Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C6E9S6 (C6E9S6_ECOBD) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
NADH-quinone oxidoreductase subunit N HAMAP-Rule MF_00445

EC=1.6.99.5 HAMAP-Rule MF_00445
Alternative name(s):
NADH dehydrogenase I subunit N HAMAP-Rule MF_00445
NDH-1 subunit N HAMAP-Rule MF_00445
Gene names
Name:nuoN HAMAP-Rule MF_00445
Ordered Locus Names:ECBD_1385 EMBL ACT28448.1
OrganismEscherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]
Taxonomic identifier469008 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00445

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_00445

Subunit structure

NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity. HAMAP-Rule MF_00445

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00445.

Membrane; Multi-pass membrane protein By similarity RuleBase RU000320.

Sequence similarities

Belongs to the complex I subunit 2 family. HAMAP-Rule MF_00445

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Transmembrane8 – 2821Helical; By similarity HAMAP-Rule MF_00445
Transmembrane35 – 5521Helical; By similarity HAMAP-Rule MF_00445
Transmembrane71 – 9121Helical; By similarity HAMAP-Rule MF_00445
Transmembrane105 – 12521Helical; By similarity HAMAP-Rule MF_00445
Transmembrane127 – 14721Helical; By similarity HAMAP-Rule MF_00445
Transmembrane159 – 17921Helical; By similarity HAMAP-Rule MF_00445
Transmembrane203 – 22321Helical; By similarity HAMAP-Rule MF_00445
Transmembrane235 – 25521Helical; By similarity HAMAP-Rule MF_00445
Transmembrane271 – 29121Helical; By similarity HAMAP-Rule MF_00445
Transmembrane297 – 31721Helical; By similarity HAMAP-Rule MF_00445
Transmembrane326 – 34621Helical; By similarity HAMAP-Rule MF_00445
Transmembrane373 – 39321Helical; By similarity HAMAP-Rule MF_00445
Transmembrane408 – 43023Helical; By similarity HAMAP-Rule MF_00445
Transmembrane455 – 47521Helical; By similarity HAMAP-Rule MF_00445

Sequences

Sequence LengthMass (Da)Tools
C6E9S6 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: A15F4875B7D19D09

FASTA48552,044
        10         20         30         40         50         60 
MTITPQNLIA LLPLLIVGLT VVVVMLSIAW RRNHFLNATL SVIGLNAALV SLWFVGQAGA 

        70         80         90        100        110        120 
MDVTPLMRVD GFAMLYTGLV LLASLATCTF AYPWLEGYND NKDEFYLLVL IAALGGILLA 

       130        140        150        160        170        180 
NANHLASLFL GIELISLPLF GLVGYAFRQK RSLEASIKYT ILSAAASSFL LFGMALVYAQ 

       190        200        210        220        230        240 
SGDLSFVALG KNLGDGMLNE PLLLAGFGLM IVGLGFKLSL VPFHLWTPDV YQGAPAPVST 

       250        260        270        280        290        300 
FLATASKIAI FGVVMRLFLY APVGDSEAIR VVLAIIAFAS IIFGNLMALS QTNIKRLLGY 

       310        320        330        340        350        360 
SSISHLGYLL VALIALQTGE MSMEAVGVYL AGYLFSSLGA FGVVSLMSSP YRGPDADSLF 

       370        380        390        400        410        420 
SYRGLFWHRP ILAAVMTVMM LSLAGIPMTL GFIGKFYVLA VGVQAHLWWL VGAVVVGSAI 

       430        440        450        460        470        480 
GLYYYLRVAV SLYLHAPEQP GRDAPSNWQY SAGGIVVLIS ALLVLVLGVW PQPLISIVRL 


AMPLM 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001665 Genomic DNA. Translation: ACT28448.1.
RefSeqYP_003035633.1. NC_012947.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RKOX-ray3.00D/N1-485[»]
ProteinModelPortalC6E9S6.
SMRC6E9S6. Positions 1-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59174N.
STRING469008.ECBD_1385.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT28448; ACT28448; ECBD_1385.
GeneID8156289.
KEGGebd:ECBD_1385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000100796.
KOK00343.
OMASIVQLAM.

Family and domain databases

HAMAPMF_00445. NDH1_NuoN_1.
InterProIPR010096. NADH-Q_OxRdtase_suN/2.
IPR001750. NADH_UbQ/plastoQ_OxRdtase.
[Graphical view]
PfamPF00361. Oxidored_q1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01770. NDH_I_N. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC6E9S6_ECOBD
AccessionPrimary (citable) accession number: C6E9S6
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)