ID H2IP35_RAHAC Unreviewed; 147 AA. AC H2IP35; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 17-JUN-2020, entry version 50. DE RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NADH dehydrogenase I subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NDH-1 subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NUO1 {ECO:0000256|HAMAP-Rule:MF_01394}; GN Name=nuoA {ECO:0000256|HAMAP-Rule:MF_01394}; GN OrderedLocusNames=Rahaq2_1334 {ECO:0000313|EMBL:AEX51214.1}; OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / OS NCIMB 13365 / CIP 78.65). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Rahnella. OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX51214.1, ECO:0000313|Proteomes:UP000009010}; RN [1] {ECO:0000313|EMBL:AEX51214.1, ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RX PubMed=22582378; DOI=10.1128/JB.00380-12; RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S., RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S., RA Tapia R., Woyke T., Sobecky P.A.; RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65."; RL J. Bacteriol. 194:3020-3021(2012). RN [2] {ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., RA Martinez R., Woyke T.; RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be CC ubiquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01394, CC ECO:0000256|RuleBase:RU003639}; CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. CC {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01394}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01394}. Cell membrane {ECO:0000256|RuleBase:RU003639}; Multi- CC pass membrane protein {ECO:0000256|RuleBase:RU003639}. CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}. 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; CP003244; AEX51214.1; -; Genomic_DNA. DR RefSeq; WP_015696460.1; NZ_JMPO01000008.1. DR STRING; 745277.GRAQ_00371; -. DR EnsemblBacteria; AEX51214; AEX51214; Rahaq2_1334. DR KEGG; raq:Rahaq2_1334; -. DR PATRIC; fig|745277.3.peg.1270; -. DR eggNOG; ENOG4105KWU; Bacteria. DR eggNOG; COG0838; LUCA. DR HOGENOM; CLU_119549_2_1_6; -. DR OMA; YECGVDP; -. DR Proteomes; UP000009010; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.58.1610; -; 1. DR HAMAP; MF_01394; NDH1_NuoA; 1. DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid. DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3. DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf. DR PANTHER; PTHR11058; PTHR11058; 1. DR Pfam; PF00507; Oxidored_q4; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01394}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01394, KW ECO:0000256|RuleBase:RU003639}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01394}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01394}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000313|EMBL:AEX51214.1}. FT TRANSMEM 12..37 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394" FT TRANSMEM 68..87 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394" FT TRANSMEM 99..118 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394" SQ SEQUENCE 147 AA; 16133 MW; D6BB2E8539C5EE30 CRC64; MSMSTATEVI AQHWAFAVFL IVAMGLCCLM LLGAAFLGGR ARARYKNTPF ESGIASVGTA RLRLSAKFYL VAMFFVIFDV EALYLYAWST SIRESGWTGF VEATIFILVL LAGLFYLVRI GALDWTPTRS KGPVKPSPAI NTNSHPQ //