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Database: UniProt
Entry: P28763
LinkDB: P28763
Original site: P28763 
ID   SODM_LISIV              Reviewed;         202 AA.
AC   P28763;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   01-OCT-2014, entry version 68.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod;
OS   Listeria ivanovii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19119 / DSM 20750 / JCM 7681 / NCTC 11846 / SLCC 2379;
RX   PubMed=1736100;
RA   Haas A., Goebel W.;
RT   "Cloning of a superoxide dismutase gene from Listeria ivanovii by
RT   functional complementation in Escherichia coli and characterization of
RT   the gene product.";
RL   Mol. Gen. Genet. 231:313-322(1992).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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DR   EMBL; X64011; CAA45406.1; -; Genomic_DNA.
DR   PIR; S20019; S20019.
DR   ProteinModelPortal; P28763; -.
DR   SMR; P28763; 3-201.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11404; PTHR11404; 1.
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   Manganese; Metal-binding; Oxidoreductase.
FT   CHAIN         1    202       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160043.
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;  22671 MW;  C04193B793E29AD0 CRC64;
     MTYELPKLPY TYDALEPNFD KETMEIHYTK HHNIYVTKLN EAVSGHAELA SKPGEELVAN
     LDSVPEEIRG AVRNHGGGHA NHTLFWSSLS PNGGGAPTGN LKAAIESEFG TFDEFKEKFN
     AAAAARFGSG WAWLVVNNGK LEIVSTANQD SPLSEGKTPV LGLDVWEHAY YLKFQNRRPE
     YIDTFWNVIN WDERNKRFDA AK
//
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