ID G4NQ28_BACS4 Unreviewed; 281 AA. AC G4NQ28; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAR-2024, entry version 50. DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682}; DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682}; GN OrderedLocusNames=GYO_2335 {ECO:0000313|EMBL:AEP86956.1}; OS Bacillus spizizenii (strain DSM 15029 / JCM 12233 / NBRC 101239 / NRRL OS B-23049 / TU-B-10) (Bacillus subtilis subsp. spizizenii). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1052585 {ECO:0000313|EMBL:AEP86956.1, ECO:0000313|Proteomes:UP000002651}; RN [1] {ECO:0000313|EMBL:AEP86956.1, ECO:0000313|Proteomes:UP000002651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15029 / JCM 12233 / NBRC 101239 / NRRL B-23049 / TU-B-10 RC {ECO:0000313|Proteomes:UP000002651}; RX PubMed=22493193; DOI=10.1128/JB.05675-11; RA Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A., RA Daugherty S., Losick R., Kolter R., Ravel J.; RT "Whole-genome sequences of Bacillus subtilis and close relatives."; RL J. Bacteriol. 194:2378-2379(2012). CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00008714}. 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; CP002905; AEP86956.1; -; Genomic_DNA. DR RefSeq; WP_014114085.1; NC_016047.1. DR AlphaFoldDB; G4NQ28; -. DR STRING; 1052585.GYO_2335; -. DR KEGG; bst:GYO_2335; -. DR HOGENOM; CLU_031625_1_0_9; -. DR Proteomes; UP000002651; 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; PTHR11404; SUPEROXIDE DISMUTASE 2; 1. DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:AEP86956.1}. FT DOMAIN 79..159 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 167..269 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" SQ SEQUENCE 281 AA; 33553 MW; 99CF17A0CA606885 CRC64; MKRESYQTEM FNWCEALKDQ IQKRGQLEQF EDQFDKMIEA LEDDQTTEED WYKQAAALYR DITESEDTSE RRAYVPIGKH VLPKLPYKYS ALEPYISRDI MVLHHTKHHQ SYVDGLNKAE TELKKARASK NYDLITHWER ELAFHGAGHY LHTIFWFSMH PNGKRRPTGA LFQMIDISFG SYSAFKEHFT QAAKKVEGVG WAILVWAPRS GRLEILTAEK HQLFSQWDVI PLLPLDVWEH AYYLQYKNDR ASYVDHWWNV VDWREAEKRF EQAKEVVWKL Y //