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Database: UniProt
Entry: P53642
LinkDB: P53642
Original site: P53642 
ID   SODM_BORPE              Reviewed;         211 AA.
AC   P53642;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-DEC-2018, entry version 113.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=BP0193;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=9079904; DOI=10.1128/jb.179.7.2194-2201.1997;
RA   Graeff-Wohlleben H., Killat S., Banemann A., Guiso N., Gross R.;
RT   "Cloning and characterization of an Mn-containing superoxide dismutase
RT   (SodA) of Bordetella pertussis.";
RL   J. Bacteriol. 179:2194-2201(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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; X84800; CAA59267.1; -; Genomic_DNA.
DR   EMBL; BX640411; CAE40572.1; -; Genomic_DNA.
DR   RefSeq; NP_879082.1; NC_002929.2.
DR   RefSeq; WP_010929673.1; NC_002929.2.
DR   ProteinModelPortal; P53642; -.
DR   SMR; P53642; -.
DR   STRING; 257313.BP0193; -.
DR   PRIDE; P53642; -.
DR   EnsemblBacteria; CAE40572; CAE40572; BP0193.
DR   GeneID; 2664387; -.
DR   KEGG; bpe:BP0193; -.
DR   PATRIC; fig|257313.5.peg.204; -.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   BioCyc; BPER257313:BP0193_2-MONOMER; -.
DR   Proteomes; UP000002676; 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    211       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160021.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        82     82       Manganese. {ECO:0000250}.
FT   METAL       165    165       Manganese. {ECO:0000250}.
FT   METAL       169    169       Manganese. {ECO:0000250}.
SQ   SEQUENCE   211 AA;  23212 MW;  354903AF71136CD8 CRC64;
     MPYVLPALSY AYDALEPHID ARTMEIHHTR HHQTYVNGLN AALEGAGLDS EEPVEQLLRR
     IPALPPGIHG AVRNHGGGHA NHSLLWTVMS PSGGGRPDGR LAADIQAQLG GHDAFQAAFT
     QAALGRFGSG WAWLTVTPAG RLRVDSSANQ DSPLMEGNTP ILGLDVWEHA YYLQYQNRRP
     EYIEAFYRVV DWAEVARRYE IALAELGREA A
//
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