ID X5GEG1_9MYCO Unreviewed; 148 AA. AC X5GEG1; A0A088MGG3; X5GFB1; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 24-JUN-2015, entry version 9. DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414}; DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414}; DE Flags: Fragment; GN Name=sodA {ECO:0000313|EMBL:AHW98351.1}; OS Mycobacterium celeriflavum. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1249101 {ECO:0000313|EMBL:AHW98351.1}; RN [1] {ECO:0000313|EMBL:AHW98351.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AFPC-000207 {ECO:0000313|EMBL:AHW98349.1}, E498 RC {ECO:0000313|EMBL:AIN39497.1}, and FI-09258 RC {ECO:0000313|EMBL:AHW98351.1}; RX PubMed=25389151; DOI=10.1099/ijs.0.064832-0; RA Shahraki A.H., Cavusoglu C., Borroni E., Heidarieh P., Koksalan O.K., RA Cabibbe A.M., Hashemzadeh M., Mariottini A., Mostafavi E., Cittaro D., RA Feizabadi M.M., Lazarevic D., Yaghmaei F., Molinari G.L., Camaggi A., RA Tortoli E.; RT "Mycobacterium celeriflavum sp. nov., a rapidly growing RT scotochromogenic bacterium isolated from clinical specimens."; RL Int. J. Syst. Evol. Microbiol. 65:510-515(2015). 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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC {ECO:0000256|RuleBase:RU000414}. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase CC family. {ECO:0000256|RuleBase:RU004477}. 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; KJ586625; AHW98349.1; -; Genomic_DNA. DR EMBL; KJ586627; AHW98351.1; -; Genomic_DNA. DR EMBL; KM396308; AIN39497.1; -; Genomic_DNA. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. 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 PANTHER; PTHR11404; PTHR11404; 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; SSF46609; SSF46609; 1. DR SUPFAM; SSF54719; SSF54719; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|RuleBase:RU000414}. FT NON_TER 1 1 {ECO:0000313|EMBL:AHW98351.1}. FT NON_TER 148 148 {ECO:0000313|EMBL:AHW98351.1}. SQ SEQUENCE 148 AA; 16299 MW; 7DCDC6E5FD62A420 CRC64; ATYVKGLNDA IAKLEEARAN GDHAAIFLNE KNLAFHLGGH VNHTIWWKNL SPNGGDKPTG DLGAAIDDQF GSFDKFQAQF AAAANGLQGS GWAVLGYDTL GQRLLTFQLY DQQANVPLGI IPLLQVDMWE HAYYLQYKNV KADYVKAF //