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Q8G1A7 (NUOK_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 K

EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I subunit K
NDH-1 subunit K
Gene names
Name:nuoK
Ordered Locus Names:BR0812, BS1330_I0808
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length102 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_01456

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01456

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_01456.

Sequence similarities

Belongs to the complex I subunit 4L 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 (quinone) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 102102NADH-quinone oxidoreductase subunit K HAMAP-Rule MF_01456
PRO_0000389977

Regions

Transmembrane5 – 2521Helical; Potential
Transmembrane31 – 5121Helical; Potential
Transmembrane66 – 8621Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q8G1A7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E3EC572231BD3204

FASTA10210,942
        10         20         30         40         50         60 
MEIGIAHYLT VSAILFTLGV FGIFLNRKNV IVILMSIELI LLSVNLNFVA FSSQLGDLVG 

        70         80         90        100 
QVFALFVLTV AAAEAAIGLA ILVVFFRNRG SIAVEDVNVM KG 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN29741.1.
CP002997 Genomic DNA. Translation: AEM18158.1.
PIRAF3395.
RefSeqNP_697826.1. NC_004310.3.
YP_005615650.1. NC_017251.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR0812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN29741; AAN29741; BR0812.
AEM18158; AEM18158; BS1330_I0808.
GeneID1166480.
12137134.
KEGGbms:BR0812.
bsi:BS1330_I0808.
PATRIC17789922. VBIBruSui107850_0822.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0713.
HOGENOMHOG000066429.
KOK00340.
OMAVEDINMM.
OrthoDBEOG6MSS3R.

Family and domain databases

HAMAPMF_01456. NDH1_NuoK.
InterProIPR001133. NADH_UbQ_OxRdtase_chain4L/K.
[Graphical view]
PANTHERPTHR11434. PTHR11434. 1 hit.
PfamPF00420. Oxidored_q2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOK_BRUSU
AccessionPrimary (citable) accession number: Q8G1A7
Secondary accession number(s): G0K8W0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 66 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

Brucella suis

Brucella suis (strain 1330): entries and gene names