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   03-AUG-2022, entry version 144.
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; Moraxellales; Moraxellaceae;
OC   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 from
RT   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., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   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 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 family.
CC       {ECO:0000305}.
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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   AlphaFoldDB; Q59094; -.
DR   SMR; Q59094; -.
DR   STRING; 62977.ACIAD1070; -.
DR   EnsemblBacteria; CAG67957; CAG67957; ACIAD1070.
DR   GeneID; 45233511; -.
DR   KEGG; aci:ACIAD1070; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_6; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04930-MON; -.
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; 3.55.40.20; -; 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; Periplasm; Reference proteome;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..228
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000032903"
FT   BINDING         49
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="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