ID K0CC82_ALCDB Unreviewed; 448 AA.
AC K0CC82;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:AFT70115.1};
GN OrderedLocusNames=B5T_01840 {ECO:0000313|EMBL:AFT70115.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT70115.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT70115.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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; CP003466; AFT70115.1; -; Genomic_DNA.
DR RefSeq; WP_014994187.1; NC_018691.1.
DR AlphaFoldDB; K0CC82; -.
DR STRING; 930169.B5T_01840; -.
DR KEGG; adi:B5T_01840; -.
DR PATRIC; fig|930169.3.peg.1819; -.
DR eggNOG; COG1726; Bacteria.
DR HOGENOM; CLU_046656_0_0_6; -.
DR OrthoDB; 9774536at2; -.
DR Proteomes; UP000006286; 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 Reference proteome {ECO:0000313|Proteomes:UP000006286};
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 263..311
FT /note="Na(+)-translocating NADH-quinone reductase subunit A
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11973"
SQ SEQUENCE 448 AA; 48843 MW; DD2F36FEE0D9B4F5 CRC64;
MIKIKKGLDL PIAGAPRQAI EEGHQVRSVA VLGGDYVGMK PTMEVREGDQ VKKGQLIFTD
KKTDGVKYTA PAGGTVVAIN RGHKRVLQSV VIEVADQEEE VTFTAYQPDQ LASLDREAVV
SQLVDSGEWT LLRTRPFGKV PAPQSVPNSI FVTAIDTNPL CQDPSLVIQE NEQSFRHGLT
VLSRLTEGPV WVCKAAKSKL PSFAQGQIRE ESFAGKHPAG NPGTHVHFLD PVSLNKQVWT
VGYQEVIAIG KLFIEGRISS ERVVALGGPQ VKTPRLLRTR VGAQSDDFCR GELKDGENRV
ISGSVFNGHH ARGPVAHLGR LCNQVTVLRE GHERDLLGYV SPGTNRFSVM NIYLSRLMPG
KRFNFTTTTN GSERAMVPIG AYEEVMPLDI LPTQLLRALA VGDTDSASAL GALELVEEDL
ALCTFVCPGK YEYGPILRDN LTTIEVES
//