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Database: UniProt
Entry: A0A1H3Y7A0_9BACT
LinkDB: A0A1H3Y7A0_9BACT
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ID   A0A1H3Y7A0_9BACT        Unreviewed;       459 AA.
AC   A0A1H3Y7A0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE            Short=Na(+)-NQR subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE            Short=Na(+)-translocating NQR subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE            EC=7.2.1.1 {ECO:0000256|HAMAP-Rule:MF_00425};
DE   AltName: Full=NQR complex subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE   AltName: Full=NQR-1 subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
GN   Name=nqrA {ECO:0000256|HAMAP-Rule:MF_00425};
GN   ORFNames=SAMN04487851_102212 {ECO:0000313|EMBL:SEA07463.1};
OS   Prevotella sp. tc2-28.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1761888 {ECO:0000313|EMBL:SEA07463.1, ECO:0000313|Proteomes:UP000199625};
RN   [1] {ECO:0000313|EMBL:SEA07463.1, ECO:0000313|Proteomes:UP000199625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC2-28 {ECO:0000313|EMBL:SEA07463.1,
RC   ECO:0000313|Proteomes:UP000199625};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00425}.
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:0000256|HAMAP-
CC         Rule:MF_00425};
CC   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC       NqrF. {ECO:0000256|HAMAP-Rule:MF_00425}.
CC   -!- SIMILARITY: Belongs to the NqrA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00425}.
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DR   EMBL; FNRE01000002; SEA07463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3Y7A0; -.
DR   STRING; 1761888.SAMN04487851_102212; -.
DR   OrthoDB; 9774536at2; -.
DR   Proteomes; UP000199625; Unassembled WGS sequence.
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   Gene3D; 2.40.50.100; -; 1.
DR   HAMAP; MF_00425; NqrA; 1.
DR   InterPro; IPR008703; NqrA.
DR   InterPro; IPR022615; NqrA_C_domain.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01936; nqrA; 1.
DR   PANTHER; PTHR37839; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR37839:SF1; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT A; 1.
DR   Pfam; PF05896; NQRA; 1.
DR   Pfam; PF11973; NQRA_SLBB; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
PE   3: Inferred from homology;
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00425};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00425};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199625};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_00425};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201, ECO:0000256|HAMAP-
KW   Rule:MF_00425};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_00425};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00425};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW   Rule:MF_00425}.
FT   DOMAIN          268..316
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit A
FT                   C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11973"
SQ   SEQUENCE   459 AA;  50811 MW;  54D8E8B5051A5445 CRC64;
     MVNVIKLRKG LDINLKGKAE EKLIRLKSKG QYALVPDDFE GVTPKVVVKE GDHVKAGDAL
     FVNKMYPEVK FASPVSGTVR EVVRGERRKV LCVKVDADAQ QEHVDFGKRD VIAMDGKQVV
     DALLEAGIFG YINQLPYAVS TNPSVQPKAI FVSALRDKPL AGDFQFEVKE QEVDFVTGIM
     ALSKIAKTYV GLGIQPEFQS EIRKMGIDNY AQLTIFDGPC PAGNVGVQVN HLSPVNKGEV
     VWTIGDPTVV LFIGRLFNTG KVDLHRRVAL CGSEIKSPAY VDMLVGEELS TLLSNSYNAS
     HHVRIINGNV LTGRPTTKEG YLGAHTSEIT VIPEGDDANE LFGWILPRFK QFSVSRSYFS
     WLQNLGFGSK KNYALDARIK GGERHMIMSG EYDKVLPMDI YGEYLIKAII SGDIDRQEAL
     GIYEVSPEDF ALAEFVDSSK LELQRIVREG LNILRKENA
//
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