ID U5UJF4_STRSU Unreviewed; 201 AA.
AC U5UJF4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 28-MAR-2018, entry version 25.
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:AGZ23630.1};
GN ORFNames=T15_1541 {ECO:0000313|EMBL:AGZ23630.1};
OS Streptococcus suis T15.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1340847 {ECO:0000313|EMBL:AGZ23630.1, ECO:0000313|Proteomes:UP000017744};
RN [1] {ECO:0000313|EMBL:AGZ23630.1, ECO:0000313|Proteomes:UP000017744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T15 {ECO:0000313|EMBL:AGZ23630.1,
RC ECO:0000313|Proteomes:UP000017744};
RA Wei Z.;
RT "Completed genome of Streptococcus suis T15.";
RL Submitted (JUN-2013) 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; CP006246; AGZ23630.1; -; Genomic_DNA.
DR RefSeq; WP_023370925.1; NC_022665.1.
DR EnsemblBacteria; AGZ23630; AGZ23630; T15_1541.
DR KEGG; ssui:T15_1541; -.
DR PATRIC; fig|1340847.3.peg.1504; -.
DR KO; K04564; -.
DR Proteomes; UP000017744; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 2.40.500.20; -; 1.
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:UP000017744};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
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; 22464 MW; 66BCFC5B385D6831 CRC64;
MAIILPDLPY AYDALEPHID AETMTLHHDK HHATYVANAN AALEKHPEIG EDLEALLSNV
DQIPSDIRQA LINNGGGHLN HALFWELLSP EKTEISAELA ADIDATFGSF DAFKEAFTAA
ATTRFGSGWA FLVVNKEGKL EVISTANQDT PIMQGLKPIL ALDVWEHAYY LNYRNVRPNY
IKAFFEVINW DKVNELYKAA K
//
