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Database: UniProt
Entry: Q9RUV2
LinkDB: Q9RUV2
Original site: Q9RUV2 
ID   SODM_DEIRA              Reviewed;         211 AA.
AC   Q9RUV2;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JAN-2019, entry version 117.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
DE   AltName: Full=MnSOD;
GN   Name=sodA; OrderedLocusNames=DR_1279;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 /
OS   LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus
RT   radiodurans R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RA   Joshi B.S., Apte S.K., Schmid R., Altendorf K.;
RL   Submitted (APR-2003) to UniProtKB.
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AE000513; AAF10851.1; -; Genomic_DNA.
DR   PIR; B75415; B75415.
DR   RefSeq; NP_295003.1; NC_001263.1.
DR   RefSeq; WP_010887922.1; NZ_CP015081.1.
DR   PDB; 1Y67; X-ray; 1.85 A; A/B/C/D=2-211.
DR   PDB; 2AW9; X-ray; 2.70 A; A/B=2-211.
DR   PDB; 2CDY; X-ray; 2.00 A; A/B/C/D=2-211.
DR   PDB; 2CE4; X-ray; 2.20 A; A/B=2-211.
DR   PDB; 3KKY; X-ray; 1.80 A; A/B=1-211.
DR   PDBsum; 1Y67; -.
DR   PDBsum; 2AW9; -.
DR   PDBsum; 2CDY; -.
DR   PDBsum; 2CE4; -.
DR   PDBsum; 3KKY; -.
DR   ProteinModelPortal; Q9RUV2; -.
DR   SMR; Q9RUV2; -.
DR   STRING; 243230.DR_1279; -.
DR   EnsemblBacteria; AAF10851; AAF10851; DR_1279.
DR   GeneID; 1797407; -.
DR   KEGG; dra:DR_1279; -.
DR   PATRIC; fig|243230.17.peg.1475; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; Q9RUV2; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BRENDA; 1.15.1.1; 1856.
DR   EvolutionaryTrace; Q9RUV2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:CACAO.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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   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   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|Ref.2}.
FT   CHAIN         2    211       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160029.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        81     81       Manganese. {ECO:0000250}.
FT   METAL       173    173       Manganese. {ECO:0000250}.
FT   METAL       177    177       Manganese. {ECO:0000250}.
FT   TURN         12     18       {ECO:0000244|PDB:3KKY}.
FT   HELIX        21     29       {ECO:0000244|PDB:3KKY}.
FT   HELIX        31     43       {ECO:0000244|PDB:3KKY}.
FT   TURN         47     50       {ECO:0000244|PDB:3KKY}.
FT   HELIX        53     56       {ECO:0000244|PDB:3KKY}.
FT   TURN         60     62       {ECO:0000244|PDB:3KKY}.
FT   HELIX        65     67       {ECO:0000244|PDB:3KKY}.
FT   HELIX        68     86       {ECO:0000244|PDB:3KKY}.
FT   HELIX       102    112       {ECO:0000244|PDB:3KKY}.
FT   HELIX       115    128       {ECO:0000244|PDB:3KKY}.
FT   STRAND      131    140       {ECO:0000244|PDB:3KKY}.
FT   STRAND      143    150       {ECO:0000244|PDB:3KKY}.
FT   HELIX       155    157       {ECO:0000244|PDB:3KKY}.
FT   HELIX       159    162       {ECO:0000244|PDB:3KKY}.
FT   STRAND      166    173       {ECO:0000244|PDB:3KKY}.
FT   HELIX       176    178       {ECO:0000244|PDB:3KKY}.
FT   HELIX       180    183       {ECO:0000244|PDB:3KKY}.
FT   HELIX       187    194       {ECO:0000244|PDB:3KKY}.
FT   HELIX       195    197       {ECO:0000244|PDB:3KKY}.
FT   HELIX       200    210       {ECO:0000244|PDB:3KKY}.
SQ   SEQUENCE   211 AA;  23478 MW;  A71F22F516A1897E CRC64;
     MAYTLPQLPY AYDALEPHID ARTMEIHHTK HHQTYVDNAN KALEGTEFAD LPVEQLIQQL
     DRVPADKKGA LRNNAGGHAN HSMFWQIMGQ GQGQNGANQP SGELLDAINS AFGSFDAFKQ
     KFEDAAKTRF GSGWAWLVVK DGKLDVVSTA NQDNPLMGEA IAGVSGTPIL GVDVWEHAYY
     LNYQNRRPDY LAAFWNVVNW DEVSKRYAAA K
//
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