RNFG_ACEWD
ID RNFG_ACEWD Reviewed; 207 AA.
AC H6LC30; C4N8U2;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G {ECO:0000305};
DE EC=7.2.1.2 {ECO:0000269|PubMed:20921383, ECO:0000269|PubMed:24045950};
DE AltName: Full=Rnf electron transport complex subunit G {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305};
GN Name=rnfG {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000303|PubMed:19222539};
GN OrderedLocusNames=Awo_c22040 {ECO:0000312|EMBL:AFA48978.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=19222539; DOI=10.1111/j.1462-2920.2009.01871.x;
RA Biegel E., Schmidt S., Muller V.;
RT "Genetic, immunological and biochemical evidence for a Rnf complex in the
RT acetogen Acetobacterium woodii.";
RL Environ. Microbiol. 11:1438-1443(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=20921383; DOI=10.1073/pnas.1010318107;
RA Biegel E., Mueller V.;
RT "Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18138-18142(2010).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=24045950; DOI=10.1074/jbc.m113.510255;
RA Hess V., Schuchmann K., Mueller V.;
RT "The ferredoxin:NAD+ oxidoreductase (Rnf) from the acetogen Acetobacterium
RT woodii requires Na+ and is reversibly coupled to the membrane potential.";
RL J. Biol. Chem. 288:31496-31502(2013).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane. Couples
CC electron transfer from reduced ferredoxin to NAD(+) with electrogenic
CC movement of Na(+) out of the cell. Involved in caffeate respiration.
CC {ECO:0000269|PubMed:20921383, ECO:0000269|PubMed:24045950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + Na(+)(in) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] =
CC Na(+)(out) + NADH + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:46800, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.2.1.2;
CC Evidence={ECO:0000269|PubMed:20921383, ECO:0000269|PubMed:24045950};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00479};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00479,
CC ECO:0000305|PubMed:20921383}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00479,
CC ECO:0000269|PubMed:19222539}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00479}.
CC -!- SIMILARITY: Belongs to the RnfG family. {ECO:0000255|HAMAP-
CC Rule:MF_00479}.
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DR EMBL; FJ416148; ACR23744.1; -; Genomic_DNA.
DR EMBL; CP002987; AFA48978.1; -; Genomic_DNA.
DR RefSeq; WP_014356578.1; NC_016894.1.
DR AlphaFoldDB; H6LC30; -.
DR SMR; H6LC30; -.
DR STRING; 931626.Awo_c22040; -.
DR TCDB; 3.D.6.1.2; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR EnsemblBacteria; AFA48978; AFA48978; Awo_c22040.
DR KEGG; awo:Awo_c22040; -.
DR eggNOG; COG4659; Bacteria.
DR HOGENOM; CLU_077882_2_1_9; -.
DR OMA; YSGAIHL; -.
DR OrthoDB; 1381933at2; -.
DR BioCyc; MetaCyc:MON-21344; -.
DR BRENDA; 7.2.1.2; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR HAMAP; MF_00479; RsxG_RnfG; 1.
DR InterPro; IPR007329; FMN-bd.
DR InterPro; IPR010209; Ion_transpt_RnfG/RsxG.
DR PANTHER; PTHR36118; PTHR36118; 1.
DR Pfam; PF04205; FMN_bind; 1.
DR PIRSF; PIRSF006091; E_trnsport_RnfG; 1.
DR SMART; SM00900; FMN_bind; 1.
DR TIGRFAMs; TIGR01947; rnfG; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; Flavoprotein; FMN; Membrane; NAD;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..207
FT /note="Na(+)-translocating ferredoxin:NAD(+) oxidoreductase
FT complex subunit G"
FT /id="PRO_0000443496"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00479"
FT MOD_RES 185
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00479"
SQ SEQUENCE 207 AA; 21832 MW; 5C01956DC96FB043 CRC64;
METKEKVQID WKVVFKLGLI LFVISAVAAC ALALTNYVTA GTIEEMNVQT NTVARQEVLP
KAADFEAVPA KDVEKIASEI GMEKPEELLE VYIGKSNGEV VGYTVKTGPT SGYAGEVQVL
TGISADGVIT GITIIKSNET PGLGAKASGV WNDQFTGKSA KEELVVVKGT TKEGSNEIQA
ITGSTITSKA VTSGVNMSIQ VYQNLSK
