ID A5YM81_9ACTN Unreviewed; 145 AA. AC A5YM81; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 12-AUG-2020, entry version 41. 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; OS Nocardiopsis halotolerans. OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae; OC Nocardiopsis. OX NCBI_TaxID=124252 {ECO:0000313|EMBL:ABQ96940.1}; RN [1] {ECO:0000313|EMBL:ABQ96940.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 44410 {ECO:0000313|EMBL:ABQ96940.1}; RA Yang L.-L., Zhi X.-Y., Li W.-J.; RT "Phylogenetic analysis of Nocardiopsis species based on partial 16S rRNA RT and gyrB gene sequences."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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; EF565389; ABQ96940.1; -; 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 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|RuleBase:RU000414}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000414}. FT DOMAIN 2..43 FT /note="Sod_Fe_N" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 50..145 FT /note="Sod_Fe_C" FT /evidence="ECO:0000259|Pfam:PF02777" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABQ96940.1" FT NON_TER 145 FT /evidence="ECO:0000313|EMBL:ABQ96940.1" SQ SEQUENCE 145 AA; 16113 MW; 3DEBC03B152835C2 CRC64; TALEKMAEAR ETGDFGTIPM LEKNLAFNLG GHVNHSIFWN NLSPEGGDKP EGELGAAIDD QFGSFDAFRA HFTSVATTIQ GSGWAILAWD ALGQRLIIEQ LYDQQGNTAL SSVPLLMLDM WEHAFYLQYK NVKAEYAKAF WNVVN //