ID Q5KXL3_GEOKA Unreviewed; 411 AA. AC Q5KXL3; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682}; DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682}; GN OrderedLocusNames=GK2288 {ECO:0000313|EMBL:BAD76573.1}; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD76573.1, ECO:0000313|Proteomes:UP000001172}; RN [1] {ECO:0000313|EMBL:BAD76573.1, ECO:0000313|Proteomes:UP000001172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD76573.1, RC ECO:0000313|Proteomes:UP000001172}; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of thermophilic RT Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(2004). 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; BA000043; BAD76573.1; -; Genomic_DNA. DR AlphaFoldDB; Q5KXL3; -. DR STRING; 235909.GK2288; -. DR KEGG; gka:GK2288; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_1_1_9; -. DR Proteomes; UP000001172; 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:BAD76573.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001172}. FT DOMAIN 210..289 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 297..399 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT REGION 111..150 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 168..211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 132..150 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..198 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 411 AA; 47286 MW; C94C32B00BC4AFA1 CRC64; MRGASTDGAS SLLEFIAEHD GEWTEEAVRE LQRLADDVYV GALRQYVMEA AAWGRQVEQA LSARRMAEDV GLSSLLAYID GHGDEWTEEA IYELQRLVDD VYTRAVRLAD SSAADREEEA TQEQVEGESV SPELESENKE NEDGWLDTSG TAERVEDAKE PAFMAELSDS PTDAADGEPD QADNVTDGKR RWVDADDGGE PRQQVAPGRH VLPPLPYRYD ALEPHISEEI MRLHHTKHHQ SYVDGLNQAE RMMAEARRTN NFDLLKHWER EAAFHGSGHY LHTIFWYNMH PEGGGEPRGE LRAQIERDFG SFTAFRRHFT EAAKSAEGVG WALLVWAPRA HRLEILQAEK HQLMAQWDVI PLLVLDVWEH AYYLQYKNDR AAYIEHWWNV VNWRNVEERF HEAQKLRWQP F //