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Database: UniProt
Entry: Q59094
LinkDB: Q59094
Original site: Q59094 
ID   SODM_ACIAD              Reviewed;         228 AA.
AC   Q59094;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-FEB-2019, entry version 126.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sodA; Synonyms=sodM; OrderedLocusNames=ACIAD1070;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9074511; DOI=10.1016/S0378-1119(96)00728-7;
RA   Geissdoerfer W., Ratajczak A., Hillen W.;
RT   "Nucleotide sequence of a putative periplasmic Mn superoxide dismutase
RT   from Acinetobacter calcoaceticus ADP1.";
RL   Gene 186:305-308(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; Z46863; CAA86923.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG67957.1; -; Genomic_DNA.
DR   PIR; JC6320; JC6320.
DR   RefSeq; WP_004921627.1; NC_005966.1.
DR   ProteinModelPortal; Q59094; -.
DR   SMR; Q59094; -.
DR   STRING; 62977.ACIAD1070; -.
DR   EnsemblBacteria; CAG67957; CAG67957; ACIAD1070.
DR   KEGG; aci:ACIAD1070; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; YSKHHAT; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04930-MONOMER; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; 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   3: Inferred from homology;
KW   Complete proteome; Manganese; Metal-binding; Oxidoreductase;
KW   Periplasm; Reference proteome; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    228       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000032903.
FT   METAL        49     49       Manganese. {ECO:0000250}.
FT   METAL       100    100       Manganese. {ECO:0000250}.
FT   METAL       188    188       Manganese. {ECO:0000250}.
FT   METAL       192    192       Manganese. {ECO:0000250}.
SQ   SEQUENCE   228 AA;  25741 MW;  4475C9AD9FFEE0F8 CRC64;
     MTRSLKTTLI LLASSVISMS ALAEFKQAPL PYATNALQPA IDQQTMEIHY GKHHKAYVDN
     LNAQIKTYPE LDKTDLIQLQ KQISKYNTAV RNNGGGHFNH TFFWESLAAT NKTGQPSPAL
     VKQITQDFGS LDAFKQKFNE AASGRFGSGW AWLIVTPNGK LAVTSTPNQD NPLMDLSETK
     GTPLLGLDVW EHAYYLKYQN RRADYIKAFW SVVNWNKVNE RYNEAIKK
//
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