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 01-MAY-2013, entry version 56. DE RecName: Full=NADH-quinone oxidoreductase subunit N; DE EC=1.6.99.5; DE AltName: Full=NADH dehydrogenase I subunit N; DE AltName: Full=NDH-1 subunit N; GN Name=nuoN; 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- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex (By similarity). CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. 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; YP_458209.1; NC_007722.1. DR STRING; 314225.ELI_06600; -. DR EnsemblBacteria; ABC63412; ABC63412; ELI_06600. DR GeneID; 3870384; -. DR KEGG; eli:ELI_06600; -. DR PATRIC; 21859772; VBIEryLit102657_1312. DR eggNOG; COG1007; -. DR HOGENOM; HOG000100795; -. DR KO; K00343; -. DR OMA; INIDSAY; -. DR ProtClustDB; PRK05777; -. DR BioCyc; ELIT314225:GHLE-1364-MONOMER; -. DR GO; GO:0016021; C:integral to 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 GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_00445; NDH1_NuoN_1; 1; -. DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2. DR InterPro; IPR001750; NADH_UbQ/plastoQ_OxRdtase. DR Pfam; PF00361; Oxidored_q1; 1. DR TIGRFAMs; TIGR01770; NDH_I_N; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Transmembrane; Transmembrane helix; KW Transport; Ubiquinone. FT CHAIN 1 487 NADH-quinone oxidoreductase subunit N. FT /FTId=PRO_0000391144. FT TRANSMEM 7 27 Helical; (Potential). FT TRANSMEM 37 57 Helical; (Potential). FT TRANSMEM 81 101 Helical; (Potential). FT TRANSMEM 112 132 Helical; (Potential). FT TRANSMEM 166 186 Helical; (Potential). FT TRANSMEM 207 227 Helical; (Potential). FT TRANSMEM 237 257 Helical; (Potential). FT TRANSMEM 276 296 Helical; (Potential). FT TRANSMEM 307 327 Helical; (Potential). FT TRANSMEM 329 349 Helical; (Potential). FT TRANSMEM 373 393 Helical; (Potential). FT TRANSMEM 407 427 Helical; (Potential). FT TRANSMEM 452 472 Helical; (Potential). 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 //