ID A3YDK9_9GAMM Unreviewed; 445 AA.
AC A3YDK9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=MED121_23424 {ECO:0000313|EMBL:EAQ64752.1};
OS Marinomonas sp. MED121.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ64752.1, ECO:0000313|Proteomes:UP000003436};
RN [1] {ECO:0000313|EMBL:EAQ64752.1, ECO:0000313|Proteomes:UP000003436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED121 {ECO:0000313|EMBL:EAQ64752.1,
RC ECO:0000313|Proteomes:UP000003436};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ64752.1}.
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DR EMBL; AANE01000010; EAQ64752.1; -; Genomic_DNA.
DR RefSeq; WP_009833697.1; NZ_CH672430.1.
DR AlphaFoldDB; A3YDK9; -.
DR STRING; 314277.MED121_23424; -.
DR HOGENOM; CLU_046656_0_0_6; -.
DR OrthoDB; 9774536at2; -.
DR Proteomes; UP000003436; 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 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:EAQ64752.1};
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 260..308
FT /note="Na(+)-translocating NADH-quinone reductase subunit A
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11973"
SQ SEQUENCE 445 AA; 48135 MW; A29FEDC0B2A6846C CRC64;
MFKITKGLDL PISGAPNQVI ENAPAARSVA VIGPDYHGMK PTMAVAVGDK VKKGQLLFTD
KKTEGVKYTA PAAGTIAAIN RGDKRVLQSV VIDVQGDEKE EFASFSGSEL KSLERQAVVT
NLIDSGLWTA FRTRPFSKVP EVASIPSSIF VTAMDTNPLA ASAEVVLADK AEAFADGLTV
LSRLTQGKVF LCKAPDTKIP STTDVSVQEF AGIHPAGLAG THIHFLDPVS DKKSVWSINY
QDVVAIGKLF VTGELDAERV ISLAGPQVVK PRLVRTQLGA NLDSLTSGEL LEGDNRIISG
SVLSGRKAFG PYAFLGRYHN QVVVIAEGRE RQMMHYLRAG VEKHSVLNVF WSKLTGKNNF
AMSSTTNGSD RTMLPLGHFE RLMPMDILPT QLLRSLVVKD TEQAQLLGAL ELDEEDLSLC
TYSCSGKFEY GPILRDCLTL IEKEG
//
