ID   NUON_PARDP              Reviewed;         499 AA.
AC   A1B479;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=NADH-quinone oxidoreductase subunit N;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit 14;
DE   AltName: Full=NADH dehydrogenase I subunit N;
DE   AltName: Full=NADH-quinone oxidoreductase subunit 14;
DE            Short=NQO14;
DE   AltName: Full=NDH-1 subunit 14;
DE   AltName: Full=NDH-1 subunit N;
GN   Name=nuoN; Synonyms=nqo14 {ECO:0000303|PubMed:14610094};
GN   OrderedLocusNames=Pden_2231;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION IN NADH OXIDASE SUPERCOMPLEX, FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=14610094; DOI=10.1074/jbc.m309505200;
RA   Stroh A., Anderka O., Pfeiffer K., Yagi T., Finel M., Ludwig B.,
RA   Schagger H.;
RT   "Assembly of respiratory complexes I, III, and IV into NADH oxidase
RT   supercomplex stabilizes complex I in Paracoccus denitrificans.";
RL   J. Biol. Chem. 279:5000-5007(2004).
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:0000305|PubMed:14610094}.
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   -!- SUBUNIT: NDH-1 is composed of at least 14 different subunits, Nqo1 to
CC       Nqo14. The complex has a L-shaped structure, with the hydrophobic arm
CC       (subunits Nqo7, Nqo8, Nqo10 to Nqo14) embedded in the inner membrane
CC       and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9)
CC       protruding into the bacterial cytoplasm. The hydrophilic domain
CC       contains all the redox centers (By similarity). NADH-quinone
CC       oxidoreductase forms a supercomplex with ubiquinol-cytochrome c
CC       reductase complex (complex III or cytochrome b-c1 complex) and
CC       cytochrome c oxidase (complex IV), which stabilizes the NADH-quinone
CC       oxidoreductase complex (PubMed:14610094). {ECO:0000250,
CC       ECO:0000269|PubMed:14610094}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:14610094}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:14610094}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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; CP000489; ABL70323.1; -; Genomic_DNA.
DR   RefSeq; WP_011748518.1; NC_008686.1.
DR   AlphaFoldDB; A1B479; -.
DR   SMR; A1B479; -.
DR   STRING; 318586.Pden_2231; -.
DR   EnsemblBacteria; ABL70323; ABL70323; Pden_2231.
DR   GeneID; 75501710; -.
DR   KEGG; pde:Pden_2231; -.
DR   eggNOG; COG1007; Bacteria.
DR   HOGENOM; CLU_007100_1_3_5; -.
DR   OrthoDB; 9811718at2; -.
DR   Proteomes; UP000000361; Chromosome 1.
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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   CHAIN           1..499
FT                   /note="NADH-quinone oxidoreductase subunit N"
FT                   /id="PRO_0000391197"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   499 AA;  52535 MW;  F116A0CEA09ED72A CRC64;
     MTSLDFSTIL PEVVLAGYAL AALMAGAYLG KDRLARTLLW VTVAAFLVVA AMVGLGNHVD
     GAAFHGMFID DGFSRFAKVV TLVAAAGVLA MSADYMQRRN MLRFEFPIIV ALAVLGMMFM
     VSAGDLLTLY MGLELQSLAL YVVAAMRRDS VRSSEAGLKY FVLGSLSSGL LLYGASLVYG
     FAGTTGFEGI ISTIEAGHLS LGVLFGLVFM LVGLSFKVSA VPFHMWTPDV YEGSPTPVTA
     FFATAPKVAA MALIARLVFD AFGHVIGDWS QIVAALAVMS MFLGSIAGIG QTNIKRLMAY
     SSIAHMGFAL VGLAAGTAIG VQNMLLYMTI YAVMNIGTFA FILSMERDGV PVTDLAALNR
     FAWTDPVKAL AMLVLMFSLA GVPPTLGFFA KFGVLTAAVD AGMGWLAVLG VIASVIGAFY
     YLRIVYYMYF GGESEGMTSR MGAVQYLALM VPALAMLVGA ISMFGVDSAA GRAAETLVGP
     VAAIEQPAEA AQAEPVQGE
//