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Database: UniProt
Entry: K6XGC9_9ALTE
LinkDB: K6XGC9_9ALTE
Original site: K6XGC9_9ALTE 
ID   K6XGC9_9ALTE            Unreviewed;       178 AA.
AC   K6XGC9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   10-APR-2019, entry version 28.
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:GAC19709.1};
GN   ORFNames=GARC_2744 {ECO:0000313|EMBL:GAC19709.1};
OS   Paraglaciecola arctica BSs20135.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC19709.1, ECO:0000313|Proteomes:UP000006327};
RN   [1] {ECO:0000313|EMBL:GAC19709.1, ECO:0000313|Proteomes:UP000006327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20135 {ECO:0000313|EMBL:GAC19709.1,
RC   ECO:0000313|Proteomes:UP000006327};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals
RT   the high degree of genomic diversity and genomic characteristic for
RT   cold adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAC19709.1}.
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DR   EMBL; BAEO01000037; GAC19709.1; -; Genomic_DNA.
DR   RefSeq; WP_007620849.1; NZ_BAEO01000037.1.
DR   STRING; 493475.GARC_2744; -.
DR   EnsemblBacteria; GAC19709; GAC19709; GARC_2744.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; GCF_000314995:G1EFD-2544-MONOMER; -.
DR   Proteomes; UP000006327; 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   Complete proteome {ECO:0000313|Proteomes:UP000006327};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:GAC19709.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006327};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    178       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003900296.
FT   DOMAIN       38    176       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   178 AA;  18528 MW;  4D6ADD3F6AA7EBF5 CRC64;
     MNKYLVTAFL GSISLALSAV SFASDKGQTV TMNDLQSGQS IGSIMVSDYD DDGVVFTPNL
     SGLTPGIHGF HIHQNGDCSA AIKDGKNVLG GAAGGHFDPE NTGKHSVPWS EEGHEGDLPT
     LFVDENGKAT QAFFAPEIEL DDIKGRAIMI HAGGDNYSDS PKPLGGGGDR VACGVIHK
//
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