RNFD_CLOLD
ID RNFD_CLOLD Reviewed; 331 AA.
AC D8GR67;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D {ECO:0000305};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000269|PubMed:23269825};
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:0000312|EMBL:ADK14205.1};
GN OrderedLocusNames=CLJU_c11370 {ECO:0000312|EMBL:ADK14205.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=23269825; DOI=10.1128/mbio.00406-12;
RA Tremblay P.L., Zhang T., Dar S.A., Leang C., Lovley D.R.;
RT "The Rnf complex of Clostridium ljungdahlii is a proton-translocating
RT ferredoxin:NAD+ oxidoreductase essential for autotrophic growth.";
RL MBio 4:E00406-E00412(2012).
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 translocation
CC of H(+) out of the cell. Essential for energy conservation during
CC autotrophic growth. Contributes to ATP synthesis during heterotrophic
CC growth. {ECO:0000269|PubMed:23269825}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00462};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00462}.
CC -!- INDUCTION: Up-regulated when grown on H(2)-CO(2).
CC {ECO:0000269|PubMed:23269825}.
CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC Rule:MF_00462}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001666; ADK14205.1; -; Genomic_DNA.
DR RefSeq; WP_013237802.1; NZ_LITS01000015.1.
DR AlphaFoldDB; D8GR67; -.
DR SMR; D8GR67; -.
DR STRING; 748727.CLJU_c11370; -.
DR EnsemblBacteria; ADK14205; ADK14205; CLJU_c11370.
DR KEGG; clj:CLJU_c11370; -.
DR PATRIC; fig|748727.19.peg.4235; -.
DR eggNOG; COG4658; Bacteria.
DR HOGENOM; CLU_042020_1_0_9; -.
DR OMA; GWQWINL; -.
DR OrthoDB; 1654433at2; -.
DR BRENDA; 7.1.1.11; 12866.
DR Proteomes; UP000001656; 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 2: Evidence at transcript level;
KW Cell membrane; Electron transport; Flavoprotein; FMN; Membrane; NAD;
KW Phosphoprotein; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..331
FT /note="Proton-translocating ferredoxin:NAD(+)
FT oxidoreductase complex subunit D"
FT /id="PRO_0000443491"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 84..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT MOD_RES 163
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
SQ SEQUENCE 331 AA; 35268 MW; 0E1D4ECFF2C44863 CRC64;
MAEAQIKKNI FTISSSPHVR CDESVSKIMW SVCLALTPAA VFGVFNFGIH ALEVIITGII
AAVVTEYFVE KVRNKPITIT DGSAFLTGLL LSMCLPPDIP PYMVAIGSFI AIAIAKHSMG
GLGQNIFNPA HIGRAALMVS WPVAMTTWSK LSASGVDAVT TATPLGILKL QGYSKLLETF
GGQGALYKAM FLGTRNGSIG ETSTILLVLG GLYLIYKKYI NWQIPVVMIG TVGILTWAFG
GTTGIFTGDP VFHMMAGGLV IGAFFMATDM VTIPMTIKGQ IIFALGAGAL TSLIRLKGGY
PEGVCYSILL MNAVTPLIDK FTQPVKFGTR R
