Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADH-quinone oxidoreductase subunit N

Gene

nuoN

Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).By similarity

Catalytic activityi

NADH + quinone = NAD+ + quinol.

GO - Molecular functioni

  1. NADH dehydrogenase (ubiquinone) activity Source: InterPro
  2. quinone binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP synthesis coupled electron transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, Ubiquinone

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-2271-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-quinone oxidoreductase subunit N (EC:1.6.99.5)
Alternative name(s):
NADH dehydrogenase I subunit 14
NADH dehydrogenase I subunit N
NADH-quinone oxidoreductase subunit 14
Short name:
NQO14
NDH-1 subunit 14
NDH-1 subunit N
Gene namesi
Name:nuoN
Synonyms:nqo14
Ordered Locus Names:Pden_2231
OrganismiParacoccus denitrificans (strain Pd 1222)
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
ProteomesiUP000000361 Componenti: Chromosome 1

Subcellular locationi

  1. Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Transmembranei37 – 5721HelicalSequence AnalysisAdd
BLAST
Transmembranei76 – 9621HelicalSequence AnalysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence AnalysisAdd
BLAST
Transmembranei126 – 14621HelicalSequence AnalysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence AnalysisAdd
BLAST
Transmembranei196 – 21621HelicalSequence AnalysisAdd
BLAST
Transmembranei235 – 25521HelicalSequence AnalysisAdd
BLAST
Transmembranei269 – 28921HelicalSequence AnalysisAdd
BLAST
Transmembranei301 – 32121HelicalSequence AnalysisAdd
BLAST
Transmembranei324 – 34421HelicalSequence AnalysisAdd
BLAST
Transmembranei369 – 38921HelicalSequence AnalysisAdd
BLAST
Transmembranei402 – 42221HelicalSequence AnalysisAdd
BLAST
Transmembranei446 – 46621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499NADH-quinone oxidoreductase subunit NPRO_0000391197Add
BLAST

Keywords - PTMi

Quinone

Interactioni

Subunit structurei

NDH-1 is composed of at least 14 different subunits, nqo1 to nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers (By similarity). NADH-quinone oxidoreductase forms a supercomplex with ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) and cytochrome c oxidase (complex IV), which stabilizes the NADH-quinone oxidoreductase complex.By similarity1 Publication

Protein-protein interaction databases

STRINGi318586.Pden_2231.

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1007.
HOGENOMiHOG000100795.
KOiK00343.
OMAiPIGEFAA.
OrthoDBiEOG64JFNZ.

Family and domain databases

HAMAPiMF_00445. NDH1_NuoN_1.
InterProiIPR010096. NADH-Q_OxRdtase_suN/2.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Oxidored_q1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01770. NDH_I_N. 1 hit.

Sequencei

Sequence statusi: Complete.

A1B479-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSLDFSTIL PEVVLAGYAL AALMAGAYLG KDRLARTLLW VTVAAFLVVA
60 70 80 90 100
AMVGLGNHVD GAAFHGMFID DGFSRFAKVV TLVAAAGVLA MSADYMQRRN
110 120 130 140 150
MLRFEFPIIV ALAVLGMMFM VSAGDLLTLY MGLELQSLAL YVVAAMRRDS
160 170 180 190 200
VRSSEAGLKY FVLGSLSSGL LLYGASLVYG FAGTTGFEGI ISTIEAGHLS
210 220 230 240 250
LGVLFGLVFM LVGLSFKVSA VPFHMWTPDV YEGSPTPVTA FFATAPKVAA
260 270 280 290 300
MALIARLVFD AFGHVIGDWS QIVAALAVMS MFLGSIAGIG QTNIKRLMAY
310 320 330 340 350
SSIAHMGFAL VGLAAGTAIG VQNMLLYMTI YAVMNIGTFA FILSMERDGV
360 370 380 390 400
PVTDLAALNR FAWTDPVKAL AMLVLMFSLA GVPPTLGFFA KFGVLTAAVD
410 420 430 440 450
AGMGWLAVLG VIASVIGAFY YLRIVYYMYF GGESEGMTSR MGAVQYLALM
460 470 480 490
VPALAMLVGA ISMFGVDSAA GRAAETLVGP VAAIEQPAEA AQAEPVQGE
Length:499
Mass (Da):52,535
Last modified:January 23, 2007 - v1
Checksum:iF116A0CEA09ED72A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000489 Genomic DNA. Translation: ABL70323.1.
RefSeqiWP_011748518.1. NC_008686.1.
YP_916019.1. NC_008686.1.

Genome annotation databases

EnsemblBacteriaiABL70323; ABL70323; Pden_2231.
KEGGipde:Pden_2231.
PATRICi22855587. VBIParDen97112_2162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000489 Genomic DNA. Translation: ABL70323.1.
RefSeqiWP_011748518.1. NC_008686.1.
YP_916019.1. NC_008686.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318586.Pden_2231.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL70323; ABL70323; Pden_2231.
KEGGipde:Pden_2231.
PATRICi22855587. VBIParDen97112_2162.

Phylogenomic databases

eggNOGiCOG1007.
HOGENOMiHOG000100795.
KOiK00343.
OMAiPIGEFAA.
OrthoDBiEOG64JFNZ.

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-2271-MONOMER.

Family and domain databases

HAMAPiMF_00445. NDH1_NuoN_1.
InterProiIPR010096. NADH-Q_OxRdtase_suN/2.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Oxidored_q1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01770. NDH_I_N. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pd 1222.
  2. "Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans."
    Stroh A., Anderka O., Pfeiffer K., Yagi T., Finel M., Ludwig B., Schagger H.
    J. Biol. Chem. 279:5000-5007(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN NADH OXIDASE SUPERCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNUON_PARDP
AccessioniPrimary (citable) accession number: A1B479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.