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Database: UniProt/TrEMBL
Entry: F6FZ89_RALS8
LinkDB: F6FZ89_RALS8
Original site: F6FZ89_RALS8 
ID   F6FZ89_RALS8            Unreviewed;       178 AA.
AC   F6FZ89;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC {ECO:0000313|EMBL:AEG68380.1};
GN   OrderedLocusNames=RSPO_c01079 {ECO:0000313|EMBL:AEG68380.1};
OS   Ralstonia solanacearum (strain Po82).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=1031711 {ECO:0000313|EMBL:AEG68380.1, ECO:0000313|Proteomes:UP000007953};
RN   [1] {ECO:0000313|EMBL:AEG68380.1, ECO:0000313|Proteomes:UP000007953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Po82 {ECO:0000313|EMBL:AEG68380.1,
RC   ECO:0000313|Proteomes:UP000007953};
RX   PubMed=21685279; DOI=10.1128/JB.05384-11;
RA   Xu J., Zheng H.J., Liu L., Pan Z.C., Prior P., Tang B., Xu J.S., Zhang H.,
RA   Tian Q., Zhang L.Q., Feng J.;
RT   "Complete genome sequence of the plant pathogen Ralstonia solanacearum
RT   strain Po82.";
RL   J. Bacteriol. 193:4261-4262(2011).
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}.
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DR   EMBL; CP002819; AEG68380.1; -; Genomic_DNA.
DR   RefSeq; WP_003273050.1; NC_017574.1.
DR   AlphaFoldDB; F6FZ89; -.
DR   KEGG; rsn:RSPO_c01079; -.
DR   PATRIC; fig|1031711.3.peg.1058; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_8_2_4; -.
DR   OMA; AQRGFHI; -.
DR   Proteomes; UP000007953; 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; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..178
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003334377"
FT   DOMAIN          44..175
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          84..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   178 AA;  17449 MW;  87AD6CA002526D1A CRC64;
     MKQLVIGLAA IGLMAGCASN AGTGAPAASA SASATLAPKS GSNVQGTIKL LQQGDNRVAM
     AVDIAGLPPN GMFGFHVHEK GDCSAPDGMS AGGHFNPTGQ PHGDPRSGPH HAGDIPMLQS
     DANGKAAGSI VLNGVTLAPG PTSLVGHAVI VHSGMDDYKT QPTGNSGGRI ACGVIVAN
//
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