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Protein

NADH-quinone oxidoreductase subunit N

Gene

nuoN

Organism
Pelobacter propionicus (strain DSM 2379)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

NADH + quinone = NAD+ + quinol.UniRule annotation

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
  2. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Transport

Keywords - Ligandi

NAD, Ubiquinone

Enzyme and pathway databases

BioCyciPPRO338966:GHL0-646-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-quinone oxidoreductase subunit NUniRule annotation (EC:1.6.99.5UniRule annotation)
Alternative name(s):
NADH dehydrogenase I subunit NUniRule annotation
NDH-1 subunit NUniRule annotation
Gene namesi
Name:nuoNUniRule annotation
Ordered Locus Names:Ppro_0641
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000006732: Chromosome

Subcellular locationi

Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2521HelicalUniRule annotationAdd
BLAST
Transmembranei34 – 5421HelicalUniRule annotationAdd
BLAST
Transmembranei72 – 9221HelicalUniRule annotationAdd
BLAST
Transmembranei99 – 11921HelicalUniRule annotationAdd
BLAST
Transmembranei120 – 14021HelicalUniRule annotationAdd
BLAST
Transmembranei154 – 17421HelicalUniRule annotationAdd
BLAST
Transmembranei196 – 21621HelicalUniRule annotationAdd
BLAST
Transmembranei230 – 25021HelicalUniRule annotationAdd
BLAST
Transmembranei259 – 27921HelicalUniRule annotationAdd
BLAST
Transmembranei286 – 30318HelicalUniRule annotationAdd
BLAST
Transmembranei314 – 33421HelicalUniRule annotationAdd
BLAST
Transmembranei356 – 37621HelicalUniRule annotationAdd
BLAST
Transmembranei393 – 41321HelicalUniRule annotationAdd
BLAST
Transmembranei432 – 45221HelicalUniRule annotationAdd
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 – 463463NADH-quinone oxidoreductase subunit NPRO_0000391201Add
BLAST

Keywords - PTMi

Quinone

Interactioni

Subunit structurei

NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.UniRule annotation

Protein-protein interaction databases

STRINGi338966.Ppro_0641.

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 2 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1007.
HOGENOMiHOG000129655.
KOiK00343.
OMAiALIYMET.
OrthoDBiEOG64JFNZ.

Family and domain databases

HAMAPiMF_00445. NDH1_NuoN_1.
InterProiIPR010096. NADH-Q_OxRdtase_suN/2.
IPR001750. NADH_UbQ/plastoQ_OxRdtase.
[Graphical view]
PfamiPF00361. Oxidored_q1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1ALQ2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATDLLYGLL PEHILLGLIL VLMLLEILSV DKRAGSALFI ASLLAGAGVL
60 70 80 90 100
VMQLQTGYTA DIVMNEIRID RFSEIGRLII VSCGAILGVY SLSSEAGHKY
110 120 130 140 150
WILIASSLLG AMIILDSAGF ISLFMGIEIL SLPGFALMVL NNGKSTASEG
160 170 180 190 200
SIKYLLLSSV ATALVLFGLS LVYGSTGNLN ISSFTAAVAT GGVQNLAASV
210 220 230 240 250
MILSGFFLKA SVFPFHGWAP DAYSSARLPV TAFLASIVKA AVVLGLVRIL
260 270 280 290 300
GNAVLNPEAV TVIALLSMLS MFYGNITAIH QTAFKKMLAY SSISHAGYMM
310 320 330 340 350
FALVDNTGAR TEALLYYVAV YAVTTITACA CFSILSGEDD NLDNLNGIFR
360 370 380 390 400
KKPVAAILLS LCVLSLAGIP PLPGFLAKFF VFKTVIASGH LTVAVLAFVA
410 420 430 440 450
SYIGTFFYLG VVLRMFRSDA ETVEQPANAT CLCWTWGGAL LGTLALALFM
460
LLPNIFHWVM TGI
Length:463
Mass (Da):49,096
Last modified:January 23, 2007 - v1
Checksum:i83B7BA884BE83ABB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABK98272.1.
RefSeqiWP_011734585.1. NC_008609.1.
YP_900330.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABK98272; ABK98272; Ppro_0641.
GeneIDi4571818.
KEGGippd:Ppro_0641.
PATRICi22894315. VBIPelPro64470_0795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABK98272.1.
RefSeqiWP_011734585.1. NC_008609.1.
YP_900330.1. NC_008609.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338966.Ppro_0641.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK98272; ABK98272; Ppro_0641.
GeneIDi4571818.
KEGGippd:Ppro_0641.
PATRICi22894315. VBIPelPro64470_0795.

Phylogenomic databases

eggNOGiCOG1007.
HOGENOMiHOG000129655.
KOiK00343.
OMAiALIYMET.
OrthoDBiEOG64JFNZ.

Enzyme and pathway databases

BioCyciPPRO338966:GHL0-646-MONOMER.

Family and domain databases

HAMAPiMF_00445. NDH1_NuoN_1.
InterProiIPR010096. NADH-Q_OxRdtase_suN/2.
IPR001750. NADH_UbQ/plastoQ_OxRdtase.
[Graphical view]
PfamiPF00361. Oxidored_q1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiNUON_PELPD
AccessioniPrimary (citable) accession number: A1ALQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 50 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.