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Database: UniProt
Entry: P0C0I0
LinkDB: P0C0I0
Original site: P0C0I0 
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   05-DEC-2018, entry version 55.
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
RT   12 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
RT   prtF 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
RT   bacteria 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
CC       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
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Although found extracellularly, no signal sequence is
CC       present. An alternative secretory pathway may be used.
CC       {ECO:0000305}.
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   ProteinModelPortal; P0C0I0; -.
DR   SMR; P0C0I0; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
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; 2.40.500.20; -; 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      1       Removed. {ECO:0000269|PubMed:9532741}.
FT   CHAIN         2    201       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160100.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        81     81       Manganese. {ECO:0000250}.
FT   METAL       163    163       Manganese. {ECO:0000250}.
FT   METAL       167    167       Manganese. {ECO:0000250}.
FT   CONFLICT     40     40       D -> N (in Ref. 2, 3 and 4).
FT                                {ECO:0000305}.
FT   CONFLICT     61     61       P -> T (in Ref. 2, 3 and 4).
FT                                {ECO:0000305}.
FT   CONFLICT    194    195       SA -> LE (in Ref. 2; AAB17024).
FT                                {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
//
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