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Database: UniProt
Entry: A0A1D8GL79_9CLOT
LinkDB: A0A1D8GL79_9CLOT
Original site: A0A1D8GL79_9CLOT 
ID   A0A1D8GL79_9CLOT        Unreviewed;       178 AA.
AC   A0A1D8GL79;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=Gferi_20245 {ECO:0000313|EMBL:AOT71661.1};
OS   Geosporobacter ferrireducens.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Geosporobacter.
OX   NCBI_TaxID=1424294 {ECO:0000313|EMBL:AOT71661.1, ECO:0000313|Proteomes:UP000095743};
RN   [1] {ECO:0000313|EMBL:AOT71661.1, ECO:0000313|Proteomes:UP000095743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRF9 {ECO:0000313|EMBL:AOT71661.1,
RC   ECO:0000313|Proteomes:UP000095743};
RA   Kim S.-J.;
RT   "Genomic analysis reveals versatility of anaerobic energy metabolism
RT   of Geosporobacter ferrireducens IRF9 of phylum Firmicutes.";
RL   Submitted (SEP-2016) 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.
CC       {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.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; CP017269; AOT71661.1; -; Genomic_DNA.
DR   RefSeq; WP_069979736.1; NZ_CP017269.1.
DR   EnsemblBacteria; AOT71661; AOT71661; Gferi_20245.
DR   KEGG; gfe:Gferi_20245; -.
DR   KO; K04565; -.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; GCF_001750685:G1F7O-4090-MONOMER; -.
DR   Proteomes; UP000095743; Chromosome.
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; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000095743};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       21    156       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   178 AA;  19709 MW;  20CB8D7A02216353 CRC64;
     MDNSIQCTMA VAEIRGGPLA PQIRGTVILK EVPGGTEVYV QVEGLPHYQP ARNGKDPIGP
     HGFHIHEHGT CKVSDPEEPF EAAGEHWNPT NQPHGNHAGD FPVLFSNNGI ARMSFFTNKF
     RPRDAVGKTI MIHENPDDYR SQPAGDAGRR LACGIIQCMQ PQTQIWSGYG YTNYLRPY
//
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