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Database: UniProt
Entry: Q694A3
LinkDB: Q694A3
Original site: Q694A3 
ID   SODM_GLOMM              Reviewed;         216 AA.
AC   Q694A3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   05-DEC-2018, entry version 50.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=Sod2;
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Hippoboscoidea; Glossinidae; Glossina.
OX   NCBI_TaxID=37546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16164604; DOI=10.1111/j.1365-2583.2005.00579.x;
RA   Munks R.J., Sant'Anna M.R., Grail W., Gibson W., Igglesden T.,
RA   Yoshiyama M., Lehane S.M., Lehane M.J.;
RT   "Antioxidant gene expression in the blood-feeding fly Glossina
RT   morsitans morsitans.";
RL   Insect Mol. Biol. 14:483-491(2005).
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AY625509; AAT85826.1; -; mRNA.
DR   ProteinModelPortal; Q694A3; -.
DR   Proteomes; UP000092444; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Complete proteome; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1     18       Mitochondrion. {ECO:0000250}.
FT   CHAIN        19    216       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000291555.
FT   METAL        44     44       Manganese. {ECO:0000250}.
FT   METAL        92     92       Manganese. {ECO:0000250}.
FT   METAL       176    176       Manganese. {ECO:0000250}.
FT   METAL       180    180       Manganese. {ECO:0000250}.
SQ   SEQUENCE   216 AA;  24571 MW;  C758C0EEEFC7AA59 CRC64;
     MSFLNRNLSR TIKAAVRGKH TLPKLPYDYG ALAPIISKDI LEVHHGKHHQ TYVNNLNAVE
     EQMTEAHSKK DVNKVVELSK NYAFNWGGHL NHSIYWQNLS PTKSEPSADL KKAIEEQFSS
     FEQFKKDLSA LSIGVQGSGW GWLGYNKKXK KLQILAVSNQ EPLQAVTGLV PLFAIDVWEH
     AYYLQXKNXX AKYVEAXWDI ANWKBISDRY AEATCN
//
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