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Q56222 (NQO1_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 102. 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 1

EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I chain 1
NDH-1 subunit 1
Gene names
Name:nqo1
Ordered Locus Names:TTHA0089
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length438 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 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. The nqo1 subunit contains the NADH-binding site and the primary electron acceptor FMN.

Catalytic activity

NADH + quinone = NAD+ + quinol.

Cofactor

Binds 1 FMN per subunit.

Binds 1 4Fe-4S cluster per subunit. This 4Fe-4S cluster is referred to as N3.

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. Ref.3 Ref.4

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side.

Domain

The subunit can be separated roughly into four domains: an N-terminal domain (residues 7 to 72) ending with a glycine-rich loop, followed by a Rossman-fold domain (73 to 240), a ubiquitin-like domain (241 to 335) and a C-terminal four-helical bundle containing cluster N3 (336 to 438).

Sequence similarities

Belongs to the complex I 51 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438NADH-quinone oxidoreductase subunit 1
PRO_0000118567

Regions

Nucleotide binding66 – 694NAD Probable
Nucleotide binding92 – 965FMN
Nucleotide binding180 – 1856NAD Probable
Nucleotide binding218 – 2203FMN

Sites

Metal binding3531Iron-sulfur (4Fe-4S)
Metal binding3561Iron-sulfur (4Fe-4S)
Metal binding3591Iron-sulfur (4Fe-4S)
Metal binding4001Iron-sulfur (4Fe-4S)
Binding site751FMN
Binding site971NAD Probable

Secondary structure

....................................................................................... 438
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56222 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 73ADB3AF31BBE4C0

FASTA43848,632
        10         20         30         40         50         60 
MTGPILSGLD PRFERTLYAH VGKEGSWTLD YYLRHGGYET AKRVLKEKTP DEVIEEVKRS 

        70         80         90        100        110        120 
GLRGRGGAGF PTGLKWSFMP KDDGKQHYLI CNADESEPGS FKDRYILEDV PHLLIEGMIL 

       130        140        150        160        170        180 
AGYAIRATVG YIYVRGEYRR AADRLEQAIK EARARGYLGK NLFGTDFSFD LHVHRGAGAY 

       190        200        210        220        230        240 
ICGEETALMN SLEGLRANPR LKPPFPAQSG LWGKPTTINN VETLASVVPI MERGADWFAQ 

       250        260        270        280        290        300 
MGTEQSKGMK LYQISGPVKR PGVYELPMGT TFRELIYEWA GGPLEPIQAI IPGGSSTPPL 

       310        320        330        340        350        360 
PFTEEVLDTP MSYEHLQAKG SMLGTGGVIL IPERVSMVDA MWNLTRFYAH ESCGKCTPCR 

       370        380        390        400        410        420 
EGVAGFMVNL FAKIGTGQGE EKDVENLEAL LPLIEGRSFC PLADAAVWPV KGSLRHFKDQ 

       430 
YLALAREKRP VPRPSLWR 

« 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] [Europe PMC] [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].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Identification of a novel subunit of respiratory complex I from Thermus thermophilus."
Hinchliffe P., Carroll J., Sazanov L.A.
Biochemistry 45:4413-4420(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, EPR SPECTROSCOPY, SUBUNIT.
[4]"Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus."
Sazanov L.A., Hinchliffe P.
Science 311:1430-1436(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT, ELECTRON TRANSFER MECHANISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52917 Genomic DNA. Translation: AAA97943.1.
AP008226 Genomic DNA. Translation: BAD69912.1.
PIRT11903.
RefSeqYP_143355.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FUGX-ray3.301/A/J/S1-438[»]
2YBBelectron microscopy19.0011-438[»]
3I9VX-ray3.101/A1-438[»]
3IAMX-ray3.101/A1-438[»]
3IASX-ray3.151/A/J/S1-438[»]
3M9SX-ray4.501/A1-438[»]
4HEAX-ray3.301/B1-438[»]
ProteinModelPortalQ56222.
SMRQ56222. Positions 7-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59259N.
STRING300852.TTHA0089.

Protein family/group databases

TCDB3.D.1.3.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD69912; BAD69912; BAD69912.
GeneID3168453.
KEGGttj:TTHA0089.
PATRIC23955109. VBITheThe93045_0087.

Phylogenomic databases

eggNOGCOG1894.
HOGENOMHOG000251534.
KOK00335.
OMAATGVQTC.
OrthoDBEOG6W9XGK.
ProtClustDBCLSK445102.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-93-MONOMER.

Family and domain databases

InterProIPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
IPR011537. NADH-UbQ_OxRdtase_suF.
IPR011538. NADH_UbQ_OxRdtase_51kDa_su.
IPR019554. Soluble_ligand-bd.
[Graphical view]
PfamPF01512. Complex1_51K. 1 hit.
PF10589. NADH_4Fe-4S. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
SMARTSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
TIGRFAMsTIGR01959. nuoF_fam. 1 hit.
PROSITEPS00644. COMPLEX1_51K_1. 1 hit.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ56222.

Entry information

Entry nameNQO1_THET8
AccessionPrimary (citable) accession number: Q56222
Secondary accession number(s): Q5SM54
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 13, 2013
This is version 102 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references