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Database: UniProt
Entry: B9VXX2_STRGY
LinkDB: B9VXX2_STRGY
Original site: B9VXX2_STRGY 
ID   B9VXX2_STRGY            Unreviewed;       138 AA.
AC   B9VXX2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE   Flags: Fragment;
GN   Name=sodA {ECO:0000313|EMBL:ACM69286.1};
OS   Streptococcus gallolyticus (Streptococcus bovis biotype I).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=53354 {ECO:0000313|EMBL:ACM69286.1};
RN   [1] {ECO:0000313|EMBL:ACM69286.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 13808 {ECO:0000313|EMBL:ACM69286.1};
RX   PubMed=20233397; DOI=10.1186/1471-2180-10-78;
RA   Vollmer T., Hinse D., Kleesiek K., Dreier J.;
RT   "Interactions between endocarditis-derived Streptococcus gallolyticus
RT   subsp. gallolyticus isolates and human endothelial cells.";
RL   BMC Microbiol. 10:78-78(2010).
RN   [2] {ECO:0000313|EMBL:ADI49885.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 14876 {ECO:0000313|EMBL:ADI49885.1};
RX   PubMed=21247715; DOI=10.1016/j.syapm.2010.11.010;
RA   Hinse D., Vollmer T., Erhard M., Welker M., Moore E.R., Kleesiek K.,
RA   Dreier J.;
RT   "Differentiation of species of the Streptococcus bovis/equinus-complex by
RT   MALDI-TOF Mass Spectrometry in comparison to sodA sequence analyses.";
RL   Syst. Appl. Microbiol. 34:52-57(2011).
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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; FJ617227; ACM69286.1; -; Genomic_DNA.
DR   EMBL; GU991759; ADI49885.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9VXX2; -.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
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   PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN          2..69
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          75..137
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACM69286.1"
FT   NON_TER         138
FT                   /evidence="ECO:0000313|EMBL:ACM69286.1"
SQ   SEQUENCE   138 AA;  14956 MW;  13A18C4A09A4B794 CRC64;
     TETMTIHHDK HHATYVANVN AALEKHPEIG EDLEALLADV DSIPADIRQA VINNGGGHLN
     HALFWELLSP EKQEPTAQVL AAIEEAFGSF DEFKAAFTQA ATTRFGSGWA WLVVNENGKL
     EVLSTANQDT PISQGKAP
//
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