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Database: UniProt/SWISS-PROT
Entry: SODF_COXBU
LinkDB: SODF_COXBU
Original site: SODF_COXBU 
ID   SODF_COXBU              Reviewed;         193 AA.
AC   P19685;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-OCT-2017, entry version 115.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=CBU_1708;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hamilton;
RX   PubMed=2243797; DOI=10.1093/nar/18.21.6437;
RA   Heinzen R.A., Frazier M.E., Mallavia L.P.;
RT   "Nucleotide sequence of Coxiella burnetii superoxide dismutase.";
RL   Nucleic Acids Res. 18:6437-6437(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hamilton;
RX   PubMed=1500190;
RA   Heinzen R.A., Frazier M.E., Mallavia L.P.;
RT   "Coxiella burnetii superoxide dismutase gene: cloning, sequencing, and
RT   expression in Escherichia coli.";
RL   Infect. Immun. 60:3814-3823(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E.,
RA   Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J.,
RA   DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J.,
RA   Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A.,
RA   Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella
RT   burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; X54627; CAA38444.1; -; Genomic_DNA.
DR   EMBL; M74242; AAA23311.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO91203.1; -; Genomic_DNA.
DR   PIR; A44791; A44791.
DR   RefSeq; NP_820689.1; NC_002971.3.
DR   RefSeq; WP_005770533.1; NZ_CCYB01000004.1.
DR   PDB; 3TQJ; X-ray; 2.00 A; A/B=1-193.
DR   PDBsum; 3TQJ; -.
DR   ProteinModelPortal; P19685; -.
DR   SMR; P19685; -.
DR   STRING; 227377.CBU_1708; -.
DR   PRIDE; P19685; -.
DR   EnsemblBacteria; AAO91203; AAO91203; CBU_1708.
DR   GeneID; 1209619; -.
DR   GeneID; 31482933; -.
DR   KEGG; cbu:CBU_1708; -.
DR   PATRIC; fig|227377.7.peg.1694; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000002671; 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   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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    193       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159978.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        74     74       Iron. {ECO:0000250}.
FT   METAL       157    157       Iron. {ECO:0000250}.
FT   METAL       161    161       Iron. {ECO:0000250}.
FT   TURN         12     18       {ECO:0000244|PDB:3TQJ}.
FT   HELIX        21     29       {ECO:0000244|PDB:3TQJ}.
FT   HELIX        31     43       {ECO:0000244|PDB:3TQJ}.
FT   TURN         47     50       {ECO:0000244|PDB:3TQJ}.
FT   HELIX        53     59       {ECO:0000244|PDB:3TQJ}.
FT   HELIX        62     79       {ECO:0000244|PDB:3TQJ}.
FT   HELIX        91    101       {ECO:0000244|PDB:3TQJ}.
FT   HELIX       104    117       {ECO:0000244|PDB:3TQJ}.
FT   STRAND      120    128       {ECO:0000244|PDB:3TQJ}.
FT   STRAND      134    140       {ECO:0000244|PDB:3TQJ}.
FT   HELIX       145    148       {ECO:0000244|PDB:3TQJ}.
FT   STRAND      151    157       {ECO:0000244|PDB:3TQJ}.
FT   HELIX       160    162       {ECO:0000244|PDB:3TQJ}.
FT   HELIX       164    167       {ECO:0000244|PDB:3TQJ}.
FT   HELIX       171    181       {ECO:0000244|PDB:3TQJ}.
FT   HELIX       184    191       {ECO:0000244|PDB:3TQJ}.
SQ   SEQUENCE   193 AA;  22274 MW;  E18F532CB2041916 CRC64;
     MAFELPDLPY KLNALEPHIS QETLEYHHGK HHRAYVNKLN KLIEGTPFEK EPLEEIIRKS
     DGGIFNNAAQ HWNHTFYWHC MSPDGGGDPS GELASAIDKT FGSLEKFKAL FTDSANNHFG
     SGWAWLVKDN NGKLEVLSTV NARNPMTEGK KPLMTCDVWE HAYYIDTRND RPKYVNNFWQ
     VVNWDFVMKN FKS
//
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