ID NUON_AZOSB Reviewed; 491 AA. AC A1K5C1; DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 88. 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=azo1409; OS Azoarcus sp. (strain BH72). OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae; OC Azoarcus. OX NCBI_TaxID=418699; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72; RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. RT strain BH72."; RL Nat. Biotechnol. 24:1385-1391(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; AM406670; CAL94026.1; -; Genomic_DNA. DR RefSeq; WP_011765142.1; NC_008702.1. DR AlphaFoldDB; A1K5C1; -. DR SMR; A1K5C1; -. DR STRING; 62928.azo1409; -. DR KEGG; azo:azo1409; -. DR eggNOG; COG1007; Bacteria. DR HOGENOM; CLU_007100_1_3_4; -. DR Proteomes; UP000002588; 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 Gene3D; 1.10.287.3510; -; 1. 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. DR PRINTS; PR01434; NADHDHGNASE5. 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..491 FT /note="NADH-quinone oxidoreductase subunit N" FT /id="PRO_0000391101" FT TRANSMEM 11..31 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 38..58 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 74..94 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 106..126 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 128..148 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 163..183 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 243..263 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 272..292 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 301..321 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 336..356 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 379..399 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 410..430 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 465..485 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" SQ SEQUENCE 491 AA; 53128 MW; 5646C6FF251B4DA8 CRC64; MNFVVPDFYP ATAEIFVAVM ALVIMLATTF ARSVARGLAY GLTLVTLIGA AIITYNTANP RAVTTFSNMF IGDLLGDVLK LLIYFSMAVA LLYGRSYLAD RKLDKPEYYV LALLMTLGMM VMVTSNHLLS MYIGLELMSL SLYALVAFDR DSARGTEAAM KYFVLGALAS GLLLYGMSML YGATGTLEIS GIAKSVYNQA ANDTVLLFGL VFLMAGICFK LGVVPFHMWI PDVYHGANTA VTLIIATAPK LAAFAMAVRL LVWGLFDVAE HWQTMLMFVA VLSIVLGNLA AIAQTNLKRM LAYSGISHMG FMLLGLLSGV VDGDPHYALD AYSAAMFYAI SYVIMSLASF GMIILLSRAG FEAENIDDFK GLNKRSPWFA AMMMFVMFSM AGIPFFIGFF AKLAVLQAVV AAGYIWVAVV AVLMSVIGAF YYLRLVKVMY FDEPADATPI QAPAELRVFL SANGLAIAAI GLAPQGVMTL CTFVLLASTQ P //