ID NUON_ERYLH Reviewed; 487 AA. AC Q2NA79; DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 17-JUN-2020, entry version 89. 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}; OrderedLocusNames=ELI_06600; OS Erythrobacter litoralis (strain HTCC2594). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=314225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2594; RX PubMed=19168610; DOI=10.1128/jb.00026-09; RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.; RT "Complete genome sequence of Erythrobacter litoralis HTCC2594."; RL J. Bacteriol. 191:2419-2420(2009). 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; CP000157; ABC63412.1; -; Genomic_DNA. DR RefSeq; WP_011414248.1; NC_007722.1. DR STRING; 314225.ELI_06600; -. DR EnsemblBacteria; ABC63412; ABC63412; ELI_06600. DR KEGG; eli:ELI_06600; -. DR eggNOG; ENOG4105CNR; Bacteria. DR eggNOG; COG1007; LUCA. DR HOGENOM; CLU_007100_1_3_5; -. DR KO; K00343; -. DR OMA; FYIRVIV; -. DR OrthoDB; 1664448at2; -. DR BioCyc; ELIT314225:G1G5F-1320-MONOMER; -. DR Proteomes; UP000008808; 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 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 Pfam; PF00361; Proton_antipo_M; 1. DR TIGRFAMs; TIGR01770; NDH_I_N; 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_0000391144" FT TRANSMEM 7..27 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 81..101 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 112..132 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 166..186 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 207..227 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 237..257 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 276..296 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 307..327 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 329..349 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 407..427 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 452..472 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" SQ SEQUENCE 487 AA; 50816 MW; 960143C306A107D5 CRC64; MELNASLTLI LPEIVMAISA MALILITAYV GDKTARLVSI LAAATLGAAA VMVAPALTSG ASGPDTVAFG GQFLADSFAS FAKILIYLSA IGCLMIAPAF FDRLKAMRPE YPVLVLLATL GMSIMVSAGD LITLYIGLEL NSLAAYVLAS FLRNDTRSAE AGLKYFVLGA LASGILLYGM SLVYGFTGTT DFEGVRGALT GDMSTGALFG VIFVLAGLAF KIAAVPFHMW TPDVYEGAPT PVTTFFATAP KVAAVALTAR VALSPFGEQT EAWQQIVIFA ALASIVLGAL GAIGQTNLKR LLAYSSINNV GFILIGLAAS TVAGLSAMLT YLAIYVVMAL GSFVALLMLK DEDGTPLETF DDIAGLSTTR PALAWCLLFL MFSLAGIPPL LGFWGKFVVF QAAVQADMVL LAALGIAASV IGAFYYIKFV KVMFFDDAVD RVKGTSDTAH WVLLILAAVV VSPLGYLLTG WLGGLTDSAA SALFIAS //