ID NQRA_VIBAL Reviewed; 446 AA. AC Q56586; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-JUL-2017, entry version 76. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit A {ECO:0000255|HAMAP-Rule:MF_00425, ECO:0000303|PubMed:9490015}; DE Short=Na(+)-NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE Short=Na(+)-translocating NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00425, ECO:0000269|PubMed:9490015}; DE AltName: Full=NQR complex subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE AltName: Full=NQR-1 subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; GN Name=nqrA {ECO:0000255|HAMAP-Rule:MF_00425, GN ECO:0000303|PubMed:7805867}; GN Synonyms=nqr1 {ECO:0000303|PubMed:9490015}; OS Vibrio alginolyticus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=663; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10. RC STRAIN=NCIMB 11038; RX PubMed=7805867; DOI=10.1016/0014-5793(94)01275-X; RA Beattie P., Tan K., Bourne R.M., Leach D.R.F., Rich P.R., Ward F.B.; RT "Cloning and sequencing of four structural genes for the Na(+)- RT translocating NADH-ubiquinone oxidoreductase of Vibrio RT alginolyticus."; RL FEBS Lett. 356:333-338(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Hayashi M., Unemoto T., Sugiyama A.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=9490015; DOI=10.1016/S0014-5793(98)00016-7; RA Nakayama Y., Hayashi M., Unemoto T.; RT "Identification of six subunits constituting Na+-translocating NADH- RT quinone reductase from the marine Vibrio alginolyticus."; RL FEBS Lett. 422:240-242(1998). RN [4] RP PROTEIN SEQUENCE OF 1-9 AND 334-340. RX PubMed=7805866; DOI=10.1016/0014-5793(94)01274-1; RA Hayashi M., Hirai K., Unemoto T.; RT "Cloning of the Na(+)-translocating NADH-quinone reductase gene from RT the marine bacterium Vibrio alginolyticus and the expression of the RT beta-subunit in Escherichia coli."; RL FEBS Lett. 356:330-332(1994). RN [5] RP INHIBITION OF ENZYMATIC ACTIVITY. RX PubMed=10549856; DOI=10.1248/bpb.22.1064; RA Nakayama Y., Hayashi M., Yoshikawa K., Mochida K., Unemoto T.; RT "Inhibitor studies of a new antibiotic, korormicin, 2-n-heptyl-4- RT hydroxyquinoline N-oxide and Ag+ toward the Na+-translocating NADH- RT quinone reductase from the marine Vibrio alginolyticus."; RL Biol. Pharm. Bull. 22:1064-1067(1999). RN [6] RP REVIEW. RX PubMed=11248187; DOI=10.1016/S0005-2728(00)00275-9; RA Hayashi M., Nakayama Y., Unemoto T.; RT "Recent progress in the Na(+)-translocating NADH-quinone reductase RT from the marine Vibrio alginolyticus."; RL Biochim. Biophys. Acta 1505:37-44(2001). RN [7] RP REVIEW. RX PubMed=11248188; DOI=10.1016/S0005-2728(00)00276-0; RA Steuber J.; RT "Na(+) translocation by bacterial NADH:quinone oxidoreductases: an RT extension to the complex-I family of primary redox pumps."; RL Biochim. Biophys. Acta 1505:45-56(2001). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00425, CC ECO:0000305|PubMed:11248187, ECO:0000305|PubMed:11248188}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00425, CC ECO:0000269|PubMed:9490015}. CC -!- ENZYME REGULATION: This reaction is tightly coupled to the Na(+) CC pumping activity and specifically requires Na(+) for activity. CC Inhibited by korormicin and 2-N-heptyl-4-hydroxyquinoline N-oxide CC (HQNO). {ECO:0000269|PubMed:10549856}. CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00425, CC ECO:0000269|PubMed:9490015}. CC -!- SIMILARITY: Belongs to the NqrA family. {ECO:0000255|HAMAP- CC Rule:MF_00425, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z37111; CAA85476.1; -; Genomic_DNA. DR EMBL; AB008030; BAA22910.1; -; Genomic_DNA. DR PIR; S51015; S51015. DR RefSeq; WP_041853022.1; NZ_MAKC01000057.1. DR SMR; Q56586; -. DR TCDB; 3.D.5.1.1; the na(+)-translocating nadh:quinone dehydrogenase (na-ndh or nqr) family. DR eggNOG; ENOG4105DWQ; Bacteria. DR eggNOG; COG1726; LUCA. DR BRENDA; 1.6.5.8; 6624. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB. DR GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR HAMAP; MF_00425; NqrA; 1. DR InterPro; IPR008703; NqrA. DR InterPro; IPR022615; NqrA_C_domain. DR PANTHER; PTHR37839; PTHR37839; 1. DR Pfam; PF05896; NQRA; 1. DR Pfam; PF11973; NQRA_SLBB; 1. DR TIGRFAMs; TIGR01936; nqrA; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Ion transport; NAD; Oxidoreductase; Sodium; KW Sodium transport; Transport; Ubiquinone. FT CHAIN 1 446 Na(+)-translocating NADH-quinone FT reductase subunit A. FT /FTId=PRO_0000214203. FT CONFLICT 337 337 W -> L (in Ref. 4; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 446 AA; 48623 MW; 6D65ACAA53FE515C CRC64; MITIKKGLDL PIAGTPSQVI NDGKTIKKVA LLGEEYVGMR PTMHVRVGDE VKKAQVLFED KKNPGVKFTA PAAGKVIEVN RGAKRVLQSV VIEVAGEEQV TFDKFEAAQL SGLDREVIKT QLVDSGLWTA LRTRPFSKVP AIESSTKAIF VTAMDTNPLA AKPELIINEQ QEAFIAGLDI LSALTEGKVY VCKSGTSLPR SSQSNVEEHV FDGPHPAGLA GTHMHFLYPV NAENVAWSIN YQDVIAFGKL FLTGELYTDR VVSLAGPVVN NPRLVRTVIG ASLDDLTDNE LMPGEVRVIS GSVLTGTHAT GPHAYLGRYH QQVSVLREGR EKELFGWAMP GKNKFSVTRS FLGHVFKGQL FNMTTTTNGS DRSMVPIGNY ERVMPLDMEP TLLLRDLCAG DTDSAQALGA LELDEEDLAL CTFVCPGKYE YGTLLRECLD TIEKEG //