RNFB_ACEWD
ID RNFB_ACEWD Reviewed; 333 AA.
AC H6LC27; C4N8U5;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B {ECO:0000305};
DE EC=7.2.1.2 {ECO:0000269|PubMed:20921383, ECO:0000269|PubMed:24045950};
DE AltName: Full=Rnf electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
GN Name=rnfB {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000303|PubMed:19222539};
GN OrderedLocusNames=Awo_c22010 {ECO:0000312|EMBL:AFA48975.1};
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=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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00463};
CC Note=Binds 7 [4Fe-4S] clusters. {ECO:0000305};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00463,
CC ECO:0000305|PubMed:20921383}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00463}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
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DR EMBL; FJ416148; ACR23747.1; -; Genomic_DNA.
DR EMBL; CP002987; AFA48975.1; -; Genomic_DNA.
DR RefSeq; WP_014356575.1; NC_016894.1.
DR AlphaFoldDB; H6LC27; -.
DR STRING; 931626.Awo_c22010; -.
DR TCDB; 3.D.6.1.2; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR EnsemblBacteria; AFA48975; AFA48975; Awo_c22010.
DR KEGG; awo:Awo_c22010; -.
DR eggNOG; COG1245; Bacteria.
DR eggNOG; COG2878; Bacteria.
DR HOGENOM; CLU_053470_0_0_9; -.
DR OMA; MLPGANC; -.
DR OrthoDB; 1619561at2; -.
DR BioCyc; MetaCyc:MON-21340; -.
DR BRENDA; 7.2.1.2; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00463; RsxB_RnfB; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB.
DR Pfam; PF00037; Fer4; 5.
DR Pfam; PF04060; FeS; 1.
DR PROSITE; PS51656; 4FE4S; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 6.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Reference proteome; Repeat; Translocase; Transport.
FT CHAIN 1..333
FT /note="Na(+)-translocating ferredoxin:NAD(+) oxidoreductase
FT complex subunit B"
FT /id="PRO_0000443517"
FT DOMAIN 33..92
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 126..162
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 163..192
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 207..237
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 239..266
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 270..299
FT /note="4Fe-4S ferredoxin-type 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 301..330
FT /note="4Fe-4S ferredoxin-type 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT REGION 1..27
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 182
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 217
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 220
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 249
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 252
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 279
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 282
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 289
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 310
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 333 AA; 34727 MW; 138977C70B402B87 CRC64;
MLNAILVPVG ILGVFGLIFG IGLAIAAKVF EVYEDPRVPL VRAALPGANC GGCGLPGCDA
LAANIVGGSA AIDACPVGGA SCAAAVAEIM GMEAGSAVKK VATVICQGTC ETAPNRAEYY
GEMDCREAMI ASGGSKGCRY GCLGYGTCKA VCPFDAIVIG EDGLPKVDPE KCTSCGKCVE
ACPKSIMTLV PEAQEVIVKC HNFDKGKIAR LSCTTACIAC GACVKACRFD AITVENNCAK
IDYDKCRQCY ECVDKCPMNC ISGDVEYGKS TAYIIEENCI ACGLCAKNCP VNAITGEIKK
PPYVIDHDMC IGCGICFDKC RKSAIEMRPN KTK
