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Database: UniProt/TrEMBL
Entry: A0A0H3MX04_STRS4
LinkDB: A0A0H3MX04_STRS4
Original site: A0A0H3MX04_STRS4 
ID   A0A0H3MX04_STRS4        Unreviewed;       201 AA.
AC   A0A0H3MX04;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:CAZ56290.1};
GN   OrderedLocusNames=SSUBM407_1433 {ECO:0000313|EMBL:CAZ56290.1};
OS   Streptococcus suis (strain BM407).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=568814 {ECO:0000313|EMBL:CAZ56290.1, ECO:0000313|Proteomes:UP000009077};
RN   [1] {ECO:0000313|EMBL:CAZ56290.1, ECO:0000313|Proteomes:UP000009077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM407 {ECO:0000313|EMBL:CAZ56290.1,
RC   ECO:0000313|Proteomes:UP000009077};
RX   PubMed=19603075; DOI=10.1371/journal.pone.0006072;
RA   Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I.,
RA   Cronin A., Goodhead I., Mungall K., Quail M.A., Price C.,
RA   Rabbinowitsch E., Sharp S., Croucher N.J., Chieu T.B., Mai N.T.H.,
RA   Diep T.S., Chinh N.T., Kehoe M., Leigh J.A., Ward P.N., Dowson C.G.,
RA   Whatmore A.M., Chanter N., Iversen P., Gottschalk M., Slater J.D.,
RA   Smith H.E., Spratt B.G., Xu J., Ye C., Bentley S., Barrell B.G.,
RA   Schultsz C., Maskell D.J., Parkhill J.;
RT   "Rapid evolution of virulence and drug resistance in the emerging
RT   zoonotic pathogen Streptococcus suis.";
RL   PLoS ONE 4:E6072-E6072(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; FM252032; CAZ56290.1; -; Genomic_DNA.
DR   RefSeq; WP_012028394.1; NC_012926.1.
DR   RefSeq; YP_003029137.1; NC_012926.1.
DR   ProteinModelPortal; A0A0H3MX04; -.
DR   EnsemblBacteria; CAZ56290; CAZ56290; SSUBM407_1433.
DR   GeneID; 8155249; -.
DR   KEGG; ssb:SSUBM407_1433; -.
DR   PATRIC; fig|568814.3.peg.1471; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000009077; 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; IPR019833; Mn/Fe_SOD_BS.
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   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000009077};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CAZ56290.1}.
FT   DOMAIN        5     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   201 AA;  22479 MW;  6179B7140EB3B626 CRC64;
     MTIILPDLPY AYDALEPHID AETMTLHHDK HHATYVANAN AALEKHPEIG EDLVALLSDV
     EQIPSDIRQA LINNGGGHLN HALFWELLSP EKTEISAELA ADIDATFGSF DAFKEAFTAA
     ATTRFGSGWA FLVVNKEGKL EVISTANQDT PIMQGLKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEVINW DKVNELYKAA K
//
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