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   03-AUG-2022, entry version 125.
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; 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 gene
RT   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., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   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 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 Fe/Zn
RT   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 shape of
CC       a hollow sphere with an outer diameter of 60 angstroms and a large
CC       interior cavity. {ECO:0000269|PubMed:15209499}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the nickel superoxide dismutase family.
CC       {ECO:0000305}.
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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; NZ_VNID01000008.1.
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   AlphaFoldDB; P80735; -.
DR   SMR; P80735; -.
DR   STRING; 100226.SCO5254; -.
DR   GeneID; 1100695; -.
DR   KEGG; sco:SCO5254; -.
DR   PATRIC; fig|100226.15.peg.5338; -.
DR   eggNOG; ENOG502ZR3M; Bacteria.
DR   HOGENOM; CLU_141681_0_0_11; -.
DR   OMA; AHCDGPC; -.
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; Cytoplasm; Direct protein sequencing;
KW   Metal-binding; Nickel; Oxidoreductase; Reference proteome.
FT   PROPEP          1..14
FT                   /evidence="ECO:0000269|PubMed:8836134,
FT                   ECO:0000269|PubMed:8898904"
FT                   /id="PRO_0000032906"
FT   CHAIN           15..131
FT                   /note="Superoxide dismutase [Ni]"
FT                   /id="PRO_0000032907"
FT   BINDING         15
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="catalytic"
FT   BINDING         16
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="catalytic"
FT   BINDING         20
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="catalytic"
FT   CONFLICT        16
FT                   /note="C -> G (in Ref. 3; AA sequence and 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="C -> G (in Ref. 3; AA sequence and 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:3G4Z"
FT   HELIX           26..44
FT                   /evidence="ECO:0007829|PDB:1T6U"
FT   HELIX           48..75
FT                   /evidence="ECO:0007829|PDB:1T6U"
FT   HELIX           79..84
FT                   /evidence="ECO:0007829|PDB:1T6U"
FT   HELIX           88..103
FT                   /evidence="ECO:0007829|PDB:1T6U"
FT   HELIX           108..128
FT                   /evidence="ECO:0007829|PDB:1T6U"
SQ   SEQUENCE   131 AA;  14703 MW;  8DA21AFBAC0D7EF6 CRC64;
     MLSRLFAPKV TVSAHCDLPC GVYDPAQARI EAESVKAVQE KMAGNDDPHF QTRATVIKEQ
     RAELAKHHVS VLWSDYFKPP HFEKYPELHQ LVNDTLKALS AAKGSKDPAT GQKALDYIAQ
     IDKIFWETKK A