ID   NUON_RUTMC              Reviewed;         484 AA.
AC   A1AVS5;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-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=Rmag_0250;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthturnera.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(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 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}.
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DR   EMBL; CP000488; ABL02032.1; -; Genomic_DNA.
DR   RefSeq; WP_011737657.1; NC_008610.1.
DR   AlphaFoldDB; A1AVS5; -.
DR   SMR; A1AVS5; -.
DR   STRING; 413404.Rmag_0250; -.
DR   KEGG; rma:Rmag_0250; -.
DR   eggNOG; COG1007; Bacteria.
DR   HOGENOM; CLU_007100_1_3_6; -.
DR   OrthoDB; 9768329at2; -.
DR   Proteomes; UP000002587; 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.
DR   PRINTS; PR01434; NADHDHGNASE5.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..484
FT                   /note="NADH-quinone oxidoreductase subunit N"
FT                   /id="PRO_0000391218"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        79..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ   SEQUENCE   484 AA;  53607 MW;  9B9CCABC3F131AD9 CRC64;
     MNNFIEFDTS SLWIALPEIF LLSAIVIVLL IDLFLDKNFK QVTYYLIQLS LFITGLLAFN
     LIDHPQIIIF GGSFVLDNMA SVFKVFMMAA TMVAMVYSRH YLRTHSLFRG EYFVLVLLSV
     LGMMVMVSGY SLLTLYLGLE ILSLSLYALI AIARERADAI EAALKYFVLG AIASGLLLYG
     MSMIYGISGS LNINDIASFA SNTNLDSRET LIINFGLVFL VIGIAFKLGA VPFHMWVPDV
     YQGAPTSVTL FISTVPKIAA FAMLVRILVD GLDSMHAYWS DLFMVLSILS IALGSVVALM
     QSNIKRMLAY STISHVGFIM LGFVAGTPIG YGAAAFYMLV YVLMSLAAFG MIILLNKQGF
     EIDQISDFKG LNKHAPWFAL MMLIIILSMA GVPPLVGFYS KFFILQQVVS AGFITIAVIV
     VIFAVISAYY YLQIIKSMYF DETDKKITIY ASIDIQLVLS INAILILAVG LFPDFWMKLA
     LSLF
//