ID SODC_DEIRA Reviewed; 182 AA. AC Q9RU48; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Superoxide dismutase [Cu-Zn]; DE EC=1.15.1.1; DE Flags: Precursor; GN Name=sodC; OrderedLocusNames=DR_1546; OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=243230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / RC NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1; RX PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans RT R1."; RL Science 286:1571-1577(1999). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. {ECO:0000250}. 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 -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000305}; CC Note=Binds 1 copper ion per subunit. {ECO:0000305}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000305}. CC -!- CAUTION: Lacks the last conserved histidine that binds copper. CC {ECO:0000305}. 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; AE000513; AAF11107.1; -; Genomic_DNA. DR PIR; B75383; B75383. DR RefSeq; NP_295269.1; NC_001263.1. DR RefSeq; WP_010888185.1; NZ_JMLF01000003.1. DR AlphaFoldDB; Q9RU48; -. DR SMR; Q9RU48; -. DR STRING; 243230.DR_1546; -. DR PaxDb; 243230-DR_1546; -. DR EnsemblBacteria; AAF11107; AAF11107; DR_1546. DR GeneID; 69517784; -. DR KEGG; dra:DR_1546; -. DR PATRIC; fig|243230.17.peg.1748; -. DR eggNOG; COG2032; Bacteria. DR HOGENOM; CLU_056632_8_1_0; -. DR InParanoid; Q9RU48; -. DR OrthoDB; 9792957at2; -. DR Proteomes; UP000002524; Chromosome I. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central. DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central. DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central. 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 Antioxidant; Cell membrane; Copper; Disulfide bond; Lipoprotein; Membrane; KW Metal-binding; Oxidoreductase; Palmitate; Reference proteome; Signal; Zinc. FT SIGNAL 1..19 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CHAIN 20..182 FT /note="Superoxide dismutase [Cu-Zn]" FT /id="PRO_0000032841" FT REGION 91..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 69 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 71 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT LIPID 20 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT LIPID 20 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT DISULFID 76..175 FT /evidence="ECO:0000250" SQ SEQUENCE 182 AA; 18787 MW; 96749572F393CA1A CRC64; MFRTLTVVPL LALGLSLSAC ADLGQPTVRA DLLDQTGKVT GTATFSPSPI GTRVSIEVSG LKAGPHGLHI HENPNCNPGP DAQGQTIPFG AAGGHFDPGA SHNHDGPHAR NDQGHGGDLP MITVGEDGKG RLNFDTNRLK MTGPTGVLGR SIVIHADADD YQTNPAGNSG GRERCGVFQA IN //