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Database: UniProt
Entry: H6LC32
LinkDB: H6LC32
Original site: H6LC32 
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   16-JAN-2019, entry version 54.
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,
GN   ECO:0000303|PubMed:17873051};
GN   OrderedLocusNames=Awo_c22060 {ECO:0000312|EMBL:AFA48980.1};
OS   Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC
OS   1655 / WB1).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; 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
RT   dehydrogenase as 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
RT   the 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
RT   Acetobacterium woodii requires Na+ and is reversibly coupled to the
RT   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
CC       electrogenic movement of Na(+) out of the cell. Involved in
CC       caffeate respiration. {ECO:0000269|PubMed:20921383,
CC       ECO:0000269|PubMed:24045950}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + Na(+)(in) + NAD(+) + 2 reduced [2Fe-2S]-
CC         [ferredoxin] = Na(+)(out) + NADH + 2 oxidized [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:46800, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=7.2.1.2;
CC         Evidence={ECO:0000269|PubMed:20921383,
CC         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,
CC       RnfC, RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00461,
CC       ECO:0000305|PubMed:20921383}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00461, ECO:0000269|PubMed:19222539}; Peripheral membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_00461}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family.
CC       RnfC subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
DR   EMBL; FJ416148; ACR23742.1; -; Genomic_DNA.
DR   EMBL; CP002987; AFA48980.1; -; Genomic_DNA.
DR   RefSeq; WP_014356580.1; NC_016894.1.
DR   ProteinModelPortal; H6LC32; -.
DR   STRING; 931626.Awo_c22060; -.
DR   TCDB; 3.D.6.1.2; the putative 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; ENOG4107QTR; Bacteria.
DR   eggNOG; COG4656; LUCA.
DR   KO; K03615; -.
DR   OMA; QQLYWYS; -.
DR   OrthoDB; 688908at2; -.
DR   BioCyc; AWOO931626:G1H37-2281-MONOMER; -.
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; 1.10.1060.10; -; 1.
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; IPR009051; Helical_ferredxn.
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   SUPFAM; SSF46548; SSF46548; 1.
DR   TIGRFAMs; TIGR01945; rnfC; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cell membrane; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW   Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN         1    443       Na(+)-translocating ferredoxin:NAD(+)
FT                                oxidoreductase complex subunit C.
FT                                /FTId=PRO_0000443486.
FT   DOMAIN      359    391       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   DOMAIN      398    428       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       369    369       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       372    372       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       375    375       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       379    379       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       408    408       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       411    411       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       414    414       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       418    418       Iron-sulfur 1 (4Fe-4S).
FT                                {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
//
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