W., Davis C.B., Inglis T.J., Kaestli M., Koren S.,
RA   Mayo M., Merritt A.J., Price E.P., Sarovich D.S., Warner J.,
RA   Rosovitz M.J.;
RT   "Whole-Genome Sequences of 80 Environmental and Clinical Isolates of
RT   Burkholderia pseudomallei.";
RL   Genome Announc. 3:0-0(2015).
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; CP009170; AIS52060.1; -; Genomic_DNA.
DR   RefSeq; WP_049684871.1; NZ_CP009170.1.
DR   EnsemblBacteria; AIS52060; AIS52060; TKV_c08790.
DR   KEGG; tki:TKV_c08790; -.
DR   KO; K04564; -.
DR   Proteomes; UP000029669; 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; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000029669};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AIS52060.1}.
FT   DOMAIN       16     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       88    188       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        24     24       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       155    155       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       159    159       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   198 AA;  23234 MW;  3ADDFD0017B6C7CD CRC64;
     MDKLVAKKYN LVLRGISQRT LEEHYKLYNG YVEKTNEIRE KLKTVDRSKA NASYSEYREL
     KLEETYNLDG VKLHELYFEN LGGPGGIPDG IIASMITLDF GSFENWRQDF IACGMASRGW
     TVLCFDPIDL KLHNYLQDLH NQGIVLRTIP LLVLDTYEHA YFIDYGTDKR SYIEAFMNNI
     KWEEVNRRVT SWIEMHSF
//
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