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 J

Gene

nuoJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Catalytic activityi

NADH + a quinone = NAD+ + a quinol.

GO - Molecular functioni

  • NADH dehydrogenase (ubiquinone) activity Source: EcoCyc
  • quinone binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, Ubiquinone

Enzyme and pathway databases

BioCyciEcoCyc:NUOJ-MONOMER.
ECOL316407:JW2275-MONOMER.
MetaCyc:NUOJ-MONOMER.

Protein family/group databases

TCDBi3.D.1.1.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-quinone oxidoreductase subunit J (EC:1.6.5.11)
Alternative name(s):
NADH dehydrogenase I subunit J
NDH-1 subunit J
NUO10
Gene namesi
Name:nuoJ
Ordered Locus Names:b2280, JW2275
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12090. nuoJ.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2121HelicalSequence analysisAdd
BLAST
Topological domaini22 – 276CytoplasmicSequence analysis
Transmembranei28 – 4821HelicalSequence analysisAdd
BLAST
Topological domaini49 – 535PeriplasmicSequence analysis
Transmembranei54 – 7421HelicalSequence analysisAdd
BLAST
Topological domaini75 – 9117CytoplasmicSequence analysisAdd
BLAST
Transmembranei92 – 11221HelicalSequence analysisAdd
BLAST
Topological domaini113 – 13725PeriplasmicSequence analysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence analysisAdd
BLAST
Topological domaini159 – 18426CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • NADH dehydrogenase complex Source: EcoliWiki
  • plasma membrane Source: EcoCyc
  • plasma membrane respiratory chain complex I Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184NADH-quinone oxidoreductase subunit JPRO_0000118370Add
BLAST

Keywords - PTMi

Quinone

Proteomic databases

PaxDbiP0AFE0.

Interactioni

Subunit structurei

Composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.

Protein-protein interaction databases

BioGridi4260509. 26 interactions.
DIPiDIP-59258N.
STRINGi511145.b2280.

Structurei

3D structure databases

ProteinModelPortaliP0AFE0.
SMRiP0AFE0. Positions 1-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 6 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107UFS. Bacteria.
COG0839. LUCA.
HOGENOMiHOG000262591.
InParanoidiP0AFE0.
KOiK00339.
OMAiIGVRHIG.
OrthoDBiEOG683SBP.
PhylomeDBiP0AFE0.

Family and domain databases

InterProiIPR001457. NADH_UbQ/plastoQ_OxRdtase_su6.
[Graphical view]
PfamiPF00499. Oxidored_q3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AFE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFAFYICGL IAILATLRVI THTNPVHALL YLIISLLAIS GVFFSLGAYF
60 70 80 90 100
AGALEIIVYA GAIMVLFVFV VMMLNLGGSE IEQERQWLKP QVWIGPAILS
110 120 130 140 150
AIMLVVIVYA ILGVNDQGID GTPISAKAVG ITLFGPYVLA VELASMLLLA
160 170 180
GLVVAFHVGR EERAGEVLSN RKDDSAKRKT EEHA
Length:184
Mass (Da):19,875
Last modified:December 20, 2005 - v1
Checksum:i9C9D0C9ABAEC7755
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851R → T in CAA48369 (PubMed:7690854).Curated
Sequence conflicti126 – 1261A → R in CAA48369 (PubMed:7690854).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68301 Genomic DNA. Translation: CAA48369.1.
U00096 Genomic DNA. Translation: AAC75340.1.
AP009048 Genomic DNA. Translation: BAA16108.1.
PIRiF64999.
RefSeqiNP_416783.1. NC_000913.3.
WP_000393511.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75340; AAC75340; b2280.
BAA16108; BAA16108; BAA16108.
GeneIDi946756.
KEGGiecj:JW2275.
eco:b2280.
PATRICi32119927. VBIEscCol129921_2373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68301 Genomic DNA. Translation: CAA48369.1.
U00096 Genomic DNA. Translation: AAC75340.1.
AP009048 Genomic DNA. Translation: BAA16108.1.
PIRiF64999.
RefSeqiNP_416783.1. NC_000913.3.
WP_000393511.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AFE0.
SMRiP0AFE0. Positions 1-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260509. 26 interactions.
DIPiDIP-59258N.
STRINGi511145.b2280.

Protein family/group databases

TCDBi3.D.1.1.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Proteomic databases

PaxDbiP0AFE0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75340; AAC75340; b2280.
BAA16108; BAA16108; BAA16108.
GeneIDi946756.
KEGGiecj:JW2275.
eco:b2280.
PATRICi32119927. VBIEscCol129921_2373.

Organism-specific databases

EchoBASEiEB2014.
EcoGeneiEG12090. nuoJ.

Phylogenomic databases

eggNOGiENOG4107UFS. Bacteria.
COG0839. LUCA.
HOGENOMiHOG000262591.
InParanoidiP0AFE0.
KOiK00339.
OMAiIGVRHIG.
OrthoDBiEOG683SBP.
PhylomeDBiP0AFE0.

Enzyme and pathway databases

BioCyciEcoCyc:NUOJ-MONOMER.
ECOL316407:JW2275-MONOMER.
MetaCyc:NUOJ-MONOMER.

Miscellaneous databases

PROiP0AFE0.

Family and domain databases

InterProiIPR001457. NADH_UbQ/plastoQ_OxRdtase_su6.
[Graphical view]
PfamiPF00499. Oxidored_q3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I."
    Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.
    J. Mol. Biol. 233:109-122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / AN387.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiNUOJ_ECOLI
AccessioniPrimary (citable) accession number: P0AFE0
Secondary accession number(s): P33605, P78236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 83 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.