ID SODM_STAES Reviewed; 199 AA. AC P0C0Q6; P0C0Q5; Q93CF4; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Superoxide dismutase [Mn/Fe]; DE EC=1.15.1.1 {ECO:0000305|PubMed:11948161}; GN Name=sodA; OrderedLocusNames=SE_1240; OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=11948161; DOI=10.1128/jb.184.9.2465-2472.2002; RA Wright Valderas M., Gatson J.W., Wreyford N., Hart M.E.; RT "The superoxide dismutase gene sodM is unique to Staphylococcus aureus: RT absence of sodM in coagulase-negative staphylococci."; RL J. Bacteriol. 184:2465-2472(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12228 / FDA PCI 1200; RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological systems. CC Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 CC by successive reduction and oxidation of the transition metal ion at CC the active site. {ECO:0000250|UniProtKB:P80293}. 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 Evidence={ECO:0000305|PubMed:11948161}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697; CC Evidence={ECO:0000305|PubMed:11948161}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P80293}; CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000250|UniProtKB:P80293}; CC Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit. CC {ECO:0000250|UniProtKB:P80293}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11948161}. 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; AF410177; AAL09677.1; -; Genomic_DNA. DR EMBL; AE015929; AAO04839.1; -; Genomic_DNA. DR RefSeq; NP_764795.1; NC_004461.1. DR RefSeq; WP_001831217.1; NZ_WBME01000008.1. DR AlphaFoldDB; P0C0Q6; -. DR SMR; P0C0Q6; -. DR GeneID; 50018644; -. DR KEGG; sep:SE_1240; -. DR PATRIC; fig|176280.10.peg.1208; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_1_9; -. DR OrthoDB; 9803125at2; -. DR Proteomes; UP000001411; 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; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1. DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 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 1: Evidence at protein level; KW Iron; Manganese; Metal-binding; Oxidoreductase; Stress response. FT CHAIN 1..199 FT /note="Superoxide dismutase [Mn/Fe]" FT /id="PRO_0000160077" FT BINDING 27 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000250|UniProtKB:P80293" FT BINDING 27 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P80293" FT BINDING 81 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000250|UniProtKB:P80293" FT BINDING 81 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P80293" FT BINDING 161 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000250|UniProtKB:P80293" FT BINDING 161 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P80293" FT BINDING 165 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000250|UniProtKB:P80293" FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P80293" SQ SEQUENCE 199 AA; 22722 MW; E25419284F3378DD CRC64; MAFELPNLPY AYDALEPHID KQTMEIHHDK HHNTYVTKLN SAVEGTDLEA KSIEEIVANL DSVPSNIQTA VRNNGGGHLN HSLFWELLSP NSEEKGEVVD KIKEQWGSLD EFKKEFADKA AARFGSGWAW LVVNNGQLEI VTTPNQDNPI TEGKTPILGL DVWEHAYYLK YQNKRPDYIN AFWNVVNWEK VNELYNATK //