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Database: UniProt/SWISS-PROT
Entry: SODC1_AQUAE
LinkDB: SODC1_AQUAE
Original site: SODC1_AQUAE 
ID   SODC1_AQUAE             Reviewed;         169 AA.
AC   O67149;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   28-FEB-2018, entry version 121.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sodC1; OrderedLocusNames=aq_1050;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; AE000657; AAC07105.1; -; Genomic_DNA.
DR   PIR; B70390; B70390.
DR   RefSeq; NP_213712.1; NC_000918.1.
DR   RefSeq; WP_010880650.1; NC_000918.1.
DR   ProteinModelPortal; O67149; -.
DR   SMR; O67149; -.
DR   STRING; 224324.aq_1050; -.
DR   EnsemblBacteria; AAC07105; AAC07105; aq_1050.
DR   GeneID; 1193783; -.
DR   KEGG; aae:aq_1050; -.
DR   PATRIC; fig|224324.8.peg.813; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263448; -.
DR   InParanoid; O67149; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05EB; -.
DR   BioCyc; AAEO224324:G1G15-738-MONOMER; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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   Antioxidant; Complete proteome; Copper; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Signal; Zinc.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    169       Superoxide dismutase [Cu-Zn] 1.
FT                                /FTId=PRO_0000032818.
FT   METAL        65     65       Copper; catalytic. {ECO:0000250}.
FT   METAL        67     67       Copper; catalytic. {ECO:0000250}.
FT   METAL        83     83       Copper; catalytic. {ECO:0000250}.
FT   METAL        83     83       Zinc; structural. {ECO:0000250}.
FT   METAL        91     91       Zinc; structural. {ECO:0000250}.
FT   METAL       100    100       Zinc; structural. {ECO:0000250}.
FT   METAL       103    103       Zinc; structural. {ECO:0000250}.
FT   METAL       145    145       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     72    165       {ECO:0000250}.
SQ   SEQUENCE   169 AA;  18301 MW;  AA133160A0AF0793 CRC64;
     MFEQWDALCA VLFSFSIAQE LKTHADIVNQ KGEKIGKAEL IQTNSGVLIK LEASNLPPNA
     ELAFHIHELG KCDPPDFKSA KGHFNPFKKK HGLLNPEGPH AGDMPNIHTD DKGNVRVQVL
     NPFVTLKKGK KNSLFKEGGT ALVIHGGPDD YKSDPAGNAG KRIACGVVK
//
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