ID   SODN_STRSO              Reviewed;         131 AA.
AC   P80734; Q9Z368;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 91.
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;
OS   Streptomyces seoulensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=73044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMSNU-1;
RA   Kang S.-O., Yim Y.I., Youn H.-D.;
RT   "Cloning and sequencing of sodN encoding Ni-containing superoxide dismutase
RT   from Streptomyces seoulensis.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 15-28.
RC   STRAIN=IMSNU-1;
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   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-131 IN COMPLEX WITH NICKEL
RP   IONS, MUTAGENESIS OF HIS-15; TYR-23; GLU-31 AND ARG-53, AND SUBUNIT.
RX   PubMed=15173586; DOI=10.1073/pnas.0308514101;
RA   Wuerges J., Lee J.W., Yim Y.I., Yim H.S., Kang S.O., Carugo K.D.;
RT   "Crystal structure of nickel-containing superoxide dismutase reveals
RT   another type of active site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8569-8574(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 roughly the shape of a
CC       hollow sphere with an outer diameter of 72 Angstroms and a large inner
CC       cavity. {ECO:0000269|PubMed:15173586}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the nickel superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF047528; AAD17486.1; -; Genomic_DNA.
DR   EMBL; AF047461; AAD17482.1; -; Genomic_DNA.
DR   RefSeq; WP_031181160.1; NZ_JNXP01000009.1.
DR   PDB; 1Q0D; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=15-131.
DR   PDB; 1Q0F; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=15-131.
DR   PDB; 1Q0G; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L=15-131.
DR   PDB; 1Q0K; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=15-131.
DR   PDB; 1Q0M; X-ray; 1.68 A; A/B/C/D/E/F=15-131.
DR   PDBsum; 1Q0D; -.
DR   PDBsum; 1Q0F; -.
DR   PDBsum; 1Q0G; -.
DR   PDBsum; 1Q0K; -.
DR   PDBsum; 1Q0M; -.
DR   AlphaFoldDB; P80734; -.
DR   SMR; P80734; -.
DR   STRING; 73044.JNXP01000009_gene2839; -.
DR   OrthoDB; 1789560at2; -.
DR   EvolutionaryTrace; P80734; -.
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.
FT   PROPEP          1..14
FT                   /evidence="ECO:0000269|PubMed:8836134"
FT                   /id="PRO_0000032908"
FT   CHAIN           15..131
FT                   /note="Superoxide dismutase [Ni]"
FT                   /id="PRO_0000032909"
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   MUTAGEN         15
FT                   /note="H->A,C,D,K,N,Q,R,W,Y: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:15173586"
FT   MUTAGEN         23
FT                   /note="Y->A,K,Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:15173586"
FT   MUTAGEN         23
FT                   /note="Y->F,W: Slight decrease of activity."
FT                   /evidence="ECO:0000269|PubMed:15173586"
FT   MUTAGEN         31
FT                   /note="E->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:15173586"
FT   MUTAGEN         53
FT                   /note="R->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:15173586"
FT   CONFLICT        16
FT                   /note="C -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="C -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           26..44
FT                   /evidence="ECO:0007829|PDB:1Q0G"
FT   HELIX           48..74
FT                   /evidence="ECO:0007829|PDB:1Q0G"
FT   HELIX           79..84
FT                   /evidence="ECO:0007829|PDB:1Q0G"
FT   HELIX           88..103
FT                   /evidence="ECO:0007829|PDB:1Q0G"
FT   HELIX           108..130
FT                   /evidence="ECO:0007829|PDB:1Q0G"
SQ   SEQUENCE   131 AA;  14717 MW;  DD5467214689478C CRC64;
     MLSRLFAPKV KVSAHCDLPC GVYDPAQARI EAESVKAIQE KMAANDDLHF QIRATVIKEQ
     RAELAKHHLD VLWSDYFKPP HFESYPELHT LVNEAVKALS AAKASTDPAT GQKALDYIAQ
     IDKIFWETKK A