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Database: UniProt/SWISS-PROT
Entry: SODN_STRCO
LinkDB: SODN_STRCO
Original site: SODN_STRCO 
ID   SODN_STRCO              Reviewed;         131 AA.
AC   P80735; O51921;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   05-DEC-2018, entry version 113.
DE   RecName: Full=Superoxide dismutase [Ni];
DE            EC=1.15.1.1;
DE   AltName: Full=NiSOD;
DE   AltName: Full=Nickel-containing superoxide dismutase;
DE   Flags: Precursor;
GN   Name=sodN; Synonyms=sod1; OrderedLocusNames=SCO5254;
GN   ORFNames=2SC7G11.16c;
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, and
RC   ATCC BAA-471 / A3(2) / M145;
RX   PubMed=9466266; DOI=10.1046/j.1365-2958.1998.00674.x;
RA   Kim E.-J., Chung H.-J., Suh B., Hah Y.C., Roe J.-H.;
RT   "Transcriptional and post-transcriptional regulation by nickel of sodN
RT   gene encoding nickel-containing superoxide dismutase from Streptomyces
RT   coelicolor Muller.";
RL   Mol. Microbiol. 27:187-195(1998).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 15-28.
RC   STRAIN=ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020;
RX   PubMed=8836134; DOI=10.1042/bj3180889;
RA   Youn H.-D., Kim E.-J., Roe J.-H., Hah Y.C., Kang S.-O.;
RT   "A novel nickel-containing superoxide dismutase from Streptomyces
RT   spp.";
RL   Biochem. J. 318:889-896(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 15-28.
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).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 15-131 IN COMPLEX WITH NICKEL
RP   IONS, AND SUBUNIT.
RX   PubMed=15209499; DOI=10.1021/bi0496081;
RA   Barondeau D.P., Kassmann C.J., Bruns C.K., Tainer J.A., Getzoff E.D.;
RT   "Nickel superoxide dismutase structure and mechanism.";
RL   Biochemistry 43:8038-8047(2004).
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=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC   -!- SUBUNIT: Homohexamer. The hexameric protein has a roughly the
CC       shape of a hollow sphere with an outer diameter of 60 angstroms
CC       and a large interior cavity. {ECO:0000269|PubMed:15209499}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the nickel superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; AF012193; AAC38082.1; -; Genomic_DNA.
DR   EMBL; AF104994; AAF25537.1; -; Genomic_DNA.
DR   EMBL; AL939123; CAC05965.1; -; Genomic_DNA.
DR   RefSeq; NP_629400.1; NC_003888.3.
DR   RefSeq; WP_003973716.1; NC_003888.3.
DR   PDB; 1T6I; X-ray; 2.81 A; A/B/C=15-131.
DR   PDB; 1T6Q; X-ray; 2.05 A; A/B/C=15-131.
DR   PDB; 1T6U; X-ray; 1.30 A; A/B/C/D/E/F/G/H/I/J/K/L=15-131.
DR   PDB; 3G4X; X-ray; 2.01 A; A/B/C=15-131.
DR   PDB; 3G4Z; X-ray; 1.87 A; A/B/C=15-131.
DR   PDB; 3G50; X-ray; 1.90 A; A/B/C=15-131.
DR   PDB; 4NCQ; X-ray; 2.08 A; A/B/C=15-131.
DR   PDBsum; 1T6I; -.
DR   PDBsum; 1T6Q; -.
DR   PDBsum; 1T6U; -.
DR   PDBsum; 3G4X; -.
DR   PDBsum; 3G4Z; -.
DR   PDBsum; 3G50; -.
DR   PDBsum; 4NCQ; -.
DR   ProteinModelPortal; P80735; -.
DR   SMR; P80735; -.
DR   STRING; 100226.SCO5254; -.
DR   PRIDE; P80735; -.
DR   EnsemblBacteria; CAC05965; CAC05965; CAC05965.
DR   GeneID; 1100695; -.
DR   KEGG; sco:SCO5254; -.
DR   PATRIC; fig|100226.15.peg.5338; -.
DR   eggNOG; ENOG4108VEQ; Bacteria.
DR   eggNOG; ENOG4111IW1; LUCA.
DR   HOGENOM; HOG000020289; -.
DR   KO; K00518; -.
DR   OMA; WTDYFKP; -.
DR   OrthoDB; POG091H0C3T; -.
DR   EvolutionaryTrace; P80735; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.120.400; -; 1.
DR   InterPro; IPR036502; NiSOD_sf.
DR   InterPro; IPR014123; Superoxide_dismutase_Ni-type.
DR   Pfam; PF09055; Sod_Ni; 1.
DR   SUPFAM; SSF109770; SSF109770; 1.
DR   TIGRFAMs; TIGR02753; sodN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antioxidant; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; Nickel; Oxidoreductase;
KW   Reference proteome.
FT   PROPEP        1     14       {ECO:0000269|PubMed:8836134,
FT                                ECO:0000269|PubMed:8898904}.
FT                                /FTId=PRO_0000032906.
FT   CHAIN        15    131       Superoxide dismutase [Ni].
FT                                /FTId=PRO_0000032907.
FT   METAL        15     15       Nickel; catalytic.
FT   METAL        16     16       Nickel; catalytic.
FT   METAL        20     20       Nickel; catalytic.
FT   CONFLICT     16     16       C -> G (in Ref. 3; AA sequence and 4; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT     20     20       C -> G (in Ref. 3; AA sequence and 4; AA
FT                                sequence). {ECO:0000305}.
FT   STRAND       17     19       {ECO:0000244|PDB:3G4Z}.
FT   HELIX        26     44       {ECO:0000244|PDB:1T6U}.
FT   HELIX        48     75       {ECO:0000244|PDB:1T6U}.
FT   HELIX        79     84       {ECO:0000244|PDB:1T6U}.
FT   HELIX        88    103       {ECO:0000244|PDB:1T6U}.
FT   HELIX       108    128       {ECO:0000244|PDB:1T6U}.
SQ   SEQUENCE   131 AA;  14703 MW;  8DA21AFBAC0D7EF6 CRC64;
     MLSRLFAPKV TVSAHCDLPC GVYDPAQARI EAESVKAVQE KMAGNDDPHF QTRATVIKEQ
     RAELAKHHVS VLWSDYFKPP HFEKYPELHQ LVNDTLKALS AAKGSKDPAT GQKALDYIAQ
     IDKIFWETKK A
//
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