ID Q9R391_STRPA Unreviewed; 122 AA.
AC Q9R391;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 03-MAY-2023, entry version 79.
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:BAA85585.1};
OS Streptococcus parasanguinis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1318 {ECO:0000313|EMBL:BAA85585.1};
RN [1] {ECO:0000313|EMBL:BAA85585.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GTC498T {ECO:0000313|EMBL:BAA85498.1}, and O-151A
RC {ECO:0000313|EMBL:BAA85585.1};
RX PubMed=10517614;
RA Kawamura Y., Whiley R.A., Shu S.E., Ezaki T., Hardie J.M.;
RT "Genetic approaches to the identification of the mitis group within the
RT genus Streptococcus.";
RL Microbiology 145:2605-2613(1999).
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; AB021550; BAA85498.1; -; Genomic_DNA.
DR EMBL; AB021637; BAA85585.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9R391; -.
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 1..56
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 63..121
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA85585.1"
FT NON_TER 122
FT /evidence="ECO:0000313|EMBL:BAA85585.1"
SQ SEQUENCE 122 AA; 13073 MW; 9A85DA8E1A9D8A7E CRC64;
QTYVNNVNAA LEKHPEIGED LESLLADVES IPADIRQAVI NNGGGHLNHA LFWELMTPEQ
TAPSAELAAA IDATFGSFED FKAAFTAAAT TRFGSGWAWL VVNKEGKLEV TSTANQDTPL
SE
//
