ID NUON_ECOK1 Reviewed; 485 AA. AC A1ADC4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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=Ecok1_21700; ORFNames=APECO1_4289; OS Escherichia coli O1:K1 / APEC. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=405955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17293413; DOI=10.1128/jb.01726-06; RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.; RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 RT shares strong similarities with human extraintestinal pathogenic E. coli RT genomes."; RL J. Bacteriol. 189:3228-3236(2007). 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 13 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; CP000468; ABJ01664.1; -; Genomic_DNA. DR RefSeq; WP_000156712.1; NZ_CADILS010000025.1. DR AlphaFoldDB; A1ADC4; -. DR SMR; A1ADC4; -. DR KEGG; ecv:APECO1_4289; -. DR HOGENOM; CLU_007100_1_5_6; -. DR Proteomes; UP000008216; 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..485 FT /note="NADH-quinone oxidoreductase subunit N" FT /id="PRO_1000017376" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 35..55 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 105..125 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 127..147 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 271..291 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 297..317 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 326..346 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 373..393 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 408..430 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 455..475 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" SQ SEQUENCE 485 AA; 52072 MW; BFBFAEF428B0FA09 CRC64; MTITPQNLIA LLPLLIVGLT VVVVMLSIAW RRNHFLNATL SVIGLNAALV SLWFVGQAGA MDVTPLMRVD GFAMLYTGLV LLASLATCTF AYPWLEGYND NKDEFYLLVL IAALGGILLA NANHLASLFL GIELISLPLF GLVGYAFRQK RSLEASIKYT ILSAAASSFL LFGMALVYAQ SGDLSFVALG KNLGDGMLNE PLLLAGFGLM IVGLGFKLSL VPFHLWTPDV YQGAPAPVST FLATASKIAI FGVVMRLFLY APVGDSEAIR VVLAIIAFAS IIFGNLMALS QTNIKRLLGY SSISHLGYLL VALIALQTGE MSMEAVGVYL VGYLFSSLGA FGVVSLMSSP YRGPDADSLF SYRGLFWHRP ILAAVMTVMM LSLAGIPMTL GFIGKFYVLA VGVQAHLWWL VGAVVVGSAI GLYYYLRVAV SLYLHAPEQP GRDAPSNWQY SAGGIVVLIS ALLVLVLGVW PQPLISIVRL AMPLM //