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 03-AUG-2022, entry version 132.
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; Coxiellaceae;
OC 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; DOI=10.1128/iai.60.9.3814-3823.1992;
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., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella 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 systems.
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 -!- 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 family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P19685; -.
DR SMR; P19685; -.
DR STRING; 227377.CBU_1708; -.
DR EnsemblBacteria; AAO91203; AAO91203; CBU_1708.
DR GeneID; 1209619; -.
DR KEGG; cbu:CBU_1708; -.
DR PATRIC; fig|227377.7.peg.1694; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_0_6; -.
DR OMA; YLHSIFW; -.
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 Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 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 1: Evidence at protein level;
KW 3D-structure; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..193
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159978"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT TURN 12..18
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:3TQJ"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 62..79
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:3TQJ"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:3TQJ"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3TQJ"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:3TQJ"
FT HELIX 184..191
FT /evidence="ECO:0007829|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
