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Database: UniProt
Entry: P47201
LinkDB: P47201
Original site: P47201 
ID   SODM_MYCAV              Reviewed;         207 AA.
AC   P47201;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 80.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod;
OS   Mycobacterium avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25291 / DSM 44156 / NCTC 13034 / TMC 724;
RX   PubMed=8692009; DOI=10.1006/mpat.1996.0004;
RA   Escuyer V.E., Haddad N., Frehel C., Berche P.;
RT   "Molecular characterization of a surface-exposed superoxide dismutase
RT   of Mycobacterium avium.";
RL   Microb. Pathog. 20:41-55(1996).
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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; U11550; AAB08770.1; -; Genomic_DNA.
DR   RefSeq; WP_003872294.1; NZ_NSFM01000001.1.
DR   ProteinModelPortal; P47201; -.
DR   SMR; P47201; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
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   Manganese; Metal-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    207       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160045.
FT   METAL        28     28       Manganese. {ECO:0000250}.
FT   METAL        76     76       Manganese. {ECO:0000250}.
FT   METAL       160    160       Manganese. {ECO:0000250}.
FT   METAL       164    164       Manganese. {ECO:0000250}.
SQ   SEQUENCE   207 AA;  23044 MW;  EDA8DE05B2F1AC7F CRC64;
     MAEYTLPDLD WDYAALEPHI SGQINEIHHT KHHATYVKGV NDALAKLEEA RANEDHAAIF
     LNEKNLAFHL GGHVNHSIWW KNLSPDGGDK PTGELAAAID DAFGSFDKFR AQFSAAANGL
     QGSGWAVLGY DTLGSRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWADV QKRYAAATSK AQGLIFG
//
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