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
//