DFX_CLOAB
ID DFX_CLOAB Reviewed; 125 AA.
AC Q97GB9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Desulfoferrodoxin;
DE Short=Dfx;
DE AltName: Full=Superoxide reductase;
DE Short=SOR;
DE EC=1.15.1.2;
GN Name=dfx; Synonyms=dsr; OrderedLocusNames=CA_C2450;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP INDUCTION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19124587; DOI=10.1128/aem.01425-08;
RA Kawasaki S., Sakai Y., Takahashi T., Suzuki I., Niimura Y.;
RT "O2 and reactive oxygen species detoxification complex, composed of O2-
RT responsive NADH:rubredoxin oxidoreductase-flavoprotein A2-desulfoferrodoxin
RT operon enzymes, rubperoxin, and rubredoxin, in Clostridium
RT acetobutylicum.";
RL Appl. Environ. Microbiol. 75:1021-1029(2009).
RN [3]
RP INDUCTION BY LOW LEVELS OF OXYGEN.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=16332833; DOI=10.1128/aem.71.12.8442-8450.2005;
RA Kawasaki S., Watamura Y., Ono M., Watanabe T., Takeda K., Niimura Y.;
RT "Adaptive responses to oxygen stress in obligatory anaerobes Clostridium
RT acetobutylicum and Clostridium aminovalericum.";
RL Appl. Environ. Microbiol. 71:8442-8450(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=18005665; DOI=10.1016/j.febslet.2007.11.008;
RA Riebe O., Fischer R.J., Bahl H.;
RT "Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide
RT reductase.";
RL FEBS Lett. 581:5605-5610(2007).
RN [5]
RP REPRESSION BY PERR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=18430081; DOI=10.1111/j.1365-2958.2008.06192.x;
RA Hillmann F., Fischer R.J., Saint-Prix F., Girbal L., Bahl H.;
RT "PerR acts as a switch for oxygen tolerance in the strict anaerobe
RT Clostridium acetobutylicum.";
RL Mol. Microbiol. 68:848-860(2008).
RN [6]
RP INDUCTION BY O(2), AND REPRESSION BY PERR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19648241; DOI=10.1128/jb.00351-09;
RA Hillmann F., Doring C., Riebe O., Ehrenreich A., Fischer R.J., Bahl H.;
RT "The role of PerR in O2-affected gene expression of Clostridium
RT acetobutylicum.";
RL J. Bacteriol. 191:6082-6093(2009).
CC -!- FUNCTION: Catalyzes the reduction of superoxide to hydrogen peroxide,
CC using electrons from NADH and NADH:rubredoxin oxidoreductase (NROR) and
CC rubredoxin (Rd) as electron transport intermediaries between NADH and
CC Dfx. Is a key factor in the superoxide reductase dependent part of a
CC pathway for detoxification of reactive oxygen species (ROS) in
CC C.acetobutylicum, an obligate anaerobic bacterium.
CC {ECO:0000269|PubMed:18005665, ECO:0000269|PubMed:19124587}.
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:0000269|PubMed:18005665, ECO:0000269|PubMed:19124587};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:18005665, ECO:0000269|PubMed:19124587,
CC ECO:0000305};
CC Note=Binds 1 Fe(2+) ion per subunit. In contrast to some other SORs,
CC does not bind a second iron ion. {ECO:0000269|PubMed:18005665,
CC ECO:0000269|PubMed:19124587, ECO:0000305};
CC -!- INDUCTION: Up-regulated after exposure to oxygen stress (at both
CC transcript and protein levels). Repressed by PerR.
CC {ECO:0000269|PubMed:16332833, ECO:0000269|PubMed:18005665,
CC ECO:0000269|PubMed:18430081, ECO:0000269|PubMed:19124587,
CC ECO:0000269|PubMed:19648241}.
CC -!- MISCELLANEOUS: The SOR reaction is believed to be advantageous to
CC anaerobic bacteria, in comparison to SOD (superoxide dismutase),
CC because SOR produces no oxygen by reducing superoxide.
CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family. {ECO:0000305}.
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DR EMBL; AE001437; AAK80404.1; -; Genomic_DNA.
DR PIR; A97202; A97202.
DR RefSeq; NP_349064.1; NC_003030.1.
DR RefSeq; WP_010965745.1; NC_003030.1.
DR AlphaFoldDB; Q97GB9; -.
DR SMR; Q97GB9; -.
DR STRING; 272562.CA_C2450; -.
DR EnsemblBacteria; AAK80404; AAK80404; CA_C2450.
DR GeneID; 44998928; -.
DR KEGG; cac:CA_C2450; -.
DR PATRIC; fig|272562.8.peg.2646; -.
DR eggNOG; COG2033; Bacteria.
DR HOGENOM; CLU_118960_1_0_9; -.
DR OMA; EEKHYIQ; -.
DR OrthoDB; 1496450at2; -.
DR BRENDA; 1.15.1.2; 1452.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016721; F:oxidoreductase activity, acting on superoxide radicals as acceptor; IDA:UniProtKB.
DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:UniProtKB.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:UniProtKB.
DR Gene3D; 2.60.40.730; -; 1.
DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom.
DR InterPro; IPR036073; Desulfoferrodoxin_Fe-bd_dom_sf.
DR Pfam; PF01880; Desulfoferrodox; 1.
DR SUPFAM; SSF49367; SSF49367; 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; Stress response;
KW Transport.
FT CHAIN 1..125
FT /note="Desulfoferrodoxin"
FT /id="PRO_0000403463"
FT BINDING 49
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 125 AA; 13677 MW; 3BF9EAA5802D927F CRC64;
MNNDLSIYVS KNSGTAVLLL QGNGTDLTCG SEPMAKIVAN TTDAAQEKHV PHITKNGNNI
DVSVGSVEHP MTPEHFIEWI ILVSGDRLEM AKLTPDMKPR AQFHNVTSGT VYAYCNLHSL
WKADI
