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Reviewed, UniProtKB/Swiss-Prot Q56217 (NQO7_THET8)

Last modified January 19, 2010. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADH-quinone oxidoreductase subunit 7
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I chain 7
    NDH-1 subunit 7
Gene names
Name: nqo7
Ordered Locus Names: TTHA0084
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length119 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 menaquinone. 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 required for the synthesis of ATP. HAMAP MF_01394

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP MF_01394

Subunit structure

NDH-1 is composed of 15 different subunits, nqo1 to nqo15. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8 and nqo10 to nqo14) embedded in the membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9 and nqo15) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers. HAMAP MF_01394

Subcellular location

Cell inner membrane; Multi-pass membrane protein HAMAP MF_01394.

Sequence similarities

Belongs to the complex I subunit 3 family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   LigandNAD
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: HAMAP

photosynthesis, light reaction

Inferred from electronic annotation. Source: HAMAP

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 119119NADH-quinone oxidoreductase subunit 7 HAMAP MF_01394
PRO_0000117861

Regions

Transmembrane11 – 3121 Potential
Transmembrane59 – 7921 Potential
Transmembrane88 – 10821 Potential

Sequences

Sequence LengthMass (Da)Tools
Q56217-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 10FFA8C204B0AFF5

FASTA11913,145
        10         20         30         40         50         60 
MAPIQEYVGT LIYVGVALFI GVAALLVGAL LGPKKPGRAK LMPYESGNDP AGEVKRFPVH 

        70         80         90        100        110 
FYVVAMLFIL FDVEVAFLWP YAVSAGGLGL YGFLGVLAFT LLLFVGFLYE WWKGVMRWH 

« Hide

References

« Hide 'large scale' references
[1]"The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQO2 subunit."
Yano T., Chu S.S., Sled' V.D., Ohnishi T., Yagi T.
J. Biol. Chem. 272:4201-4211(1997) [PubMed: 9020134] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52917 Genomic DNA. Translation: AAA97938.1.
AP008226 Genomic DNA. Translation: BAD69907.1.
PIRT11898.
RefSeqYP_143350.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ56217.

Protein family/group databases

TCDB3.D.1.3.1. H+ or Na+-translocating NADH dehydrogenase (NDH) family.

Genome annotation databases

GeneID3168352.
GenomeReviewsGene locus TTHA0084 in contig AP008226_GR.
KEGGttj:TTHA0084.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0838.
HOGENOMHBG605540.
OMACEPVGSA.

Enzyme and pathway databases

BioCycTTHE300852:TTHA0084-MONOMER.

Family and domain databases

HAMAPMF_01394. NDH1_NuoA.
[Tree]
InterProIPR000440. NADH_UbQ/plastoQ_OxRdtase_su3.
[Graphical view]
PANTHERPTHR11058. Oxidored_q4. 1 hit.
PfamPF00507. Oxidored_q4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNQO7_THET8
AccessionPrimary (citable) accession number: Q56217
Secondary accession number(s): Q5SM59
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents