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Database: UniProt
Entry: I3CI98_9GAMM
LinkDB: I3CI98_9GAMM
Original site: I3CI98_9GAMM 
ID   I3CI98_9GAMM            Unreviewed;       177 AA.
AC   I3CI98;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   10-APR-2019, entry version 29.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=BegalDRAFT_2496 {ECO:0000313|EMBL:EIJ43341.1};
OS   Beggiatoa alba B18LD.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Beggiatoa.
OX   NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ43341.1, ECO:0000313|Proteomes:UP000005744};
RN   [1] {ECO:0000313|EMBL:EIJ43341.1, ECO:0000313|Proteomes:UP000005744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B18LD {ECO:0000313|EMBL:EIJ43341.1,
RC   ECO:0000313|Proteomes:UP000005744};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K.,
RA   Teske A., Mueller J., Woyke T.;
RT   "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL   Submitted (NOV-2011) 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; JH600070; EIJ43341.1; -; Genomic_DNA.
DR   RefSeq; WP_002690435.1; NZ_JH600070.1.
DR   STRING; 395493.BegalDRAFT_2496; -.
DR   EnsemblBacteria; EIJ43341; EIJ43341; BegalDRAFT_2496.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; BALB395493:G1H31-2504-MONOMER; -.
DR   Proteomes; UP000005744; 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; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005744};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005744};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    177       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003669547.
FT   DOMAIN       39    176       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   177 AA;  18061 MW;  90A9EAA9CF6C24DA CRC64;
     MQKSLKNALL LVGLGLGSVA YADEGLSITM NLISETGIGE EVGTISATDS EYGLLLTPNL
     KNLTTGVHGF HVHEKPDCNA GEKDGKAVAG LAAGGHFDPE KTAKHMGPYD KTGHLGDLPP
     LIVGKDGTAT TPILAPRLKV ADLKGHSLMV HVGGDNFSDN PAALGGGGAR MACGVVK
//
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