GenomeNet

Database: UniProt/TrEMBL
Entry: I3VXB7_THESW
LinkDB: I3VXB7_THESW
Original site: I3VXB7_THESW 
ID   I3VXB7_THESW            Unreviewed;       198 AA.
AC   I3VXB7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   25-OCT-2017, entry version 24.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Tsac_2158 {ECO:0000313|EMBL:AFK87162.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK87162.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) 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: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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP003184; AFK87162.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFK87162; AFK87162; Tsac_2158.
DR   KEGG; tsh:Tsac_2158; -.
DR   PATRIC; fig|1094508.3.peg.2185; -.
DR   KO; K04564; -.
DR   OMA; YEHAYFI; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; TSAC1094508:GLMA-2189-MONOMER; -.
DR   Proteomes; UP000006178; 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:UP000006178};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006178}.
FT   DOMAIN       16     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    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;  23159 MW;  ACB1D12A03141F49 CRC64;
     MKRLIPKKYN LVLNGISQKT LQEHYKLYEG YVNKTNEIWE KLTTSDRENA NATYSQYREL
     KLEETYALDG VKLHELYFEN LGGTGGPATG IIASMITYDF GSYENWLNDF KACAISSRGW
     TVLCFDPIDL KLHNYLQDLH NHGIISRSIP LLIIDTYEHA YFIDYGTDKK GYIDAFMNNV
     KWDEVNKRVY NWIDMKKI
//
DBGET integrated database retrieval system