ID NUON_AERHH Reviewed; 487 AA. AC A0KJ55; DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_00445}; DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445}; DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_00445}; DE AltName: Full=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_00445}; GN Name=nuoN {ECO:0000255|HAMAP-Rule:MF_00445}; GN OrderedLocusNames=AHA_1770; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / RC KCTC 2358 / NCIMB 9240 / NCTC 8049; RX PubMed=16980456; DOI=10.1128/jb.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."; RL J. Bacteriol. 188:8272-8282(2006). 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:0000255|HAMAP-Rule:MF_00445}. 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:0000255|HAMAP-Rule:MF_00445}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. CC {ECO:0000255|HAMAP-Rule:MF_00445}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00445}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000255|HAMAP-Rule:MF_00445}. 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; CP000462; ABK39107.1; -; Genomic_DNA. DR RefSeq; WP_011705656.1; NC_008570.1. DR RefSeq; YP_856306.1; NC_008570.1. DR AlphaFoldDB; A0KJ55; -. DR SMR; A0KJ55; -. DR STRING; 380703.AHA_1770; -. DR EnsemblBacteria; ABK39107; ABK39107; AHA_1770. DR KEGG; aha:AHA_1770; -. DR PATRIC; fig|380703.7.peg.1786; -. DR eggNOG; COG1007; Bacteria. DR HOGENOM; CLU_007100_1_5_6; -. DR OrthoDB; 9768329at2; -. DR Proteomes; UP000000756; Chromosome. 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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR HAMAP; MF_00445; NDH1_NuoN_1; 1. DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2. DR InterPro; IPR001750; ND/Mrp_mem. DR NCBIfam; TIGR01770; NDH_I_N; 1. DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1. DR PANTHER; PTHR22773:SF41; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1. DR Pfam; PF00361; Proton_antipo_M; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; KW Reference proteome; Translocase; Transmembrane; Transmembrane helix; KW Transport; Ubiquinone. FT CHAIN 1..487 FT /note="NADH-quinone oxidoreductase subunit N" FT /id="PRO_0000391091" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 37..57 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 71..91 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 104..124 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 125..145 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 159..179 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 203..223 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 235..255 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 269..289 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 303..323 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 327..347 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 374..394 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 408..427 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 449..469 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" SQ SEQUENCE 487 AA; 52486 MW; 55445AC63FC249F0 CRC64; MTFTASQLLA LLPLLLTTGA MVALMLAIAW KRCDDTAFVV TIAGLNLALF SLPIVMAQGD QGVTPLLQID GYAVFYMGLV LIGALATCTF GRSWLKGYPD NREEFYLLLL IATAGGLVLA GSRHLASLFI GIEMLTLPMF GLVGYAYRER HSLEASIKYM VLSAAATAFL LFGMALLYAQ AGSLSFSDLG LTLATTPAHH PLLMGGLGLM LVGFAFKLSL APFHLWTPDV YEGAPAPVAT FLATVSKIAV FCVLLRFYLA VPAAADPMIH WLLAAMAVIS IVIGNLLALL QTNIKRMMGY SSISHFGYLL AVIVASRLGQ MPVEAAGVYL LMYLFTSLGA FGVISMMSSP YRGKDADSLH SYRGLFWRRP YLTAVLTVMM LSLAGIPMTL GFIGKFYLIG VTVDAKLWWL SGAIVLGSAL GLYYYLRVMV TLYLREPGMQ LRDAKGDWAI TSGGLVVLLS AALVVALGLY PQPVISLVQG FQNVVLH //