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Database: UniProt
Entry: A0A017HB68_9RHOB
LinkDB: A0A017HB68_9RHOB
Original site: A0A017HB68_9RHOB 
ID   A0A017HB68_9RHOB        Unreviewed;       260 AA.
AC   A0A017HB68;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=Rumeso_05007 {ECO:0000313|EMBL:EYD71606.1};
OS   Rubellimicrobium mesophilum DSM 19309.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD71606.1, ECO:0000313|Proteomes:UP000019666};
RN   [1] {ECO:0000313|EMBL:EYD71606.1, ECO:0000313|Proteomes:UP000019666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD71606.1,
RC   ECO:0000313|Proteomes:UP000019666};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (FEB-2013) 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}.
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:EYD71606.1}.
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DR   EMBL; AOSK01000136; EYD71606.1; -; Genomic_DNA.
DR   RefSeq; WP_051521637.1; NZ_KK088637.1.
DR   EnsemblBacteria; EYD71606; EYD71606; Rumeso_05007.
DR   OrthoDB; 2015673at2; -.
DR   Proteomes; UP000019666; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019666};
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:UP000019666};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    260       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001495755.
FT   DOMAIN       86    216       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
FT   COILED       43     63       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   260 AA;  26375 MW;  7AA032D2256DAA24 CRC64;
     MTRTPILALA LAALAAPAMA QENQPATESQ ETRPTNQTTQ FTSEGLQEQN RQEVEQAAET
     QSQPENAMGE GEWSQGGTGA LIAADGTQLG NVSIAATASG YALVTINAEG IPEGVHGVHV
     HQVGDCSGAG FESAGEHISG NDEHGVMTDT GPHPGDLPNI TVAKDGVVAI DAFAPALTMD
     MVFDEDGSAV IIHADADDYT TQPGGNSGDR IACAAIQAAP GTEDDATVDS DEAQQQAPAD
     APANGETTQP AEGETDSNGG
//
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