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Database: UniProt
Entry: D6ZKL6_MOBCV
LinkDB: D6ZKL6_MOBCV
Original site: D6ZKL6_MOBCV 
ID   D6ZKL6_MOBCV            Unreviewed;       206 AA.
AC   D6ZKL6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 43.
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:ADI67265.1};
GN   OrderedLocusNames=HMPREF0573_10946 {ECO:0000313|EMBL:ADI67265.1};
OS   Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS   vaginalis).
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI67265.1, ECO:0000313|Proteomes:UP000006742};
RN   [1] {ECO:0000313|Proteomes:UP000006742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43063 / DSM 2711 / V125
RC   {ECO:0000313|Proteomes:UP000006742};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT   "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL   Submitted (MAR-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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={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; CP001992; ADI67265.1; -; Genomic_DNA.
DR   RefSeq; WP_004007494.1; NC_014246.1.
DR   ProteinModelPortal; D6ZKL6; -.
DR   EnsemblBacteria; ADI67265; ADI67265; HMPREF0573_10946.
DR   KEGG; mcu:HMPREF0573_10946; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000006742; 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:UP000006742};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ADI67265.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006742}.
FT   DOMAIN        4     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       93    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   206 AA;  23081 MW;  DF60D55A19FA05CA CRC64;
     MAVYTLPELP YDYAALEPHI SGKIMQLHHD KHHANYVNGA NTALEKLEEA RATGNFATIN
     QLEKDLAFNL GGHANHSAFW KMMGPANDTP DRPSGELAAA IDEYFGSFEA FQKHFTAAAT
     GLQGSGWAVL AWDSVAGRPV IFQLFDQQSN VPIAQIPLLM LDMWEHAFYL DYLNVKGDYV
     KAWWNVVNWT EVENRFHAAS KHHGVL
//
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