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Database: UniProt
Entry: O51917
LinkDB: O51917
Original site: O51917 
ID   SODF_STRCO              Reviewed;         213 AA.
AC   O51917;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JAN-2019, entry version 122.
DE   RecName: Full=Superoxide dismutase [Fe-Zn] 1;
DE            EC=1.15.1.1;
DE   AltName: Full=FeSOD I;
DE   AltName: Full=SOD2;
GN   Name=sodF1; Synonyms=sodB, sodF; OrderedLocusNames=SCO2633;
GN   ORFNames=SC8E4A.03;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020;
RX   PubMed=9555880;
RA   Kim E.-J., Chung H.-J., Suh B., Hah Y.C., Roe J.-H.;
RT   "Expression and regulation of the sodF gene encoding iron- and zinc-
RT   containing superoxide dismutase in Streptomyces coelicolor Muller.";
RL   J. Bacteriol. 180:2014-2020(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=10231572; DOI=10.1016/S0378-1119(99)00088-8;
RA   Chung H.J., Kim E.J., Suh B., Choi J.H., Roe J.H.;
RT   "Duplicate genes for Fe-containing superoxide dismutase in
RT   Streptomyces coelicolor A3(2).";
RL   Gene 231:87-93(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020;
RX   PubMed=8898904; DOI=10.1111/j.1432-1033.1996.0178t.x;
RA   Kim F.-J., Kim H.-P., Hah Y.V., Roe J.-H.;
RT   "Differential expression of superoxide dismutases containing Ni and
RT   Fe/Zn in Streptomyces coelicolor.";
RL   Eur. J. Biochem. 241:178-185(1996).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 Fe(2+) or Zn(2+) ion per subunit.;
CC   -!- SUBUNIT: Tetramer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Inhibited by nickel.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF012087; AAC46274.1; -; Genomic_DNA.
DR   EMBL; AF099014; AAD33128.1; -; Genomic_DNA.
DR   EMBL; AL939113; CAB71808.1; -; Genomic_DNA.
DR   PIR; T42080; T42080.
DR   RefSeq; NP_626869.1; NC_003888.3.
DR   RefSeq; WP_003976168.1; NC_003888.3.
DR   ProteinModelPortal; O51917; -.
DR   SMR; O51917; -.
DR   STRING; 100226.SCO2633; -.
DR   PRIDE; O51917; -.
DR   EnsemblBacteria; CAB71808; CAB71808; CAB71808.
DR   GeneID; 1098067; -.
DR   KEGG; sco:SCO2633; -.
DR   PATRIC; fig|100226.15.peg.2680; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; O51917; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; O51917; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
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   Complete proteome; Cytoplasm; Direct protein sequencing; Iron;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:8898904}.
FT   CHAIN         2    213       Superoxide dismutase [Fe-Zn] 1.
FT                                /FTId=PRO_0000160001.
FT   METAL        28     28       {ECO:0000255}.
FT   METAL        76     76       {ECO:0000255}.
FT   METAL       165    165       {ECO:0000255}.
FT   METAL       169    169       {ECO:0000255}.
SQ   SEQUENCE   213 AA;  23527 MW;  9E2E208E1E8CF5B4 CRC64;
     MSVYTLPELP YDYSALAPVI SPEIIELHHD KHHAAYVKGA NDTLEQLAEA RDKETWGSIN
     GLEKNLAFHL SGHILHSIYW HNMTGDGGGE PLDKDGVGEL ADAIAESFGS FAGFRAQLTK
     AAATTQGSGW GVLAYEPLSG RLIVEQIYDH QGNVGQGSTP ILVFDAWEHA FYLQYKNQKV
     DFIDAMWAVV NWQDVARRYE AAKSRTNTLL LAP
//
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