ID A0A5N4WJB4_9GAMM Unreviewed; 182 AA. AC A0A5N4WJB4; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 12-AUG-2020, entry version 4. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393}; DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393}; GN ORFNames=F4W09_06620 {ECO:0000313|EMBL:KAB1856656.1}; OS Acinetobacter tandoii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=202954 {ECO:0000313|EMBL:KAB1856656.1, ECO:0000313|Proteomes:UP000325788}; RN [1] {ECO:0000313|EMBL:KAB1856656.1, ECO:0000313|Proteomes:UP000325788} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W4-4-4 {ECO:0000313|EMBL:KAB1856656.1, RC ECO:0000313|Proteomes:UP000325788}; RA Wee S.K., Yan B., Mustaffa S.B., Yap E.P.H.; RT "Draft genome sequence of Acinetobacter tandoii W4-4-4 isolated from RT environmental water sample."; RL Submitted (SEP-2019) 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:RU000393}. 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|RuleBase:RU000393}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000393}; CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU000393}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393}; CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAB1856656.1}. 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; VXLD01000003; KAB1856656.1; -; Genomic_DNA. DR Proteomes; UP000325788; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; -; 1. DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR018152; SOD_Cu/Zn_BS. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003; PTHR10003; 1. DR Pfam; PF00080; Sod_Cu; 1. DR SUPFAM; SSF49329; SSF49329; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000393}; KW Metal-binding {ECO:0000256|RuleBase:RU000393}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000393}; KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU000393}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..182 FT /note="Superoxide dismutase [Cu-Zn]" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5024289430" FT DOMAIN 47..182 FT /note="Sod_Cu" FT /evidence="ECO:0000259|Pfam:PF00080" SQ SEQUENCE 182 AA; 18701 MW; 836FB0C59635101A CRC64; MRTSYFNTGI LTLCTALLIA GCSTTPTQST SNVRTVQINS VSAQGIGASV GTVTLQDSPV GLIIQTQLTN LPAGPHGFHI HEKGSCEPAE KDGKMVAALA AGGHYNPTQV AHHGTPMTGH MGDLPVLHVN SAGQSQLKLI APRLKLADVQ GHALMIHAGG DNYADQPKPL GGGGERIACG VI //