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 02-JUN-2021, entry version 23. 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}; DE Flags: Fragment; GN Name=sodA {ECO:0000313|EMBL:AHW98351.1}; OS Mycolicibacterium celeriflavum. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycolicibacterium. 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 scotochromogenic RT 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 -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological systems. CC {ECO:0000256|ARBA:ARBA00002170}. 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|ARBA:ARBA00001605, CC ECO:0000256|RuleBase:RU000414}; 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; 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:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.287.990; -; 1. DR Gene3D; 2.40.500.20; -; 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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000349-1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000414}. FT DOMAIN 1..51 FT /note="Sod_Fe_N" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 58..148 FT /note="Sod_Fe_C" FT /evidence="ECO:0000259|Pfam:PF02777" FT METAL 43 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT METAL 127 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT METAL 131 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHW98351.1" FT NON_TER 148 FT /evidence="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 //