GenomeNet

Database: UniProt
Entry: Q89AR7
LinkDB: Q89AR7
Original site: Q89AR7 
ID   SODM_BUCBP              Reviewed;         208 AA.
AC   Q89AR7;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JAN-2019, entry version 89.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=bbp_178;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AE016826; AAO26910.1; -; Genomic_DNA.
DR   RefSeq; WP_011091311.1; NC_004545.1.
DR   ProteinModelPortal; Q89AR7; -.
DR   SMR; Q89AR7; -.
DR   STRING; 224915.bbp178; -.
DR   EnsemblBacteria; AAO26910; AAO26910; bbp_178.
DR   KEGG; bab:bbp_178; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; BAPH224915:G1G09-181-MONOMER; -.
DR   Proteomes; UP000000601; Chromosome.
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   Complete proteome; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    208       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160024.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        81     81       Manganese. {ECO:0000250}.
FT   METAL       168    168       Manganese. {ECO:0000250}.
FT   METAL       172    172       Manganese. {ECO:0000250}.
SQ   SEQUENCE   208 AA;  24551 MW;  2FFC200F5E3CF4D7 CRC64;
     MTYVLPSLPY SYNSLEPFFD EKTMIIHHTR HHQAYINNTN SILNGTHYEN LLIEELISKL
     NILSIENKLA LQNNAGGHIN HSLFWKWLKL NTILKDDFKI ILEKNFKSVD FFKKQFEKIA
     LSHFGSGWIW LIKKYDNTLR IVTTVNQNTP LMGKEISGIS GIPILGLDLW EHAYYLKYKN
     NRSDYVNAFW NVVNWDEVSY RFFNISNM
//
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