RUBR_CLOAB
ID RUBR_CLOAB Reviewed; 54 AA.
AC Q9AL94;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Rubredoxin;
DE Short=Rd;
DE EC=1.-.-.-;
GN Name=rd; OrderedLocusNames=CA_C2778;
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 [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11444870; DOI=10.1006/bbrc.2001.5196;
RA Guedon E., Petitdemange H.;
RT "Identification of the gene encoding NADH-rubredoxin oxidoreductase in
RT Clostridium acetobutylicum.";
RL Biochem. Biophys. Res. Commun. 285:496-502(2001).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, AND COFACTOR.
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 [4]
RP FUNCTION.
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 FUNCTION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19084524; DOI=10.1016/j.febslet.2008.12.004;
RA Hillmann F., Riebe O., Fischer R.J., Mot A., Caranto J.D., Kurtz D.M. Jr.,
RA Bahl H.;
RT "Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium
RT acetobutylicum.";
RL FEBS Lett. 583:241-245(2009).
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).
RN [7]
RP FUNCTION, AND COFACTOR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19118342; DOI=10.1099/mic.0.022756-0;
RA Riebe O., Fischer R.J., Wampler D.A., Kurtz D.M. Jr., Bahl H.;
RT "Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum.";
RL Microbiology 155:16-24(2009).
CC -!- FUNCTION: Rubredoxin is a small nonheme, iron protein lacking acid-
CC labile sulfide. Its single Fe, chelated to 4 Cys, functions as an
CC electron acceptor and may also stabilize the conformation of the
CC molecule. Functions as an intermediate component in the electron
CC transfer chain: NADH->NROR->Rd->FprA1/2 in which Rd serves as the
CC proximal electron donor to the FDPs that exhibit H(2)O-forming NADH
CC oxidase activity. Also functions as the proximal electron donor to the
CC Dfx and revRbr proteins that display superoxide reductase (SOR) and
CC NADH peroxidase activity, respectively. Therefore, is a key electron
CC carrier in an efficient multienzyme complex that can scavenge O(2) and
CC reactive oxygen species (ROS), and thus plays an important role in the
CC oxidative stress defense system in C.acetobutylicum, an obligate
CC anaerobic bacterium. {ECO:0000269|PubMed:18005665,
CC ECO:0000269|PubMed:19084524, ECO:0000269|PubMed:19118342,
CC ECO:0000269|PubMed:19124587}.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:19118342, ECO:0000269|PubMed:19124587};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:19118342,
CC ECO:0000269|PubMed:19124587};
CC -!- INDUCTION: Up-regulated upon exposure to O(2). Repressed by PerR.
CC {ECO:0000269|PubMed:19648241}.
CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR EMBL; AY026864; AAK07690.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK80722.1; -; Genomic_DNA.
DR PIR; G97241; G97241.
DR RefSeq; NP_349382.1; NC_003030.1.
DR RefSeq; WP_010966063.1; NC_003030.1.
DR AlphaFoldDB; Q9AL94; -.
DR SMR; Q9AL94; -.
DR STRING; 272562.CA_C2778; -.
DR EnsemblBacteria; AAK80722; AAK80722; CA_C2778.
DR GeneID; 44999264; -.
DR KEGG; cac:CA_C2778; -.
DR PATRIC; fig|272562.8.peg.2965; -.
DR eggNOG; COG1773; Bacteria.
DR HOGENOM; CLU_128747_3_3_9; -.
DR OMA; APKDMFE; -.
DR OrthoDB; 2047418at2; -.
DR SABIO-RK; Q9AL94; -.
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:0072592; P:oxygen metabolic process; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd00730; rubredoxin; 1.
DR InterPro; IPR024922; Rubredoxin.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR Pfam; PF00301; Rubredoxin; 1.
DR PIRSF; PIRSF000071; Rubredoxin; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR PROSITE; PS00202; RUBREDOXIN; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 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..54
FT /note="Rubredoxin"
FT /id="PRO_0000135029"
FT DOMAIN 1..54
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 6
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
SQ SEQUENCE 54 AA; 5930 MW; C59103B3FE41FAD8 CRC64;
MKKYVCVVCG YIYDPAEGDP DNGVNPGTSF EDIPDDWVCP LCGVGKDQFE PSEE
