ID C6E275_GEOSM Unreviewed; 124 AA.
AC C6E275;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=GM21_0956 {ECO:0000313|EMBL:ACT17021.1};
OS Geobacter sp. (strain M21).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT17021.1};
RN [1] {ECO:0000313|EMBL:ACT17021.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21 {ECO:0000313|EMBL:ACT17021.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001661; ACT17021.1; -; Genomic_DNA.
DR AlphaFoldDB; C6E275; -.
DR STRING; 443144.GM21_0956; -.
DR KEGG; gem:GM21_0956; -.
DR eggNOG; COG2033; Bacteria.
DR HOGENOM; CLU_118960_1_0_7; -.
DR OrthoDB; 9814936at2; -.
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; cd00974; DSRD; 1.
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; TIGR00319; desulf_FeS4; 1.
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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..36
FT /note="Desulfoferrodoxin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06397"
FT DOMAIN 42..123
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 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
SQ SEQUENCE 124 AA; 13509 MW; AB32763A1C9F3DE7 CRC64;
MAEALEIYKC GSCGNIVEVF HPGAGELVCC GAPMTLQKEN TVDASKEKHV PVIERGQGSI
TVKVGSIPHP MESAHYIEWI EVIADGKVYR AQLQPGQAPE ATFPVSAKEI KVREYCNMHG
QWSA
//
