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Database: UniProt/SWISS-PROT
Entry: SODM_BACHD
LinkDB: SODM_BACHD
Original site: SODM_BACHD 
ID   SODM_BACHD              Reviewed;         202 AA.
AC   Q9KD10;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-OCT-2017, entry version 95.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=BH1409;
OS   Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM
OS   9153 / C-125).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; BA000004; BAB05128.1; -; Genomic_DNA.
DR   PIR; A83826; A83826.
DR   RefSeq; WP_010897574.1; NC_002570.2.
DR   ProteinModelPortal; Q9KD10; -.
DR   SMR; Q9KD10; -.
DR   STRING; 272558.BH1409; -.
DR   EnsemblBacteria; BAB05128; BAB05128; BAB05128.
DR   KEGG; bha:BH1409; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000001258; Chromosome.
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   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   Phosphoprotein; Reference proteome.
FT   CHAIN         1    202       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160017.
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}.
FT   MOD_RES      34     34       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES      70     70       Phosphothreonine. {ECO:0000250}.
SQ   SEQUENCE   202 AA;  22413 MW;  94384166CC56D9E7 CRC64;
     MAFELPKLPY PANALEPHID EATMNIHHGK HHNTYVTKLN AALEGHSALA EKSIEALVSD
     LDAVPENIRT AVRNNGGGHA NHTLFWQILS PNGGGAPTGE LADAINAEFG SFDQFKEKFA
     DAAANRFGSG WAWLVVNDGK LEITSTPNQD TPLMEGKTPI LGLDVWEHAY YLNYQNRRPD
     YISAFWNVVN WDEVAKRYNE AK
//
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