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Database: UniProt
Entry: E8RTA0_ASTEC
LinkDB: E8RTA0_ASTEC
Original site: E8RTA0_ASTEC 
ID   E8RTA0_ASTEC            Unreviewed;       172 AA.
AC   E8RTA0;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   16-JAN-2019, entry version 46.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=Astex_3085 {ECO:0000313|EMBL:ADU14721.1};
OS   Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / VKM B-1370 /
OS   CB 48).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU14721.1, ECO:0000313|Proteomes:UP000001492};
RN   [1] {ECO:0000313|Proteomes:UP000001492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48
RC   {ECO:0000313|Proteomes:UP000001492};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brun Y.V., Woyke T.;
RT   "Complete sequence of chromosome 2 of Asticcacaulis excentricus CB
RT   48.";
RL   Submitted (DEC-2010) 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; CP002396; ADU14721.1; -; Genomic_DNA.
DR   RefSeq; WP_013480542.1; NC_014817.1.
DR   ProteinModelPortal; E8RTA0; -.
DR   STRING; 573065.Astex_3085; -.
DR   EnsemblBacteria; ADU14721; ADU14721; Astex_3085.
DR   KEGG; aex:Astex_3085; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263448; -.
DR   KO; K04565; -.
DR   OMA; FHAVANC; -.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; AEXC573065:G1GPE-3090-MONOMER; -.
DR   Proteomes; UP000001492; Chromosome 2.
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:UP000001492};
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:UP000001492};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    172       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003230792.
FT   DOMAIN       30    171       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   172 AA;  17227 MW;  A1CA6DCCC8ABBFCE CRC64;
     MRTFAFAAAL IVAATPVFAA PATSDLIGND GKTIGTVTVT PAPKGVILRI EATGLSEGWH
     GVHFHAKGDC GDTAKFQNSG GHVHDASHGA LVHGLLNPAA NDDGDLTNIY AGKDGVAKAE
     IFSSLVSYAP TPGKSALNDA DGAAVVVHAS PDDYSSQPIG GAGARVACAV VK
//
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