ID A0A6L8PNN9_BACAN Unreviewed; 179 AA. AC A0A6L8PNN9; A0A1J9V7F5; A0A348ABG3; E9QU47; E9QU48; Q6HRL8; Q6KKY3; Q81K66; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 27-MAR-2024, entry version 15. DE SubName: Full=Superoxide dismutase, Cu-Zn {ECO:0000313|EMBL:AAT34268.1}; DE EC=1.15.1.1 {ECO:0000313|EMBL:AAT34268.1}; GN Name=sodC {ECO:0000313|EMBL:AAT34268.1}; GN OrderedLocusNames=GBAA_5139 {ECO:0000313|EMBL:AAT34268.1}; OS Bacillus anthracis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT34268.1, ECO:0000313|Proteomes:UP000000594}; RN [1] {ECO:0000313|EMBL:AAT34268.1, ECO:0000313|Proteomes:UP000000594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594}; RX PubMed=18952800; DOI=10.1128/JB.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00010457}. 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; AE017334; AAT34268.1; -; Genomic_DNA. DR RefSeq; WP_000746504.1; NZ_WXXJ01000017.1. DR AlphaFoldDB; A0A6L8PNN9; -. DR SMR; A0A6L8PNN9; -. DR GeneID; 75088079; -. DR KEGG; bar:GBAA_5139; -. DR PATRIC; fig|1392.230.peg.5063; -. DR OMA; GARYACG; -. DR OrthoDB; 9792957at2; -. DR Proteomes; UP000000594; Chromosome. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1. DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1. DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE; 1. DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1. DR Pfam; PF00080; Sod_Cu; 1. DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|ARBA:ARBA00023008}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000313|EMBL:AAT34268.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000594}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 39..169 FT /note="Superoxide dismutase copper/zinc binding" FT /evidence="ECO:0000259|Pfam:PF00080" SQ SEQUENCE 179 AA; 19052 MW; 11869BBE304D1C39 CRC64; MKKRLFFSCC LLFLMAGCDQ GKPKEIDVKL HNASGDEVGT AKVTQQTSGV KITIKGEGFA PGPHGLHVHE IGECKAPRFE SAGNHFNPDD KKHGLLNPKG AENGDLPNVI ADGSGKIKAE IDAPHITLEE GKTTIHRKDG ASIIITENAD DGMTQPTGKS GDRIACGVIV KKASDMKKK //