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Database: UniProt
Entry: W6K8D2_9PROT
LinkDB: W6K8D2_9PROT
Original site: W6K8D2_9PROT 
ID   W6K8D2_9PROT            Unreviewed;       199 AA.
AC   W6K8D2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   16-JAN-2019, entry version 18.
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:CCQ74331.1};
GN   ORFNames=MGMAQ_2468 {ECO:0000313|EMBL:CCQ74331.1};
OS   Magnetospira sp. QH-2.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospira.
OX   NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ74331.1, ECO:0000313|Proteomes:UP000032733};
RN   [1] {ECO:0000313|EMBL:CCQ74331.1, ECO:0000313|Proteomes:UP000032733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-2 {ECO:0000313|EMBL:CCQ74331.1};
RX   PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA   Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N.,
RA   Murat D., Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S.,
RA   Pradel N., Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B.,
RA   Coutinho P.M., Li Y., Xiao T., Medigue C., Barbe V., Pignol D.,
RA   Talla E., Wu L.F.;
RT   "Comparative genomic analysis provides insights into the evolution and
RT   niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL   Environ. Microbiol. 16:525-544(2014).
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:
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         Evidence={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; FO538765; CCQ74331.1; -; Genomic_DNA.
DR   RefSeq; WP_046021697.1; NZ_FO538765.1.
DR   EnsemblBacteria; CCQ74331; CCQ74331; MGMAQ_2468.
DR   KEGG; magq:MGMAQ_2468; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000032733; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000032733};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CCQ74331.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032733}.
FT   DOMAIN        3     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   199 AA;  21489 MW;  06A2F6D405B257D7 CRC64;
     MAFELPALPF AQDALEPHMC AETLDYHHGK HHNTYVVNLN NLTKDSPMAG QSLEEIISAT
     AGDAGKAGIF NNAAQVWNHT FFWNCLSANG GGAPTGDLAA KIDAAFGSLD GFKEQFTQAA
     LTQFGSGWAW LVVEGGELKI TKTANADTPI AHGQTPLLCI DVWEHAYYID HRNARPKFVE
     TFLGNLANWD FAAANLANA
//
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