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Database: UniProt/TrEMBL
Entry: D7AN07_THEM3
LinkDB: D7AN07_THEM3
Original site: D7AN07_THEM3 
ID   D7AN07_THEM3            Unreviewed;       198 AA.
AC   D7AN07;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Tmath_0836 {ECO:0000313|EMBL:ADH60573.1};
OS   Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CIP
OS   108742 / A3).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH60573.1, ECO:0000313|Proteomes:UP000002064};
RN   [1] {ECO:0000313|EMBL:ADH60573.1, ECO:0000313|Proteomes:UP000002064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11426 / CIP 108742 / A3
RC   {ECO:0000313|Proteomes:UP000002064};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT   mathranii str. A3.";
RL   Submitted (MAY-2010) 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}.
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DR   EMBL; CP002032; ADH60573.1; -; Genomic_DNA.
DR   RefSeq; WP_013150096.1; NC_014209.1.
DR   EnsemblBacteria; ADH60573; ADH60573; Tmath_0836.
DR   KEGG; tmt:Tmath_0836; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEHAYFI; -.
DR   BioCyc; TMAT583358:GHOX-814-MONOMER; -.
DR   Proteomes; UP000002064; 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   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:UP000002064};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       16     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    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;  23298 MW;  49B30D1D4FE9F188 CRC64;
     MDKLVAKKYN LMLRGISQRT LEEHYKLYNR YVDKTNEIRE KLKTADRSKA NASYSKYREL
     KLEETYNLDG VKLHELYFEN LGGPGGTPDD IIASMITLDF GSFENWKQDF IACGMASRGW
     TVLCFDPIDL KLHNYLQDLH NHGIVSRSVP LLVLDTYEHA YFIDYGTDKK SYINAFMDNI
     KWEEVNRRVT SWIYMHPF
//
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