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 24-JAN-2024, entry version 97. 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; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.GCA_000725795_02929; -. DR OrthoDB; 9790847at2; -. 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; Nickel-containing superoxide dismutase; 1. DR InterPro; IPR036502; NiSOD_sf. DR InterPro; IPR014123; Superoxide_dismutase_Ni-type. DR NCBIfam; TIGR02753; sodN; 1. DR Pfam; PF09055; Sod_Ni; 1. DR SUPFAM; SSF109770; Nickel-containing superoxide dismutase, NiSOD; 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 //