NUON_PARDP
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 25-MAY-2022, entry version 87.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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}.
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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 PRIDE; A1B479; -.
DR EnsemblBacteria; ABL70323; ABL70323; Pden_2231.
DR KEGG; pde:Pden_2231; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_3_5; -.
DR OMA; FYIRVIV; -.
DR Proteomes; UP000000361; Chromosome 1.
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 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
