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Database: UniProt
Entry: V9TX65_9PROT
LinkDB: V9TX65_9PROT
Original site: V9TX65_9PROT 
ID   V9TX65_9PROT            Unreviewed;       202 AA.
AC   V9TX65;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:AHC73925.1};
GN   ORFNames=P856_720 {ECO:0000313|EMBL:AHC73925.1};
OS   Candidatus Endolissoclinum faulkneri L5.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Candidatus Endolissoclinum.
OX   NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73925.1};
RN   [1] {ECO:0000313|EMBL:AHC73925.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L5 {ECO:0000313|EMBL:AHC73925.1};
RX   PubMed=24324632;
RA   Kwan J.C., Schmidt E.W.;
RT   "Bacterial endosymbiosis in a chordate host: long-term co-evolution
RT   and conservation of secondary metabolism.";
RL   PLoS ONE 8:E80822-E80822(2013).
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; CP006745; AHC73925.1; -; Genomic_DNA.
DR   RefSeq; WP_025300802.1; NZ_CP006745.1.
DR   EnsemblBacteria; AHC73925; AHC73925; P856_720.
DR   KEGG; efk:P856_720; -.
DR   PATRIC; fig|1401328.3.peg.728; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    195       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       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   202 AA;  22968 MW;  51F60401C24002C7 CRC64;
     MVFELPSLPY EYNALEPVMS KETLEYHHDK HHNAYVVNAN RLMNGSGLAH KSLEDAIKTA
     YLTAEAGSLF NNIAQHWNHI EFWKWMKPNG GGAIPGTLEK KIISDFGSVE AMKEKFVEFG
     IGQFGSGWVW LVLGEEGKLY ITNTSNGINP LAMGNGIALL GCDVWEHSYY IDYRNARVDY
     IRAFVRDLVN WERVADIFDQ SY
//
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