ID O33606_STRAP Unreviewed; 145 AA.
AC O33606;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 03-MAY-2023, entry version 85.
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:CAB09348.1};
OS Streptococcus anginosus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1328 {ECO:0000313|EMBL:CAB09348.1};
RN [1] {ECO:0000313|EMBL:CAB09348.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CIP 102921 T {ECO:0000313|EMBL:CAB09348.1};
RX PubMed=9431917;
RA Poyart C., Quesne G., Coulon S., Berche P., Trieu-Cuot P.;
RT "Identification of streptococci to species level by sequencing the gene
RT encoding the manganese-dependent superoxide dismutase.";
RL J. Clin. Microbiol. 36:41-47(1998).
RN [2] {ECO:0000313|EMBL:AFB69375.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VMC15 {ECO:0000313|EMBL:AFB69375.1};
RX PubMed=22189124; DOI=10.1128/JCM.06438-11;
RA Kitten T., Munro C.L., Zollar N.Q., Lee S.P., Patel R.D.;
RT "Oral streptococcal bacteremia in hospitalized patients: taxonomic
RT identification and clinical characterization.";
RL J. Clin. Microbiol. 50:1039-1042(2012).
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; JN181279; AFB69375.1; -; Genomic_DNA.
DR EMBL; Z95895; CAB09348.1; -; Genomic_DNA.
DR AlphaFoldDB; O33606; -.
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..71
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 78..145
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB09348.1"
FT NON_TER 145
FT /evidence="ECO:0000313|EMBL:CAB09348.1"
SQ SEQUENCE 145 AA; 15822 MW; D1EC10AFCACEEDAF CRC64;
YIDEETMHLH HDKHHNTYVN NVNAALAKHP EIGEDLEQLL SDVETIPADI RQAVINNGGG
HLNHALFWEL MTPEKTEPSA ALAADLEATF GSFEDFKAAF TTAATSRFGS GWAWLVVNND
GKLEVTSTAN QDTPISEGKT PILGI
//
