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Database: UniProt
Entry: P0A4J5
LinkDB: P0A4J5
Original site: P0A4J5 
ID   SODM_STRAG              Reviewed;         202 AA.
AC   P0A4J5; O33604; O54086; O54091; Q59799;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-DEC-2018, entry version 58.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod;
OS   Streptococcus agalactiae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-162.
RC   STRAIN=ATCC 13813 / CIP 103227 / DSM 2134 / JCM 5671 / NCTC 8181, and
RC   NEM1317;
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
RT   gene encoding the manganese-dependent superoxide dismutase.";
RL   J. Clin. Microbiol. 36:41-47(1998).
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       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; Z95893; CAB09346.1; -; Genomic_DNA.
DR   EMBL; Z99180; CAB16324.1; -; Genomic_DNA.
DR   PIR; S54792; S54792.
DR   RefSeq; WP_000974719.1; NZ_UHEZ01000003.1.
DR   ProteinModelPortal; P0A4J5; -.
DR   SMR; P0A4J5; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
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   3: Inferred from homology;
KW   Iron; Manganese; Metal-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    202       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000160085.
FT   METAL        27     27       Manganese or iron. {ECO:0000250}.
FT   METAL        81     81       Manganese or iron. {ECO:0000250}.
FT   METAL       163    163       Manganese or iron. {ECO:0000250}.
FT   METAL       167    167       Manganese or iron. {ECO:0000250}.
FT   VARIANT      60     60       V -> I (in strain: ATCC 13813).
FT   VARIANT      98     98       E -> D (in strain: ATCC 13813).
FT   VARIANT     104    104       N -> D (in strain: ATCC 13813).
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
//
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