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Database: UniProt/TrEMBL
Entry: A0A0N9M2J5_9GAMM
LinkDB: A0A0N9M2J5_9GAMM
Original site: A0A0N9M2J5_9GAMM 
ID   A0A0N9M2J5_9GAMM        Unreviewed;       192 AA.
AC   A0A0N9M2J5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   07-JUN-2017, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AL038_10350 {ECO:0000313|EMBL:ALG68033.1};
OS   Beggiatoa leptomitiformis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Beggiatoa.
OX   NCBI_TaxID=319938 {ECO:0000313|EMBL:ALG68033.1, ECO:0000313|Proteomes:UP000055853};
RN   [1] {ECO:0000313|EMBL:ALG68033.1, ECO:0000313|Proteomes:UP000055853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D-402 {ECO:0000313|EMBL:ALG68033.1,
RC   ECO:0000313|Proteomes:UP000055853};
RX   PubMed=26659680;
RA   Fomenkov A., Vincze T., Grabovich M.Y., Dubinina G., Orlova M.,
RA   Belousova E., Roberts R.J.;
RT   "Complete Genome Sequence of the Freshwater Colorless Sulfur Bacterium
RT   Beggiatoa leptomitiformis Neotype Strain D-402T.";
RL   Genome Announc. 3:e01436-15(2015).
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; CP012373; ALG68033.1; -; Genomic_DNA.
DR   RefSeq; WP_062152556.1; NZ_CP012373.1.
DR   EnsemblBacteria; ALG68033; ALG68033; AL038_10350.
DR   KEGG; blep:AL038_10350; -.
DR   PATRIC; fig|319938.3.peg.2180; -.
DR   KO; K04564; -.
DR   Proteomes; UP000055853; 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:UP000055853};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    189       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21755 MW;  36D098E7F3E02FD8 CRC64;
     MEHKLPELPY AMDALAPHIS KETLEFHYGK HHQTYVTNLN NLIRGTEFEN LSLEEIIKKS
     SGGLFNNAAQ VWNHTFYWHC LSPKGGNEPT GKLAEAINKQ FNSFAEFKEK FTQTAITTFG
     SGWAWLVQKA DGSLALVSTS NAATPMTAGD TALLTCDVWE HAYYVDYRNA RPKYVESFWN
     LVNWDFVASN LK
//
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