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A1AVS5 (NUON_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-quinone oxidoreductase subunit N

EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I subunit N
NDH-1 subunit N
Gene names
Name:nuoN
Ordered Locus Names:Rmag_0250
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.

Subcellular location

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

Sequence similarities

Belongs to the complex I subunit 2 family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandNAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processATP synthesis coupled electron transport

Inferred from electronic annotation. Source: InterPro

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: InterPro

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484NADH-quinone oxidoreductase subunit N HAMAP-Rule MF_00445
PRO_0000391218

Regions

Transmembrane11 – 3121Helical; Potential
Transmembrane42 – 6221Helical; Potential
Transmembrane79 – 9820Helical; Potential
Transmembrane113 – 13321Helical; Potential
Transmembrane134 – 15421Helical; Potential
Transmembrane167 – 18721Helical; Potential
Transmembrane211 – 23121Helical; Potential
Transmembrane248 – 26821Helical; Potential
Transmembrane279 – 29921Helical; Potential
Transmembrane313 – 33321Helical; Potential
Transmembrane335 – 35521Helical; Potential
Transmembrane378 – 39821Helical; Potential
Transmembrane408 – 42821Helical; Potential
Transmembrane457 – 47721Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A1AVS5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 9B9CCABC3F131AD9

FASTA48453,607
        10         20         30         40         50         60 
MNNFIEFDTS SLWIALPEIF LLSAIVIVLL IDLFLDKNFK QVTYYLIQLS LFITGLLAFN 

        70         80         90        100        110        120 
LIDHPQIIIF GGSFVLDNMA SVFKVFMMAA TMVAMVYSRH YLRTHSLFRG EYFVLVLLSV 

       130        140        150        160        170        180 
LGMMVMVSGY SLLTLYLGLE ILSLSLYALI AIARERADAI EAALKYFVLG AIASGLLLYG 

       190        200        210        220        230        240 
MSMIYGISGS LNINDIASFA SNTNLDSRET LIINFGLVFL VIGIAFKLGA VPFHMWVPDV 

       250        260        270        280        290        300 
YQGAPTSVTL FISTVPKIAA FAMLVRILVD GLDSMHAYWS DLFMVLSILS IALGSVVALM 

       310        320        330        340        350        360 
QSNIKRMLAY STISHVGFIM LGFVAGTPIG YGAAAFYMLV YVLMSLAAFG MIILLNKQGF 

       370        380        390        400        410        420 
EIDQISDFKG LNKHAPWFAL MMLIIILSMA GVPPLVGFYS KFFILQQVVS AGFITIAVIV 

       430        440        450        460        470        480 
VIFAVISAYY YLQIIKSMYF DETDKKITIY ASIDIQLVLS INAILILAVG LFPDFWMKLA 


LSLF 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL02032.1.
RefSeqYP_903503.1. NC_008610.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413404.Rmag_0250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL02032; ABL02032; Rmag_0250.
GeneID4555652.
KEGGrma:Rmag_0250.
PATRIC32000109. VBICanRut45856_0283.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1007.
HOGENOMHOG000100795.
KOK00343.
OMAIEAQLYG.
OrthoDBEOG64JFNZ.

Enzyme and pathway databases

BioCycCRUT413404:GHM7-259-MONOMER.

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 nameNUON_RUTMC
AccessionPrimary (citable) accession number: A1AVS5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families