ID K0NMG9_DESTT Unreviewed; 126 AA.
AC K0NMG9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Desulfoferrodoxin {ECO:0000256|ARBA:ARBA00014839};
DE EC=1.15.1.2 {ECO:0000256|ARBA:ARBA00012679};
DE AltName: Full=Superoxide reductase {ECO:0000256|ARBA:ARBA00031398};
GN Name=dfx {ECO:0000313|EMBL:CCK79902.1};
GN OrderedLocusNames=TOL2_C17410 {ECO:0000313|EMBL:CCK79902.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79902.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK79902.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- FUNCTION: Catalyzes the one-electron reduction of superoxide anion
CC radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a
CC fundamental role in case of oxidative stress via its superoxide
CC detoxification activity. {ECO:0000256|ARBA:ARBA00024690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized
CC [rubredoxin]; Xref=Rhea:RHEA:21324, Rhea:RHEA-COMP:10302, Rhea:RHEA-
CC COMP:10303, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.15.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001133};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604793-1};
CC Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via
CC four histidines and one cysteine residue.
CC {ECO:0000256|PIRSR:PIRSR604793-1};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|PIRSR:PIRSR604793-1};
CC Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via
CC 4 cysteine residues. {ECO:0000256|PIRSR:PIRSR604793-1};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family.
CC {ECO:0000256|ARBA:ARBA00005941}.
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DR EMBL; FO203503; CCK79902.1; -; Genomic_DNA.
DR RefSeq; WP_014957243.1; NC_018645.1.
DR AlphaFoldDB; K0NMG9; -.
DR STRING; 651182.TOL2_C17410; -.
DR KEGG; dto:TOL2_C17410; -.
DR PATRIC; fig|651182.5.peg.2072; -.
DR HOGENOM; CLU_118960_1_0_7; -.
DR OrthoDB; 9814936at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR CDD; cd03171; SORL_Dfx_classI; 1.
DR Gene3D; 2.20.28.100; Desulphoferrodoxin, N-terminal domain; 1.
DR Gene3D; 2.60.40.730; SOR catalytic domain; 1.
DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom.
DR InterPro; IPR036073; Desulfoferrodoxin_Fe-bd_dom_sf.
DR InterPro; IPR004462; Desulfoferrodoxin_N.
DR InterPro; IPR038094; Desulfoferrodoxin_N_sf.
DR InterPro; IPR004793; Desulfoferrodoxin_rbo.
DR NCBIfam; TIGR00320; dfx_rbo; 1.
DR NCBIfam; TIGR00332; neela_ferrous; 1.
DR PANTHER; PTHR36541; SUPEROXIDE REDUCTASE-RELATED; 1.
DR PANTHER; PTHR36541:SF1; SUPEROXIDE REDUCTASE-RELATED; 1.
DR Pfam; PF06397; Desulfoferrod_N; 1.
DR Pfam; PF01880; Desulfoferrodox; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR SUPFAM; SSF49367; Superoxide reductase-like; 1.
PE 3: Inferred from homology;
KW Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604793-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604793-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCK79902.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..36
FT /note="Desulfoferrodoxin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06397"
FT DOMAIN 42..126
FT /note="Desulfoferrodoxin ferrous iron-binding"
FT /evidence="ECO:0000259|Pfam:PF01880"
FT BINDING 10
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 13
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 29
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 49
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
SQ SEQUENCE 126 AA; 13865 MW; A0550466BB54673B CRC64;
MAEKLGIYKC GKCGNIVQVL HGEKPPVMCC GQAMDRLVEN TVDAALEKHV PVIEKLDGGY
LVKVGSVAHP MGNDHWIEWI ELASEDNTFV QRQMLTPSSA PEAEFKTDAA KVVARAYCNL
HGLWKS
//
