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Database: UniProt/TrEMBL
Entry: A0A0H3E1Q0_BACA1
LinkDB: A0A0H3E1Q0_BACA1
Original site: A0A0H3E1Q0_BACA1 
ID   A0A0H3E1Q0_BACA1        Unreviewed;       202 AA.
AC   A0A0H3E1Q0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   28-MAR-2018, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=BATR1942_10825 {ECO:0000313|EMBL:ADP33096.1};
OS   Bacillus atrophaeus (strain 1942).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP33096.1, ECO:0000313|Proteomes:UP000006867};
RN   [1] {ECO:0000313|Proteomes:UP000006867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA   Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C.,
RA   Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A.,
RA   Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA   Lindquist J., Liem A., Fochler E., Tapia R., Bishop-Lilly K.,
RA   Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP002207; ADP33096.1; -; Genomic_DNA.
DR   RefSeq; WP_004429530.1; NC_014639.1.
DR   STRING; 720555.BATR1942_10825; -.
DR   EnsemblBacteria; ADP33096; ADP33096; BATR1942_10825.
DR   GeneID; 23410614; -.
DR   KEGG; bae:BATR1942_10825; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   Proteomes; UP000006867; Chromosome.
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 {ECO:0000313|Proteomes:UP000006867};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006867}.
FT   DOMAIN        2     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   202 AA;  22552 MW;  DFE8702EB4F8D628 CRC64;
     MAYELPELPY AYDALEPHID KETMNIHHTK HHNTYVTNLN KAVEGNTAFA NKSVEELVAD
     LNAVPENIRT AVRNNGGGHA NHKLFWTLLS PNGGGEPTGD LAEAIKSEFG SFDKFKEQFG
     AAATGRFGSG WAWLVVNNGK LEITSTPNQD SPLSEGKTPV LGLDVWEHAY YLNYQNRRPD
     YISAFWNVVN WDEVARLYSE AK
//
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