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Database: UniProt
Entry: X5H4U3_9RICK
LinkDB: X5H4U3_9RICK
Original site: X5H4U3_9RICK 
ID   X5H4U3_9RICK            Unreviewed;       208 AA.
AC   X5H4U3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 22.
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:AHX11728.1};
GN   ORFNames=NHE_0803 {ECO:0000313|EMBL:AHX11728.1};
OS   Neorickettsia helminthoeca str. Oregon.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=1286528 {ECO:0000313|EMBL:AHX11728.1};
RN   [1] {ECO:0000313|EMBL:AHX11728.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon {ECO:0000313|EMBL:AHX11728.1};
RA   Lin M., Daugherty S.C., Nagaraj S., Cheng Z., Xiong Q., Lin F.-Y.,
RA   Sengamalay N., Ott S., Godinez A., Tallon L.J., Sadzewicz L.,
RA   Fraser C.M., Dunning Hotopp J.C., Rikihisa Y.;
RT   "Sequencing and Comparison of Genomes and Transcriptome Profiles of
RT   Human Ehrlichiosis Agents.";
RL   Submitted (MAR-2014) 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; CP007481; AHX11728.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHX11728; AHX11728; NHE_0803.
DR   KEGG; nhm:NHE_0803; -.
DR   KO; K04564; -.
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,
KW   ECO:0000313|EMBL:AHX11728.1}.
FT   DOMAIN        9     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       99    202       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        31     31       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        83     83       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       173    173       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  23698 MW;  14A294ED7BC5422E CRC64;
     MRSAIKIILP ELPYHKDALE PLISEKTLGF HYDKHHAGYV NKVNELLVES DDVGDTLLCV
     IRNTWNKQGK EAIFNNAAQV WNHTFYWNSM RPPASACSPD DRLMLQIVKD FGGMEELKQQ
     LSLAAVTQFG SGWAWLIFDK ASQRLSVVKT SNAETPLTNQ NFVPLLAIDV WEHAYYLDYQ
     NRRPDYVATF LAQLINWDFA SANYSAVG
//
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