RNFC_ACEWD
ID RNFC_ACEWD Reviewed; 443 AA.
AC H6LC32; C4N8U0;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C {ECO:0000305};
DE EC=7.2.1.2 {ECO:0000269|PubMed:20921383, ECO:0000269|PubMed:24045950};
DE AltName: Full=Rnf electron transport complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
GN Name=rnfC {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000303|PubMed:17873051};
GN OrderedLocusNames=Awo_c22060 {ECO:0000312|EMBL:AFA48980.1};
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].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=17873051; DOI=10.1128/jb.01017-07;
RA Imkamp F., Biegel E., Jayamani E., Buckel W., Muller V.;
RT "Dissection of the caffeate respiratory chain in the acetogen
RT Acetobacterium woodii: identification of an Rnf-type NADH dehydrogenase as
RT a potential coupling site.";
RL J. Bacteriol. 189:8145-8153(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 130-144, AND
RP 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 [3]
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 [4]
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 [5]
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00461};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00461};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00461,
CC ECO:0000305|PubMed:20921383}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00461,
CC ECO:0000269|PubMed:19222539}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00461}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
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DR EMBL; FJ416148; ACR23742.1; -; Genomic_DNA.
DR EMBL; CP002987; AFA48980.1; -; Genomic_DNA.
DR RefSeq; WP_014356580.1; NC_016894.1.
DR AlphaFoldDB; H6LC32; -.
DR SMR; H6LC32; -.
DR STRING; 931626.Awo_c22060; -.
DR TCDB; 3.D.6.1.2; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR EnsemblBacteria; AFA48980; AFA48980; Awo_c22060.
DR KEGG; awo:Awo_c22060; -.
DR eggNOG; COG4656; Bacteria.
DR HOGENOM; CLU_010808_6_0_9; -.
DR OMA; QQLYWYS; -.
DR OrthoDB; 688908at2; -.
DR BioCyc; MetaCyc:MON-21341; -.
DR BRENDA; 7.2.1.2; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11540; -; 1.
DR HAMAP; MF_00461; RsxC_RnfC; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010208; Ion_transpt_RnfC/RsxC.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR026902; RnfC_N.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR PANTHER; PTHR43034; PTHR43034; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF13375; RnfC_N; 1.
DR Pfam; PF10531; SLBB; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01945; rnfC; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; NAD; Reference proteome; Repeat;
KW Translocase; Transport.
FT CHAIN 1..443
FT /note="Na(+)-translocating ferredoxin:NAD(+) oxidoreductase
FT complex subunit C"
FT /id="PRO_0000443486"
FT DOMAIN 359..391
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT DOMAIN 398..428
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 369
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 372
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 375
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 379
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 408
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 411
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 414
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 418
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
SQ SEQUENCE 443 AA; 47120 MW; 1C06B339CB7BAA16 CRC64;
MNVKHGTFKG GIHPPYRKES TAEVPLGFGK KPEMVIIPMS LHIGAPCTPI VKKGDTVFLG
QRVGEPNGFV SVPVHASVSG KVIAVEERPH ASGDRVMSVV IESDGLDTID PSIKPYGTLE
DMDADAIKKM VLNAGIVGLG GATFPTHVKL AIPPDKKVDC VVLNGAECEP YLTADHHLMT
SQAEKVVMGL KLAMKSVGVE KGFIGVEDNK TDAIEALVKA IGNDSRLEVY SLHTKYPQGA
EKQLIAAITG REVPSGALPA DAGVVVMNVG TAAQIAESMI TGLPLYKRYL TCTGDAIKNP
QTIEIRIGVP FQSVIDQCGG FSSEPGKVIS GGPMMGVTQF VTDIPVMKGT SGILCLTKES
AKIATPSNCI HCGKCVGVCP IHLQPLNIAE YSQRNMWDKC ESNNAMDCIE CGSCSYICPA
KRTLVSSIRV AKREIIAQRR KGN
