ID E1GYN6_9BACT Unreviewed; 452 AA.
AC E1GYN6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ECO:0000313|EMBL:EFN90216.1};
GN ORFNames=HMPREF9018_0050 {ECO:0000313|EMBL:EFN90216.1};
OS Prevotella amnii CRIS 21A-A.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=679191 {ECO:0000313|EMBL:EFN90216.1, ECO:0000313|Proteomes:UP000016016};
RN [1] {ECO:0000313|EMBL:EFN90216.1, ECO:0000313|Proteomes:UP000016016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIS 21A-A {ECO:0000313|EMBL:EFN90216.1,
RC ECO:0000313|Proteomes:UP000016016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (SEP-2010) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFN90216.1}.
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DR EMBL; ADFQ01000112; EFN90216.1; -; Genomic_DNA.
DR RefSeq; WP_008451314.1; NZ_ADFQ01000112.1.
DR AlphaFoldDB; E1GYN6; -.
DR eggNOG; COG1726; Bacteria.
DR Proteomes; UP000016016; 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 HAMAP; MF_00425; NqrA; 1.
DR InterPro; IPR008703; NqrA.
DR InterPro; IPR022615; NqrA_C_domain.
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.
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 Oxidoreductase {ECO:0000313|EMBL:EFN90216.1};
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 265..313
FT /note="Na(+)-translocating NADH-quinone reductase subunit A
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11973"
SQ SEQUENCE 452 AA; 50022 MW; 9F9DF71CF642D579 CRC64;
MANVIKLRKG LDINMKGRAL LQSLSKNIDE ACEYALSPDD FVGVTPKVVV KEGDHVLAGE
FLFVEKKYPE IGFASPVSGV ITSIVRGKRR KVLLVKVKPD KDQQYIDFGK KDISSLASED
IIKSIVDAGL FGYIQQLPYD ISVENMEVPK SIFISALRDK PLQGDFEFEL KGQEKEFQTG
LSALAKISKV YLGLGAKQTS SALISAKDVD INIFEGPCPA GNVGVQVNHI DPVNKGEKVW
TIDPTVVLFI GRLFNTGRVD LTRKIAIAGS MMKQTGYIDA LVGTPIKALI DKNIETNRKA
RLLKGNPLTG VIANTESFVG AHTSEITAIP EGDDINEFAG WIKPRLNMFS ISRSYFSWLF
GKKKEYDIDA RIKGSKRHII MSGEYDKVLP MNIYGEFLIK AIIVGNIDKQ EQLGIYEISP
EDFALAEFVD SSKLELQKIV RTGLDILRKE NA
//