ID SODF_NOSS1 Reviewed; 200 AA. AC Q8YSZ1; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 102. DE RecName: Full=Superoxide dismutase [Fe]; DE EC=1.15.1.1; GN Name=sodB; OrderedLocusNames=alr2938; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., RA Takazawa M., Yamada M., Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological 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 cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the iron/manganese 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; BA000019; BAB74637.1; -; Genomic_DNA. DR PIR; AC2173; AC2173. DR RefSeq; WP_010997089.1; NZ_RSCN01000003.1. DR AlphaFoldDB; Q8YSZ1; -. DR SMR; Q8YSZ1; -. DR STRING; 103690.gene:10494974; -. DR KEGG; ana:alr2938; -. DR eggNOG; COG0605; Bacteria. DR OrthoDB; 9803125at2; -. DR BRENDA; 1.15.1.1; 8113. DR Proteomes; UP000002483; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1. DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1. DR PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 1. 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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1. DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 3: Inferred from homology; KW Iron; Metal-binding; Oxidoreductase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..200 FT /note="Superoxide dismutase [Fe]" FT /id="PRO_0000262945" FT BINDING 28 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 80 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 162 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 166 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" SQ SEQUENCE 200 AA; 22384 MW; 5F7D1AC6602BB760 CRC64; MAFVQEPLPY DFNALEQYGM KGETFEYHYG KHHKAYVDNL NKLTDGTELA DKSLEEVIQI AFKDASKAGI FNNAAQVWNH TFFWNSLKPA GGGAPTGEFA AKINQDFGSF DKLKEEFSNA AATQFGSGWA WLIDDGGTLK VTKTPNAENP LAHGQKALLT LDVWEHAYYI DFRNARPAFI KNYLDNLVNW DFAAANYAKA //