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Database: UniProt/TrEMBL
Entry: V6DH90_9DELT
LinkDB: V6DH90_9DELT
Original site: V6DH90_9DELT 
ID   V6DH90_9DELT            Unreviewed;       202 AA.
AC   V6DH90;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   07-JUN-2017, entry version 24.
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:CDK30308.1};
GN   ORFNames=BABL1_gene_1002 {ECO:0000313|EMBL:CDK30308.1};
OS   Candidatus Babela massiliensis.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Candidatus Babela.
OX   NCBI_TaxID=673862 {ECO:0000313|EMBL:CDK30308.1, ECO:0000313|Proteomes:UP000018769};
RN   [1] {ECO:0000313|EMBL:CDK30308.1, ECO:0000313|Proteomes:UP000018769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BABL1 {ECO:0000313|Proteomes:UP000018769};
RA   Pagnier I., Yutin N., Croce O., Makarova K.S., Wolf Y.I., Benamar S.,
RA   Raoult D., Koonin E.V., La Scola B.;
RT   "Babela massiliensis, a representative of a widespread bacterial
RT   phylum with unusual adaptations to parasitism in amoebae.";
RL   Biol. Direct 10:0-0(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; HG793133; CDK30308.1; -; Genomic_DNA.
DR   RefSeq; WP_023791252.1; NC_023003.1.
DR   EnsemblBacteria; CDK30308; CDK30308; BABL1_gene_1002.
DR   KEGG; dpb:BABL1_gene_1002; -.
DR   PATRIC; fig|673862.3.peg.196; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000018769; 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:UP000018769};
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:UP000018769}.
FT   DOMAIN        2     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        26     26       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   202 AA;  23690 MW;  9E0646F7C128B54B CRC64;
     MFKLPQLPYF YDALEPYIDA KTMEIHYTGH HQAYVNNLNA ALQNHPELQN LSLEDLITNL
     DKLPEKIRTE VRNNGGGHLN HSMFWTMMTK NSSLEPVGQL ETEIKKIWGT FEAFKEEFSN
     TAKKVFGSGW AWLTFDKAGK LIITSTPNQD TPISQDSQPI LGLDVWEHAY YLKYQNKRVD
     YIQAWWNVIN WKQIEENYRK YA
//
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