NQRD_HAEIE
ID NQRD_HAEIE Reviewed; 208 AA.
AC A5UAX4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE Short=Na(+)-NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE Short=Na(+)-translocating NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00428};
DE AltName: Full=NQR complex subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE AltName: Full=NQR-1 subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
GN Name=nqrD {ECO:0000255|HAMAP-Rule:MF_00428};
GN OrderedLocusNames=CGSHiEE_02370;
OS Haemophilus influenzae (strain PittEE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374930;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittEE;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC ubiquinol by two successive reactions, coupled with the transport of
CC Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are
CC probably involved in the second step, the conversion of ubisemiquinone
CC to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00428}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n
CC Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00428};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00428}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00428}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00428}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00428}.
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DR EMBL; CP000671; ABQ97925.1; -; Genomic_DNA.
DR RefSeq; WP_005648665.1; NC_009566.1.
DR AlphaFoldDB; A5UAX4; -.
DR SMR; A5UAX4; -.
DR KEGG; hip:CGSHiEE_02370; -.
DR HOGENOM; CLU_046659_1_1_6; -.
DR OMA; CIIMGRF; -.
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:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00428; NqrD; 1.
DR InterPro; IPR011292; NqrD.
DR InterPro; IPR003667; NqrDE/RnfAE.
DR PANTHER; PTHR30586:SF1; PTHR30586:SF1; 1.
DR Pfam; PF02508; Rnf-Nqr; 1.
DR PIRSF; PIRSF006102; NQR_DE; 1.
DR TIGRFAMs; TIGR01939; nqrD; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; NAD; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..208
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT D"
FT /id="PRO_1000060153"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
SQ SEQUENCE 208 AA; 22528 MW; EC988B5A1BC87C79 CRC64;
MSGKTSYKDL LLAPIAKNNP IALQILGICS ALAVTTKLET AFVMAIAVTL VTGLSNLFVS
LIRNYIPNSI RIIVQLAIIA SLVIVVDQIL KAYAYGLSKQ LSVFVGLIIT NCIVMGRAEA
FAMKSPPVES FVDGIGNGLG YGSMLIIVAF FRELIGSGKL FGMTIFETIQ NGGWYQANGL
FLLAPSAFFI IGFVIWGLRT WKPEQQEK
