ID I0JP11_HALH3 Unreviewed; 204 AA. AC I0JP11; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAR-2024, entry version 51. DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414}; DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414}; GN Name=sodA {ECO:0000313|EMBL:CCG45881.1}; GN OrderedLocusNames=HBHAL_3535 {ECO:0000313|EMBL:CCG45881.1}; OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / OS KCTC 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus. OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG45881.1, ECO:0000313|Proteomes:UP000007397}; RN [1] {ECO:0000313|EMBL:CCG45881.1, ECO:0000313|Proteomes:UP000007397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 / RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397}; RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x; RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V., RA Oesterhelt D.; RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated RT salinities by the moderately halophilic, chloride-dependent bacterium RT Halobacillus halophilus."; RL Environ. Microbiol. 15:1619-1633(2013). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000256|RuleBase:RU000414}. 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:0000256|RuleBase:RU000414}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}. 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; HE717023; CCG45881.1; -; Genomic_DNA. DR RefSeq; WP_014643770.1; NC_017668.1. DR AlphaFoldDB; I0JP11; -. DR STRING; 866895.HBHAL_3535; -. DR KEGG; hhd:HBHAL_3535; -. DR PATRIC; fig|866895.3.peg.2555; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_1_9; -. DR Proteomes; UP000007397; 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 3: Inferred from homology; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000349-1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000414}; KW Reference proteome {ECO:0000313|Proteomes:UP000007397}. FT DOMAIN 3..92 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 99..199 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 28 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 84 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 166 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 170 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 204 AA; 22916 MW; 8FBC4A14FCFBC644 CRC64; MAKFELPELP YAYDALEPTI DKETMNIHHT KHHNTYVTKL NNALEGHADL QDKSLEELLA NNLAAVPEDI RTPVRRNGGG HANHSLFWTI MSPNGGGEPT GDLATAINDT FGSLDQFKEK FETTAKGRFG SGWAWLVVNN GSLEVIDTLN QDSPIMEGKT PILGLDVWEH AYYLNYQNRR PDYAAAFWNV VNWDEVAKRY DAAK //