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Database: UniProt/TrEMBL
Entry: C1DW98_SULAA
LinkDB: C1DW98_SULAA
Original site: C1DW98_SULAA 
ID   C1DW98_SULAA            Unreviewed;       247 AA.
AC   C1DW98;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=SULAZ_1418 {ECO:0000313|EMBL:ACN98255.1};
OS   Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium.
OX   NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN98255.1, ECO:0000313|Proteomes:UP000001369};
RN   [1] {ECO:0000313|EMBL:ACN98255.1, ECO:0000313|Proteomes:UP000001369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Az-Fu1 / DSM 15241 / OCM 825
RC   {ECO:0000313|Proteomes:UP000001369};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the
RT   Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001229; ACN98255.1; -; Genomic_DNA.
DR   ProteinModelPortal; C1DW98; -.
DR   STRING; 204536.SULAZ_1418; -.
DR   EnsemblBacteria; ACN98255; ACN98255; SULAZ_1418.
DR   KEGG; saf:SULAZ_1418; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; SAZO204536:GHRE-1414-MONOMER; -.
DR   Proteomes; UP000001369; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001369};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACN98255.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001369}.
FT   DOMAIN       64    132       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      140    240       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        72     72       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       125    125       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       207    207       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       211    211       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   247 AA;  28488 MW;  FDA3EBE40D15F068 CRC64;
     MDRREFLKLS GLSASLILTD NLLAMEILEK EEKREIKSKS GGKKMKVVKL QPKDHLKPKG
     LVGISDEQIE VHFEAHYKGY VAKYNEIQEK LASDFADRSK ANQNYSEYRA LKVEESFNYM
     GVVLHELYFE NLVAGGKGEP SPELKKMIEE YFGSVNNCIN EIKATGIACR GWATLSYDLY
     NKILVVNGFD AHNQYGFVYS VPLIVLDVYE HAYYVDQKNK RPPYIDAFFK NLNWEVVNER
     FNKAVKF
//
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