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RNFD_ACEWD
ID   RNFD_ACEWD              Reviewed;         318 AA.
AC   H6LC31; C4N8U1;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D {ECO:0000305};
DE            EC=7.2.1.2 {ECO:0000269|PubMed:20921383, ECO:0000269|PubMed:24045950};
DE   AltName: Full=Rnf electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
GN   Name=rnfD {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000303|PubMed:17873051};
GN   OrderedLocusNames=Awo_c22050 {ECO:0000312|EMBL:AFA48979.1};
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].
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=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00462};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00462,
CC       ECO:0000305|PubMed:20921383}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00462};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00462}.
CC   -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00462}.
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DR   EMBL; FJ416148; ACR23743.1; -; Genomic_DNA.
DR   EMBL; CP002987; AFA48979.1; -; Genomic_DNA.
DR   RefSeq; WP_014356579.1; NC_016894.1.
DR   AlphaFoldDB; H6LC31; -.
DR   SMR; H6LC31; -.
DR   STRING; 931626.Awo_c22050; -.
DR   TCDB; 3.D.6.1.2; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR   EnsemblBacteria; AFA48979; AFA48979; Awo_c22050.
DR   KEGG; awo:Awo_c22050; -.
DR   eggNOG; COG4658; Bacteria.
DR   HOGENOM; CLU_042020_1_0_9; -.
DR   OMA; GWQWINL; -.
DR   OrthoDB; 1654433at2; -.
DR   BioCyc; MetaCyc:MON-21342; -.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   HAMAP; MF_00462; RsxD_RnfD; 1.
DR   InterPro; IPR004338; NqrB/RnfD.
DR   InterPro; IPR011303; RnfD.
DR   PANTHER; PTHR30578; PTHR30578; 1.
DR   PANTHER; PTHR30578:SF0; PTHR30578:SF0; 1.
DR   Pfam; PF03116; NQR2_RnfD_RnfE; 1.
DR   TIGRFAMs; TIGR01946; rnfD; 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..318
FT                   /note="Na(+)-translocating ferredoxin:NAD(+) oxidoreductase
FT                   complex subunit D"
FT                   /id="PRO_0000443490"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        77..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   MOD_RES         156
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   CONFLICT        17..18
FT                   /note="KH -> NN (in Ref. 2; ACR23743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100..104
FT                   /note="VVGSV -> AVGSL (in Ref. 2; ACR23743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124..133
FT                   /note="PALAARAFLL -> TGTCCSSLFIG (in Ref. 2; ACR23743)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  33739 MW;  68DB88A038FB785C CRC64;
     MNELNLTVSS SPHIRAKHST ASIMQNVIIA LLPALAVAGY VFGLWALALV AICVISSVAT
     EAVIQKLLKK PITVNDWSAV VTGVLLAFNL PINAPWWIGV VGSVFAIAIV KQCFGGLGQN
     FINPALAARA FLLASWPGHM TSTAYIPLTD TVTTATPLAL LKAGETGSMP STLDLFTGLN
     GVYGCIGEIS ALALLIGGLY LIYKGIISWR IPTIYLLTIA IFALLVGQDP IVHMVSGGVM
     LGAFFMATDY ASSPVTAKGQ IIYAIGCGLI TMIIRLYGGY PEGCSYSILL MNVATPLIER
     FTKERIYGVT KIKKEAKA
 
 
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