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NQRD_VIBAL
ID   NQRD_VIBAL              Reviewed;         210 AA.
AC   Q57095;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00428, ECO:0000303|PubMed:9490015};
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, ECO:0000269|PubMed:9490015};
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, ECO:0000303|PubMed:7805867};
GN   Synonyms=nqr4 {ECO:0000303|PubMed:7729558};
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 11038 / LMG 3418;
RX   PubMed=7805867; DOI=10.1016/0014-5793(94)01275-x;
RA   Beattie P., Tan K., Bourne R.M., Leach D.R.F., Rich P.R., Ward F.B.;
RT   "Cloning and sequencing of four structural genes for the Na(+)-
RT   translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus.";
RL   FEBS Lett. 356:333-338(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7729558; DOI=10.1016/0014-5793(95)00283-f;
RA   Hayashi M., Hirai K., Unemoto T.;
RT   "Sequencing and the alignment of structural genes in the nqr operon
RT   encoding the Na(+)-translocating NADH-quinone reductase from Vibrio
RT   alginolyticus.";
RL   FEBS Lett. 363:75-77(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-11, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=9490015; DOI=10.1016/s0014-5793(98)00016-7;
RA   Nakayama Y., Hayashi M., Unemoto T.;
RT   "Identification of six subunits constituting Na+-translocating NADH-quinone
RT   reductase from the marine Vibrio alginolyticus.";
RL   FEBS Lett. 422:240-242(1998).
RN   [4]
RP   INHIBITION OF ENZYMATIC ACTIVITY.
RX   PubMed=10549856; DOI=10.1248/bpb.22.1064;
RA   Nakayama Y., Hayashi M., Yoshikawa K., Mochida K., Unemoto T.;
RT   "Inhibitor studies of a new antibiotic, korormicin, 2-n-heptyl-4-
RT   hydroxyquinoline N-oxide and Ag+ toward the Na+-translocating NADH-quinone
RT   reductase from the marine Vibrio alginolyticus.";
RL   Biol. Pharm. Bull. 22:1064-1067(1999).
RN   [5]
RP   REVIEW.
RX   PubMed=11248187; DOI=10.1016/s0005-2728(00)00275-9;
RA   Hayashi M., Nakayama Y., Unemoto T.;
RT   "Recent progress in the Na(+)-translocating NADH-quinone reductase from the
RT   marine Vibrio alginolyticus.";
RL   Biochim. Biophys. Acta 1505:37-44(2001).
RN   [6]
RP   REVIEW.
RX   PubMed=11248188; DOI=10.1016/s0005-2728(00)00276-0;
RA   Steuber J.;
RT   "Na(+) translocation by bacterial NADH:quinone oxidoreductases: an
RT   extension to the complex-I family of primary redox pumps.";
RL   Biochim. Biophys. Acta 1505:45-56(2001).
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       ECO:0000305|PubMed:11248187, ECO:0000305|PubMed:11248188}.
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, ECO:0000269|PubMed:9490015};
CC   -!- ACTIVITY REGULATION: This reaction is tightly coupled to the Na(+)
CC       pumping activity and specifically requires Na(+) for activity.
CC       Inhibited by korormicin and 2-N-heptyl-4-hydroxyquinoline N-oxide
CC       (HQNO). {ECO:0000269|PubMed:10549856}.
CC   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC       NqrF. {ECO:0000255|HAMAP-Rule:MF_00428, ECO:0000269|PubMed:9490015}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00428, ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00428}.
CC   -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00428, ECO:0000305}.
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DR   EMBL; Z37111; CAA85479.1; -; Genomic_DNA.
DR   EMBL; AB008030; BAA22913.1; -; Genomic_DNA.
DR   PIR; S65529; S65529.
DR   RefSeq; WP_005380269.1; NZ_WAHT01000008.1.
DR   AlphaFoldDB; Q57095; -.
DR   SMR; Q57095; -.
DR   STRING; 663.BAU10_10825; -.
DR   TCDB; 3.D.5.1.1; the na(+)-translocating nadh:quinone dehydrogenase (na-ndh or nqr) family.
DR   GeneID; 61533194; -.
DR   eggNOG; COG1347; Bacteria.
DR   OrthoDB; 1782047at2; -.
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; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Ion transport; Membrane; NAD; Sodium; Sodium transport; Translocase;
KW   Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9490015"
FT   CHAIN           2..210
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   D"
FT                   /id="PRO_0000214239"
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   210 AA;  22602 MW;  00A85CA3D6C7DF3C CRC64;
     MSSAQNVKKS ILAPVLDNNP IALQVLGVCS ALAVTTKLET AFVMTLAVTF VTALSNFSVS
     LIRNHIPNSV RIIVQMAIIA SLVIVVDQVL KAYLYDISKQ LSVFVGLIIT NCIVMGRAEA
     FAMKSAPVPS LIDGIGNGLG YGFVLITVGF FRELFGSGKL FGLEVLPLVS NGGWYQPNGL
     MLLAPSAFFL IGFLIWVIRI LKPEQVEAKE
 
 
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