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Database: UniProt/TrEMBL
Entry: A0A0M4CZS5_9DELT
LinkDB: A0A0M4CZS5_9DELT
Original site: A0A0M4CZS5_9DELT 
ID   A0A0M4CZS5_9DELT        Unreviewed;       197 AA.
AC   A0A0M4CZS5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=DSOUD_0809 {ECO:0000313|EMBL:ALC15596.1};
OS   Desulfuromonas soudanensis.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Desulfuromonas.
OX   NCBI_TaxID=1603606 {ECO:0000313|EMBL:ALC15596.1, ECO:0000313|Proteomes:UP000057158};
RN   [1] {ECO:0000313|EMBL:ALC15596.1, ECO:0000313|Proteomes:UP000057158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WTL {ECO:0000313|EMBL:ALC15596.1,
RC   ECO:0000313|Proteomes:UP000057158};
RA   Badalamenti J.P., Summers Z.M., Gralnick J.A., Bond D.R.;
RT   "Isolation and Genomic Characterization of a Novel Halophilic Metal-
RT   Reducing Deltaproteobacterium from the Deep Subsurface.";
RL   Submitted (JUL-2015) 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; CP010802; ALC15596.1; -; Genomic_DNA.
DR   RefSeq; WP_053549789.1; NZ_CP010802.1.
DR   EnsemblBacteria; ALC15596; ALC15596; DSOUD_0809.
DR   KEGG; des:DSOUD_0809; -.
DR   PATRIC; fig|1603606.3.peg.889; -.
DR   KO; K04564; -.
DR   Proteomes; UP000057158; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000057158};
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:UP000057158}.
FT   DOMAIN        4     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   197 AA;  21693 MW;  47D1CDA4E0EE2C04 CRC64;
     MTIALPELPF PIAALEPHIS ARTFEFHHGK HHKAYVDNTN KLIEGTPLAG KDLESIILAA
     AGDQAKKGLF NNAAQVWNHS FFWKCLKPGG GGKPTGKVAA RIDADLGGYE KFAADFKNAG
     ATQFGSGWAW LVLKDGKLEI AQTANAETPL TKGHKPLLVV DVWEHGYYLD YQNRRPDFLQ
     AFLDHLVNWD FVNANLG
//
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