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Database: UniProt/TrEMBL
Entry: K4QCX0_STREQ
LinkDB: K4QCX0_STREQ
Original site: K4QCX0_STREQ 
ID   K4QCX0_STREQ            Unreviewed;       201 AA.
AC   K4QCX0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   25-OCT-2017, entry version 26.
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:CCI62983.1};
GN   ORFNames=SDSE_1489 {ECO:0000313|EMBL:CCI62983.1};
OS   Streptococcus dysgalactiae subsp. equisimilis AC-2713.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=759913 {ECO:0000313|EMBL:CCI62983.1, ECO:0000313|Proteomes:UP000009215};
RN   [1] {ECO:0000313|EMBL:CCI62983.1, ECO:0000313|Proteomes:UP000009215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC-2713 {ECO:0000313|EMBL:CCI62983.1,
RC   ECO:0000313|Proteomes:UP000009215};
RA   Luetticken R., Bruellhoff K., Van der Linden M.,
RA   Peltroche-Llacsahuanga H., Blom J., Weber-Lehmann J., Ferretti J.J.,
RA   McShan W.M.;
RT   "Complete genome sequence of a Streptococcus dysgalactiae subsp.
RT   equisimilis strain possessing Lancefield's group A antigen.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; HE858529; CCI62983.1; -; Genomic_DNA.
DR   RefSeq; WP_015057806.1; NC_019042.1.
DR   EnsemblBacteria; CCI62983; CCI62983; SDSE_1489.
DR   GeneID; 13902249; -.
DR   KEGG; sdc:SDSE_1489; -.
DR   PATRIC; fig|759913.3.peg.1401; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000009215; 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:UP000009215};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CCI62983.1}.
FT   DOMAIN        5     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    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;  22646 MW;  AF0E71A0B6AC4215 CRC64;
     MAIILPELPY AYDALEPHFD AETMTLHHDK HHATYVANAN AALEKHPEIG ENLEELLADV
     TKIPEDIRQA LINNGGGHLN HALFWELLSP EKQDVTPDVA QAIDDAFGSF DAFKEQFTAA
     ATGRFGSGWA WLVVNKEGQL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEIINW KKVSELYQAA K
//
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