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Database: UniProt
Entry: B3A0T8_STRDY
LinkDB: B3A0T8_STRDY
Original site: B3A0T8_STRDY 
ID   B3A0T8_STRDY            Unreviewed;       139 AA.
AC   B3A0T8;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   03-MAY-2023, entry version 36.
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:BAG48507.1};
OS   Streptococcus dysgalactiae subsp. dysgalactiae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=99822 {ECO:0000313|EMBL:BAG48507.1};
RN   [1] {ECO:0000313|EMBL:BAG48507.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=94377 {ECO:0000313|EMBL:BAG48507.1}, 94414
RC   {ECO:0000313|EMBL:BAG48508.1}, 94455 {ECO:0000313|EMBL:BAG48509.1},
RC   KNH07807 {ECO:0000313|EMBL:BAG48510.1}, KNH07901
RC   {ECO:0000313|EMBL:BAG48511.1}, KNH07902 {ECO:0000313|EMBL:BAG48513.1},
RC   and KNH07903 {ECO:0000313|EMBL:BAG48512.1};
RX   PubMed=19895643; DOI=10.1111/j.1574-6968.2009.01828.x;
RA   Abdelsalam M., Chen S.-C., Yoshida T.;
RT   "Phenotypic and genetic characterizations of Streptococcus dysgalactiae
RT   strains isolated from fish collected in Japan and other Asian countries.";
RL   FEMS Microbiol. Lett. 302:32-38(2009).
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; AB440299; BAG48507.1; -; Genomic_DNA.
DR   EMBL; AB440300; BAG48508.1; -; Genomic_DNA.
DR   EMBL; AB440301; BAG48509.1; -; Genomic_DNA.
DR   EMBL; AB440302; BAG48510.1; -; Genomic_DNA.
DR   EMBL; AB440303; BAG48511.1; -; Genomic_DNA.
DR   EMBL; AB440304; BAG48512.1; -; Genomic_DNA.
DR   EMBL; AB440305; BAG48513.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3A0T8; -.
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..66
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          75..139
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   NON_TER         139
FT                   /evidence="ECO:0000313|EMBL:BAG48507.1"
SQ   SEQUENCE   139 AA;  15055 MW;  A5A45B7E317521FD CRC64;
     MTLHHDKHHA TYVANANAAL EKHPEIGENL EELLADVTKI PEDIRQALIN NGGGHLNHAL
     FWELLSPEKQ DVTPDVAQAI DDAFGSFDAF KEQFTAAATG RFGSGWAWLV VNADGKLEIT
     STANQDTPIS DGKTPILGL
//
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