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Protein

NADH-quinone oxidoreductase subunit A

Gene

nuoA

Organism
Escherichia coli (strain B / BL21-DE3)
Status
Unreviewed-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.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. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

TransportUniRule annotation

Keywords - Ligandi

NADUniRule annotation, UbiquinoneUniRule annotationImported

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-quinone oxidoreductase subunit AUniRule annotation (EC:1.6.99.5UniRule annotation)
Alternative name(s):
NADH dehydrogenase I subunit AUniRule annotation
NDH-1 subunit AUniRule annotation
NUO1UniRule annotation
Gene namesi
Name:nuoAUniRule annotationImported
Ordered Locus Names:B21_02173Imported, ECBD_1373Imported, ECD_02213Imported
OrganismiEscherichia coli (strain B / BL21-DE3)Imported
Taxonomic identifieri469008 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001509: Chromosome, UP000002032: Chromosome, UP000009074: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei16 – 3621HelicalUniRule annotationAdd
BLAST
Transmembranei68 – 8821HelicalUniRule annotationAdd
BLAST
Transmembranei98 – 11821HelicalUniRule 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 membraneUniRule annotation, Cell membrane, Membrane

PTM / Processingi

Keywords - PTMi

QuinoneUniRule annotation

Interactioni

Subunit structurei

NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.UniRule annotation

Protein-protein interaction databases

DIPiDIP-59171N.
STRINGi469008.ECBD_1373.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RKOX-ray3.00A/E1-147[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 3 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotation

Phylogenomic databases

eggNOGiCOG0838.
HOGENOMiHOG000100121.
KOiK00330.
OMAiWVGFIEA.

Family and domain databases

HAMAPiMF_01394. NDH1_NuoA.
InterProiIPR023043. NAD(P)H_OxRDtase_bac/plastid.
IPR000440. NADH_UbQ/plastoQ_OxRdtase_su3.
[Graphical view]
PANTHERiPTHR11058. PTHR11058. 1 hit.
PfamiPF00507. Oxidored_q4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C6E9R4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMSTSTEVI AHHWAFAIFL IVAIGLCCLM LVGGWFLGGR ARARSKNVPF
60 70 80 90 100
ESGIDSVGSA RLRLSAKFYL VAMFFVIFDV EALYLFAWST SIRESGWVGF
110 120 130 140
VEAAIFIFVL LAGLVYLVRI GALDWTPARS RRERMNPETN SIANRQR
Length:147
Mass (Da):16,457
Last modified:September 1, 2009 - v1
Checksum:i1F9E0804B2B0D1B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001665 Genomic DNA. Translation: ACT28436.1.
CP001509 Genomic DNA. Translation: ACT44035.1.
AM946981 Genomic DNA. Translation: CAQ32690.1.
RefSeqiYP_002999952.1. NC_012892.2.
YP_003035621.1. NC_012947.1.
YP_003054806.1. NC_012971.2.

Genome annotation databases

EnsemblBacteriaiACT28436; ACT28436; ECBD_1373.
ACT44035; ACT44035; ECD_02213.
CAQ32690; CAQ32690; B21_02173.
GeneIDi8113024.
8156277.
8181263.
KEGGiebd:ECBD_1373.
ebe:B21_02173.
ebl:ECD_02213.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001665 Genomic DNA. Translation: ACT28436.1.
CP001509 Genomic DNA. Translation: ACT44035.1.
AM946981 Genomic DNA. Translation: CAQ32690.1.
RefSeqiYP_002999952.1. NC_012892.2.
YP_003035621.1. NC_012947.1.
YP_003054806.1. NC_012971.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RKOX-ray3.00A/E1-147[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59171N.
STRINGi469008.ECBD_1373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACT28436; ACT28436; ECBD_1373.
ACT44035; ACT44035; ECD_02213.
CAQ32690; CAQ32690; B21_02173.
GeneIDi8113024.
8156277.
8181263.
KEGGiebd:ECBD_1373.
ebe:B21_02173.
ebl:ECD_02213.

Phylogenomic databases

eggNOGiCOG0838.
HOGENOMiHOG000100121.
KOiK00330.
OMAiWVGFIEA.

Family and domain databases

HAMAPiMF_01394. NDH1_NuoA.
InterProiIPR023043. NAD(P)H_OxRDtase_bac/plastid.
IPR000440. NADH_UbQ/plastoQ_OxRdtase_su3.
[Graphical view]
PANTHERiPTHR11058. PTHR11058. 1 hit.
PfamiPF00507. Oxidored_q4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and gene expression analysis of Escherichia coli BL21(DE3)."
    Krempl P.M., Mairhofer J., Eisenkolb M., Specht T., Leparc G.G., Kreil D.P., Bayer K., Striedner G.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Korea]Imported and BL21Imported.
  3. "Sequencing and gene expression analysis of Escherichia coli BL21."
    Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
    Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Austria]Imported.
  4. "Complete sequence of Escherichia coli 'BL21-Gold(DE3)pLysS AG'."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21-GoldImported.
  5. "Complete sequence of Escherichia coli BL21(DE3)."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [JGI]Imported.
  6. Jeong H., Shim J.-H., Studier F.W., Oh T.K., Kim J.F.
    Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21.
  7. "Structure of the membrane domain of respiratory complex I."
    Efremov R.G., Sazanov L.A.
    Nature 476:414-420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).

Entry informationi

Entry nameiC6E9R4_ECOBD
AccessioniPrimary (citable) accession number: C6E9R4
Secondary accession number(s): C5W725
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: March 4, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

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.