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Database: UniProt
Entry: Q7UPW1_RHOBA
LinkDB: Q7UPW1_RHOBA
Original site: Q7UPW1_RHOBA 
ID   Q7UPW1_RHOBA            Unreviewed;       228 AA.
AC   Q7UPW1;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   16-JAN-2019, entry version 86.
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:CAD74947.1};
GN   OrderedLocusNames=RB6688 {ECO:0000313|EMBL:CAD74947.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD74947.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD74947.1, ECO:0000313|Proteomes:UP000001025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC   {ECO:0000313|Proteomes:UP000001025};
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T.,
RA   Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R.,
RA   Schlesner H., Amann R., Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp.
RT   strain 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294144; CAD74947.1; -; Genomic_DNA.
DR   RefSeq; NP_867401.1; NC_005027.1.
DR   RefSeq; WP_011121045.1; NC_005027.1.
DR   ProteinModelPortal; Q7UPW1; -.
DR   STRING; 243090.RB6688; -.
DR   EnsemblBacteria; CAD74947; CAD74947; RB6688.
DR   GeneID; 1790303; -.
DR   KEGG; rba:RB6688; -.
DR   PATRIC; fig|243090.15.peg.3243; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; Q7UPW1; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; RBAL243090:RB6688-MONOMER; -.
DR   Proteomes; UP000001025; 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:UP000001025};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CAD74947.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025}.
FT   DOMAIN       24    109       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      117    223       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        48     48       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       102    102       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       190    190       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       194    194       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   228 AA;  24901 MW;  4A7A5A10FAFD5F78 CRC64;
     MVRYRRRRSL YFRHPQTPMS TMAFTLPELP YAYDALEPHI DARTMEIHHS KHHNAYVTKT
     NDALAGTDLA SKSIEEVISD LSAVPDDKRG AVRNNGGGHA NHSLFWTVLG PGKGGSPSGD
     LAAAIDEACG SFDAFKEQFA NAAATRFGSG WAWLYVSGGK LHVGSTANQD SPLMGEAVAG
     IGGTPILGLD VWEHAYYLNY QNRRPDYISA FWNVVDWDAV ATRFAAAK
//
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