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Database: UniProt/TrEMBL
Entry: W5YNN8_9ALTE
LinkDB: W5YNN8_9ALTE
Original site: W5YNN8_9ALTE 
ID   W5YNN8_9ALTE            Unreviewed;       192 AA.
AC   W5YNN8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 20.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AU15_01370 {ECO:0000313|EMBL:AHI30514.1};
OS   Marinobacter salarius.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=1420917 {ECO:0000313|EMBL:AHI30514.1, ECO:0000313|Proteomes:UP000035081};
RN   [1] {ECO:0000313|EMBL:AHI30514.1, ECO:0000313|Proteomes:UP000035081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3d10 and R9SW1 {ECO:0000313|Proteomes:UP000035081};
RX   PubMed=24855296;
RA   Ivanova E.P., Ng H.J., Webb H.K., Feng G., Oshima K., Hattori M.,
RA   Ohkuma M., Sergeev A.F., Mikhailov V.V., Crawford R.J., Sawabe T.;
RT   "Draft Genome Sequences of Marinobacter similis A3d10T and
RT   Marinobacter salarius R9SW1T.";
RL   Genome Announc. 2:e00442-14(2014).
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; CP007152; AHI30514.1; -; Genomic_DNA.
DR   RefSeq; WP_036210113.1; NZ_CP007152.1.
DR   EnsemblBacteria; AHI30514; AHI30514; AU15_01370.
DR   KEGG; msr:AU15_01370; -.
DR   KO; K04564; -.
DR   Proteomes; UP000035081; 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 {ECO:0000313|Proteomes:UP000035081};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     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;  21606 MW;  E651A76E1EB9F4C3 CRC64;
     MAFELPALPY EKNALEPHIS QETLEYHYGK HHNTYVTKLN GLVEGTDNAN KSLEDIIKSA
     SGPLFNNAAQ VWNHTFYWHC LSPNGGGEPT GAAKDAIEKA FGSFEDFKKE FNDKAANNFG
     SGWTWLVKKA DGSVAIVNTS NAETPLTTAD KPVLTVDVWE HAYYIDYRNS RPNYLEAFWK
     LVNWDFVNEN LA
//
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