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Database: UniProt
Entry: P28764
LinkDB: P28764
Original site: P28764 
ID   SODM_LISMO              Reviewed;         202 AA.
AC   P28764;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   05-DEC-2018, entry version 120.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod; OrderedLocusNames=lmo1439;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EGD / Serovar 1/2a;
RX   PubMed=1511873; DOI=10.1016/0378-1119(92)90258-Q;
RA   Brehm K., Haas A., Goebel W., Kreft J.;
RT   "A gene encoding a superoxide dismutase of the facultative
RT   intracellular bacterium Listeria monocytogenes.";
RL   Gene 118:121-125(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; M80526; AAA25292.1; -; Genomic_DNA.
DR   EMBL; AL591979; CAC99517.1; -; Genomic_DNA.
DR   PIR; AG1254; AG1254.
DR   PIR; JC1272; JC1272.
DR   RefSeq; NP_464964.1; NC_003210.1.
DR   RefSeq; WP_003721944.1; NC_003210.1.
DR   ProteinModelPortal; P28764; -.
DR   SMR; P28764; -.
DR   STRING; 169963.lmo1439; -.
DR   PaxDb; P28764; -.
DR   EnsemblBacteria; CAC99517; CAC99517; CAC99517.
DR   GeneID; 986791; -.
DR   KEGG; lmo:lmo1439; -.
DR   PATRIC; fig|169963.11.peg.1478; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   PhylomeDB; P28764; -.
DR   BioCyc; LMON169963:LMO1439-MONOMER; -.
DR   Proteomes; UP000000817; 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    202       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160044.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        82     82       Manganese. {ECO:0000250}.
FT   METAL       164    164       Manganese. {ECO:0000250}.
FT   METAL       168    168       Manganese. {ECO:0000250}.
SQ   SEQUENCE   202 AA;  22631 MW;  75D40A4C45A93450 CRC64;
     MTYELPKLPY TYDALEPNFD KETMEIHYTK HHNTYVTKLN EAVAGHPELA SKSAEELVTN
     LDSVPEDIRG AVRNHGGGHA NHTLFWSILS PNGGGAPTGN LKAAIESEFG TFDEFKEKFN
     AAAAARFGSG WAWLVVNDGK LEIVSTANQD SPLSDGKTPV LGLDVWEHAY YLKFQNRRPE
     YIETFWNVIN WDEANKRFDA AK
//
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