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Database: UniProt/TrEMBL
Entry: B4U6J9_HYDS0
LinkDB: B4U6J9_HYDS0
Original site: B4U6J9_HYDS0 
ID   B4U6J9_HYDS0            Unreviewed;       207 AA.
AC   B4U6J9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=HY04AAS1_0075 {ECO:0000313|EMBL:ACG56767.1};
OS   Hydrogenobaculum sp. (strain Y04AAS1).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum.
OX   NCBI_TaxID=380749 {ECO:0000313|EMBL:ACG56767.1, ECO:0000313|Proteomes:UP000001872};
RN   [1] {ECO:0000313|Proteomes:UP000001872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y04AAS1 {ECO:0000313|Proteomes:UP000001872};
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; CP001130; ACG56767.1; -; Genomic_DNA.
DR   RefSeq; WP_012513124.1; NC_011126.1.
DR   ProteinModelPortal; B4U6J9; -.
DR   STRING; 380749.HY04AAS1_0075; -.
DR   EnsemblBacteria; ACG56767; ACG56767; HY04AAS1_0075.
DR   KEGG; hya:HY04AAS1_0075; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; HSP380749:GH30-79-MONOMER; -.
DR   Proteomes; UP000001872; 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   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:UP000001872};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACG56767.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001872}.
FT   DOMAIN       17     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       92    192       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        25     25       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       159    159       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   207 AA;  23789 MW;  805B57605C0D35DF CRC64;
     MKLEPKNHLK PSSLNGISNE QIEPHFEAHY KGYVAKFNEI QDKLADLNFS DRAKANQNYS
     EYRELKVEET FNYMGTVLHE LYFGHLTPKG TPSEALKKKV EEDFGSWDNC VTELKAAGIA
     FRGWAILGLD IFSGKLMING LDAHNLYNLT GLIPLIVLDT YEHAYYVDQK NKRPPYIDAF
     LNSLNWDVIN ERFEKAIKAY ETLKGFC
//
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