ID A9L283_SHEB9 Unreviewed; 457 AA.
AC A9L283;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=Sbal195_3685 {ECO:0000313|EMBL:ABX50846.1};
OS Shewanella baltica (strain OS195).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX50846.1, ECO:0000313|Proteomes:UP000000770};
RN [1] {ECO:0000313|EMBL:ABX50846.1, ECO:0000313|Proteomes:UP000000770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195 {ECO:0000313|EMBL:ABX50846.1,
RC ECO:0000313|Proteomes:UP000000770};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-2007) 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; CP000891; ABX50846.1; -; Genomic_DNA.
DR RefSeq; WP_006084043.1; NC_009997.1.
DR AlphaFoldDB; A9L283; -.
DR GeneID; 11773710; -.
DR KEGG; sbn:Sbal195_3685; -.
DR HOGENOM; CLU_046656_0_0_6; -.
DR Proteomes; UP000000770; Chromosome.
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 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 271..319
FT /note="Na(+)-translocating NADH-quinone reductase subunit A
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11973"
SQ SEQUENCE 457 AA; 49838 MW; 8ADD8398487F5D85 CRC64;
MADFSNQIVT IKKGLDLPIA GEPRQVIELG AKPSQVAVLG EEFVGLKPTM LVEEGDWVQK
GQALFEDKKT PGVLFTAPAS GQVVAINRGE RRILQSVVIR CDDGENRDGQ ISFEIHQDIA
ALGRSTVQAQ LVKSGLWTAL RTRPFSRVPA LDSTPAGIFV TAIDTNPLAA DPRLIIAEQT
EAFKVGLLVL SRLTEGKVYL CQDKGEAIVK EALPQLELRR FDGVHPAGLV GTHIHFTLPV
SLERQVWHIG YQDVIAYGKL FQTGELYTDR IVALGGPSVL NPRLLRTQLG AELSPLVSDD
IKPGQNRVVS GSVLSGHTAV GVHDFLGRFH NQVSVLSEDA QHHVLSWVRG GSDKFSITRA
VTSRLFGATK LFEFTTHQGG SARAMMAFGQ LDRVMPLDIL PTLLVRDLVV RDTDEAQALG
ALELDEEDLA LCTFVCPGKY DFGKELRACL DVIEREG
//