ID A0A0E1EM98_STRAG Unreviewed; 202 AA.
AC A0A0E1EM98;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 62.
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};
GN Name=sodA {ECO:0000313|EMBL:AKI95214.1};
GN ORFNames=C4618_06785 {ECO:0000313|EMBL:RDY81570.1}, C6N07_04375
GN {ECO:0000313|EMBL:TEB64475.1}, D5F95_07605
GN {ECO:0000313|EMBL:RRA59356.1}, RDF_0799 {ECO:0000313|EMBL:AKI95214.1};
OS Streptococcus agalactiae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1311 {ECO:0000313|EMBL:RRA59356.1, ECO:0000313|Proteomes:UP000272566};
RN [1] {ECO:0000313|EMBL:AKI95214.1, ECO:0000313|Proteomes:UP000035305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS1 {ECO:0000313|EMBL:AKI95214.1,
RC ECO:0000313|Proteomes:UP000035305};
RX PubMed=25941374; DOI=10.1073/pnas.1504725112;
RA Flores A.R., Galloway-Pena J., Sahasrabhojane P., Saldana M., Yao H.,
RA Su X., Ajami N.J., Holder M.E., Petrosino J.F., Thompson E.,
RA Margarit Y Ros I., Rosini R., Grandi G., Horstmann N., Teatero S.,
RA McGeer A., Fittipaldi N., Rappuoli R., Baker C.J., Shelburne S.A.;
RT "Sequence type 1 group B Streptococcus, an emerging cause of invasive
RT disease in adults, evolves by small genetic changes.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:6431-6436(2015).
RN [2] {ECO:0000313|EMBL:RDY81570.1, ECO:0000313|Proteomes:UP000256718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLGBS17 {ECO:0000313|EMBL:RDY81570.1,
RC ECO:0000313|Proteomes:UP000256718};
RX PubMed=30087323; DOI=.1038/s41426-018-0138-6;
RA Alhhazmi A., Tyrrell G.J.;
RT "Phenotypic and molecular analysis of nontypeable Group B streptococci:
RT identification of cps2a and hybrid cps2a/cps5 Group B streptococcal capsule
RT gene clusters.";
RL Emerg. Microbes Infect. 7:137-137(2018).
RN [3] {ECO:0000313|EMBL:TEB64475.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SA22AQUAVET {ECO:0000313|EMBL:TEB64475.1};
RA Leal C.A., Queiroz G.A., Pereira F.L., Tavares G.C., Dorella F.A.,
RA Figueiredo H.C.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:RRA59356.1, ECO:0000313|Proteomes:UP000272566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF4680 {ECO:0000313|EMBL:RRA59356.1,
RC ECO:0000313|Proteomes:UP000272566};
RA Rothen J.;
RT "Subspecies typing of Streptococcus agalactiae based on ribosomal subunit
RT protein mass variation by MALDI-TOF MS.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:TEB64475.1, ECO:0000313|Proteomes:UP000298531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA22AQUAVET {ECO:0000313|EMBL:TEB64475.1,
RC ECO:0000313|Proteomes:UP000298531};
RX PubMed=30882311;
RA Leal C.A.G., Queiroz G.A., Pereira F.L., Tavares G.C., Figueiredo H.C.P.;
RT "Streptococcus agalactiae Sequence Type 283 in Farmed Fish, Brazil.";
RL Emerg. Infect. Dis. 25:776-779(2019).
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; CP010867; AKI95214.1; -; Genomic_DNA.
DR EMBL; QHGZ01000154; RDY81570.1; -; Genomic_DNA.
DR EMBL; QYTS01000045; RRA59356.1; -; Genomic_DNA.
DR EMBL; PVLL01000016; TEB64475.1; -; Genomic_DNA.
DR RefSeq; WP_000974719.1; NZ_WNJJ01000001.1.
DR KEGG; sage:EN72_04680; -.
DR PATRIC; fig|1311.133.peg.860; -.
DR OMA; DSLINWD; -.
DR Proteomes; UP000035305; Chromosome.
DR Proteomes; UP000256718; Unassembled WGS sequence.
DR Proteomes; UP000272566; Unassembled WGS sequence.
DR Proteomes; UP000298531; Unassembled WGS sequence.
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; IPR019833; Mn/Fe_SOD_BS.
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 PIRSF; PIRSF000349; SODismutase; 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.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}.
FT DOMAIN 5..89
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 97..195
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 202 AA; 22621 MW; BA9A6878BB6F2E83 CRC64;
MAIILPDLPY AYDALEPHID AETMTLHHDK HHATYVANAN AALEKHPEIG EDLEALLADV
SQIPEDIRQA VINNGGGHLN HALFWELMSP EETQISQELS EDINATFGSF EDFKAAFTAA
ATGRFGSGWA WLVVNAEGKL EVLSTANQDT PIMEGKKPIL GLDVWEHAYY LNYRNVRPNY
IKAFFEIINW NKVNELYQAA KA
//
