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Database: UniProt/TrEMBL
Entry: M1RI13_9AQUI
LinkDB: M1RI13_9AQUI
Original site: M1RI13_9AQUI 
ID   M1RI13_9AQUI            Unreviewed;       207 AA.
AC   M1RI13;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   25-OCT-2017, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HydHO_0075 {ECO:0000313|EMBL:AGG14414.1};
OS   Hydrogenobaculum sp. HO.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum.
OX   NCBI_TaxID=547144 {ECO:0000313|EMBL:AGG14414.1, ECO:0000313|Proteomes:UP000011725};
RN   [1] {ECO:0000313|EMBL:AGG14414.1, ECO:0000313|Proteomes:UP000011725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO {ECO:0000313|EMBL:AGG14414.1};
RX   PubMed=23435891; DOI=10.1128/AEM.03591-12;
RA   Romano C., D'Imperio S., Woyke T., Mavromatis K., Lasken R.,
RA   Shock E.L., McDermott T.R.;
RT   "Comparative Genomic Analysis of Phylogenetically Closely Related
RT   Hydrogenobaculum sp. Isolates from Yellowstone National Park.";
RL   Appl. Environ. Microbiol. 79:2932-2943(2013).
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; CP004347; AGG14414.1; -; Genomic_DNA.
DR   RefSeq; WP_015418723.1; NC_020411.1.
DR   EnsemblBacteria; AGG14414; AGG14414; HydHO_0075.
DR   KEGG; hho:HydHO_0075; -.
DR   PATRIC; fig|547144.3.peg.77; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; HSP547144:G137M-78-MONOMER; -.
DR   Proteomes; UP000011725; 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:UP000011725};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
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;  23774 MW;  0DE8B70E172D0D87 CRC64;
     MKLEPKNHLK PSNLNGISNE QIEPHFEAHY KGYVAKFNEI QDKLADLNFS DRSKANQNYS
     EYRELKVEET FNYMGTVLHE LYFGHLTPKG APSEALKKKV EEDFGSWDNC VTELKAAGIA
     FRGWAILGLD IFSGKLMVNG LDAHNVYNLT GLIPLIVLDT YEHAYYVDQK NKRPPYIDAF
     LNSLNWDVIN ERFEKAIKAY ETLKGFC
//
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