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Database: UniProt/TrEMBL
Entry: D5DSC7_BACMQ
LinkDB: D5DSC7_BACMQ
Original site: D5DSC7_BACMQ 
ID   D5DSC7_BACMQ            Unreviewed;       202 AA.
AC   D5DSC7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 40.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:ADE71525.1};
GN   OrderedLocusNames=BMQ_4516 {ECO:0000313|EMBL:ADE71525.1};
OS   Bacillus megaterium (strain ATCC 12872 / QMB1551).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE71525.1, ECO:0000313|Proteomes:UP000000935};
RN   [1] {ECO:0000313|Proteomes:UP000000935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935};
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J.,
RA   Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J.,
RA   Vary P.S.;
RT   "Genome sequences of the industrial vitamin B12-producers B.
RT   megaterium QM B1551 and DSM319 reveal new insights into the Bacillus
RT   genome evolution and pan-genome structure.";
RL   Submitted (FEB-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; CP001983; ADE71525.1; -; Genomic_DNA.
DR   RefSeq; WP_013059198.1; NC_014019.1.
DR   STRING; 545693.BMQ_4516; -.
DR   EnsemblBacteria; ADE71525; ADE71525; BMQ_4516.
DR   KEGG; bmq:BMQ_4516; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000000935; 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   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:UP000000935};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ADE71525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000935}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    197       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;  22557 MW;  AB6C7F0F356F20DD CRC64;
     MAYKLPELPY AYDALEPHID KETMNIHHTK HHNTYVTNLN AAVEGKADLE SKSIEELISN
     LDAVPEDIRT AVRNNGGGHA NHSLFWTILC PNGGGAPTGE LADAIASKFG SFDQFKEEFA
     NAAKTRFGSG WAWLVVNNGE LEVTSTPNQD SPLMEGKTPI LGLDVWEHAY YLNYQNRRPD
     YISAFFNVVK WDEVAKRYDA AK
//
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