SODM_STRPY
ID SODM_STRPY Reviewed; 201 AA.
AC P0C0I0; O54264; P77957; Q59941;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
GN Name=sodA; Synonyms=sod;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, AND
RP CHARACTERIZATION.
RC STRAIN=12,714 / Scarlatina;
RX PubMed=9532741; DOI=10.1111/j.1574-6968.1998.tb12914.x;
RA Gerlach D., Reichardt W., Vettermann S.;
RT "Extracellular superoxide dismutase from Streptococcus pyogenes type 12
RT strain is manganese-dependent.";
RL FEMS Microbiol. Lett. 160:217-224(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-201.
RC STRAIN=HSC5 / Serotype M6;
RX PubMed=8755901; DOI=10.1128/jb.178.15.4688-4695.1996;
RA Gibson C.M., Caparon M.G.;
RT "Insertional inactivation of Streptococcus pyogenes sod suggests that prtF
RT is regulated in response to a superoxide signal.";
RL J. Bacteriol. 178:4688-4695(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-162.
RC STRAIN=BM105;
RX PubMed=7557308; DOI=10.1016/0378-1097(95)00232-t;
RA Poyart C., Berche P., Trieu-Cuot P.;
RT "Characterization of superoxide dismutase genes from Gram-positive bacteria
RT by polymerase chain reaction using degenerate primers.";
RL FEMS Microbiol. Lett. 131:41-45(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-162.
RC STRAIN=ATCC 12344 / CIP 56.41 / DSM 20565 / JCM 5674 / NCTC 8198;
RA Poyart C., Quesne G., Coulon S., Berche P., Trieu-Cuot P.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although found extracellularly, no signal sequence is present.
CC An alternative secretory pathway may be used. {ECO:0000305}.
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DR EMBL; AJ223292; CAA11227.1; -; Genomic_DNA.
DR EMBL; U43776; AAB17024.1; -; Genomic_DNA.
DR EMBL; Z49247; CAA89214.1; -; Genomic_DNA.
DR EMBL; Z95915; CAB09368.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C0I0; -.
DR SMR; P0C0I0; -.
DR eggNOG; COG0605; Bacteria.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 1.
DR Gene3D; 3.55.40.20; -; 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 Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Manganese; Metal-binding; Oxidoreductase;
KW Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9532741"
FT CHAIN 2..201
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160100"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CONFLICT 40
FT /note="D -> N (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="P -> T (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..195
FT /note="SA -> LE (in Ref. 2; AAB17024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22606 MW; 7FA4F918F7E2A3B5 CRC64;
MAIILPELPY AYDALEPQFD AETMTLHHDK HHATYVANTD AALEKHPEIG ENLEELLADV
PKIPEDIRQA LINNGGGHLN HALFWELLSP EKQDVTPDVA QAIDDAFGSF DAFKEQFTAA
ATGRFGSGWA WLVVNKEGQL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
IKAFFEIINW KKVSALYQAA K