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Database: UniProt
Entry: Q9F326
LinkDB: Q9F326
Original site: Q9F326 
ID   SODM_STACA              Reviewed;         201 AA.
AC   Q9F326; Q5IBS1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   05-DEC-2018, entry version 66.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod;
OS   Staphylococcus carnosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=833;
RX   PubMed=11556918; DOI=10.1046/j.1365-2672.2001.01411.x;
RA   Barriere C., Leroy-Setrin S., Talon R.;
RT   "Characterization of catalase and superoxide dismutase in
RT   Staphylococcus carnosus 833 strain.";
RL   J. Appl. Microbiol. 91:514-519(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-161.
RC   STRAIN=CIT S00-298;
RX   PubMed=16488037; DOI=10.1016/j.ijfoodmicro.2005.12.006;
RA   Corbiere Morot-Bizot S., Leroy S., Talon R.;
RT   "Staphylococcal community of a small unit manufacturing traditional
RT   dry fermented sausages.";
RL   Int. J. Food Microbiol. 108:210-217(2006).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000269|PubMed:11556918}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: SOD activity increases in mid-exponential growth-
CC       phase.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AJ295150; CAC14833.1; -; Genomic_DNA.
DR   EMBL; AY795886; AAW32466.1; -; Genomic_DNA.
DR   RefSeq; WP_015900423.1; NZ_LISV01000002.1.
DR   ProteinModelPortal; Q9F326; -.
DR   SMR; Q9F326; -.
DR   PATRIC; fig|1281.6.peg.252; -.
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; Stress response.
FT   CHAIN         1    201       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000293968.
FT   METAL        27     27       Manganese or iron. {ECO:0000250}.
FT   METAL        81     81       Manganese or iron. {ECO:0000250}.
FT   METAL       162    162       Manganese or iron. {ECO:0000250}.
FT   METAL       166    166       Manganese or iron. {ECO:0000250}.
SQ   SEQUENCE   201 AA;  22980 MW;  4F23EF7BF19556A4 CRC64;
     MAFELPNLPY EFDALEPYID KETMEIHHDK HHNTYVTKLN AAIEGTDLEN KSIEEIVANL
     DSVPSDIQTA VRNNGGGHLN HSLFWQLLTP NSEEKGTVID KIKEEWGSLD KFKDEFAKKA
     AGQFGSGWAW LVVDKDGKLE IVSTPNQDNP ITEGKTPILG LDVWEHAYYL KYQNKRPDYI
     DAFWNVVNWN KVDELYEAAT K
//
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