DFX_DESVH
ID DFX_DESVH Reviewed; 126 AA.
AC P20418; Q9R523;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Desulfoferrodoxin;
DE Short=Dfx;
DE EC=1.15.1.2;
DE AltName: Full=Superoxide reductase;
DE Short=SOR;
GN Name=dfx; Synonyms=rbo; OrderedLocusNames=DVU_3183;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2549009; DOI=10.1128/jb.171.9.4996-5004.1989;
RA Brumlik M.J., Voordouw G.;
RT "Analysis of the transcriptional unit encoding the genes for rubredoxin
RT (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio
RT vulgaris Hildenborough.";
RL J. Bacteriol. 171:4996-5004(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-45, AND SPECTROSCOPIC STUDIES.
RX PubMed=2174880; DOI=10.1016/s0021-9258(18)45782-1;
RA Moura I., Tavares P., Moura J.J.G., Ravi N., Huynh B.H., Liu M.-Y.,
RA Le Gall J.;
RT "Purification and characterization of desulfoferrodoxin. A novel protein
RT from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio
RT vulgaris (strain Hildenborough) that contains a distorted rubredoxin center
RT and a mononuclear ferrous center.";
RL J. Biol. Chem. 265:21596-21602(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-16, COFACTOR, SUBUNIT, REDOX POTENTIAL, AND
RP SPECTROSCOPIC STUDIES.
RX PubMed=8262195; DOI=10.1016/0014-5793(93)81599-u;
RA Verhagen M.F.J.M., Voorhorst W.G.B., Kolkman J.A., Wolbert R.B.G.,
RA Hagen W.R.;
RT "On the two iron centers of desulfoferrodoxin.";
RL FEBS Lett. 336:13-18(1993).
RN [5]
RP ROLE IN OXIDATIVE STRESS.
RX PubMed=9687445; DOI=10.1128/aem.64.8.2882-2887.1998;
RA Voordouw J.K., Voordouw G.;
RT "Deletion of the rbo gene increases the oxygen sensitivity of the sulfate-
RT reducing bacterium Desulfovibrio vulgaris Hildenborough.";
RL Appl. Environ. Microbiol. 64:2882-2887(1998).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLU-47 AND LYS-48, KINETIC STUDIES, AND REACTION
RP MECHANISM.
RX PubMed=11914081; DOI=10.1021/bi0119159;
RA Emerson J.P., Coulter E.D., Cabelli D.E., Phillips R.S., Kurtz D.M. Jr.;
RT "Kinetics and mechanism of superoxide reduction by two-iron superoxide
RT reductase from Desulfovibrio vulgaris.";
RL Biochemistry 41:4348-4357(2002).
RN [7]
RP FUNCTION, ROLE IN OXIDATIVE STRESS, AND KINETIC STUDIES.
RX PubMed=12900405; DOI=10.1074/jbc.m306488200;
RA Emerson J.P., Coulter E.D., Phillips R.S., Kurtz D.M. Jr.;
RT "Kinetics of the superoxide reductase catalytic cycle.";
RL J. Biol. Chem. 278:39662-39668(2003).
RN [8]
RP SPECTROSCOPIC STUDIES.
RX PubMed=12764688; DOI=10.1007/s00775-003-0465-4;
RA Clay M.D., Emerson J.P., Coulter E.D., Kurtz D.M. Jr., Johnson M.K.;
RT "Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-
RT superoxide reductase from Desulfovibrio vulgaris.";
RL J. Biol. Inorg. Chem. 8:671-682(2003).
RN [9]
RP MUTAGENESIS OF CYS-13.
RX PubMed=12637682; DOI=10.1073/pnas.0537177100;
RA Emerson J.P., Cabelli D.E., Kurtz D.M. Jr.;
RT "An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site
RT retains its catalytic properties in vitro and in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3802-3807(2003).
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:0000269|PubMed:11914081,
CC ECO:0000269|PubMed:12900405, ECO:0000269|PubMed:9687445}.
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:0000250|UniProtKB:Q97GB9};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:8262195};
CC Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via
CC 4 cysteine residues. {ECO:0000269|PubMed:8262195};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:8262195};
CC Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via
CC four histidines and one cysteine residue. {ECO:0000269|PubMed:8262195};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +2 mV for center I and +90 mV for center II at pH 7.5.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8262195}.
CC -!- DOMAIN: Is organized in two protein domains. The N-terminal domain has
CC a fold similar to that of desulforedoxin and contains a mononuclear
CC Fe(3+) ion, center I. The second domain contains a different
CC mononuclear iron center, center II, with a Fe(2+) ion.
CC -!- MISCELLANEOUS: Catalysis occurs at center II. Fe(2+) ion of center II
CC is the electron donor and is converted to the Fe(3+) form during the
CC reaction.
CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a rubredoxin oxidoreductase.
CC {ECO:0000305|PubMed:2549009}.
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DR EMBL; M28848; AAA64797.1; -; Genomic_DNA.
DR EMBL; M81168; AAA23380.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS97653.1; -; Genomic_DNA.
DR PIR; A33962; RDDVBX.
DR RefSeq; WP_010940441.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_012393.1; NC_002937.3.
DR AlphaFoldDB; P20418; -.
DR SMR; P20418; -.
DR STRING; 882.DVU_3183; -.
DR PaxDb; P20418; -.
DR PRIDE; P20418; -.
DR EnsemblBacteria; AAS97653; AAS97653; DVU_3183.
DR KEGG; dvu:DVU_3183; -.
DR PATRIC; fig|882.5.peg.2888; -.
DR eggNOG; COG2033; Bacteria.
DR HOGENOM; CLU_118960_1_0_7; -.
DR OMA; EEKHYIQ; -.
DR PhylomeDB; P20418; -.
DR BRENDA; 1.15.1.2; 1914.
DR Proteomes; UP000002194; 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; cd00974; DSRD; 1.
DR Gene3D; 2.20.28.100; -; 1.
DR Gene3D; 2.60.40.730; -; 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 Pfam; PF06397; Desulfoferrod_N; 1.
DR Pfam; PF01880; Desulfoferrodox; 1.
DR SUPFAM; SSF49367; SSF49367; 1.
DR TIGRFAMs; TIGR00319; desulf_FeS4; 1.
DR TIGRFAMs; TIGR00320; dfx_rbo; 1.
DR TIGRFAMs; TIGR00332; neela_ferrous; 1.
PE 1: Evidence at protein level;
KW Detoxification; Direct protein sequencing; Electron transport; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2174880,
FT ECO:0000269|PubMed:8262195"
FT CHAIN 2..126
FT /note="Desulfoferrodoxin"
FT /id="PRO_0000140865"
FT BINDING 10
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 13
FT /note="C->S: No effect on activity. No iron present in
FT center I."
FT /evidence="ECO:0000269|PubMed:12637682"
FT MUTAGEN 47
FT /note="E->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11914081"
FT MUTAGEN 48
FT /note="K->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11914081"
SQ SEQUENCE 126 AA; 13983 MW; 4F0E96111A966A36 CRC64;
MPNQYEIYKC IHCGNIVEVL HAGGGDLVCC GEPMKLMKEG TSDGAKEKHV PVIEKTANGY
KVTVGSVAHP MEEKHWIEWI ELVADGVSYK KFLKPGDAPE AEFCIKADKV VAREYCNLHG
HWKAEA
