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UniProtKB/Swiss-Prot entry Q56224


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NQO9_THET8
Primary accession number Q56224
Secondary accession number Q5SM51
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 70)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit 9
Synonyms EC 1.6.99.5
NADH dehydrogenase I subunit 9
NDH-1 subunit 9
Gene name
Name: nqo9
OrderedLocusNames: TTHA0092
From
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [TaxID: 300852] [HAMAP proteome]
Taxonomy Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1074/jbc.272.7.4201; PubMed=9020134 [NCBI, ExPASy, EBI, Israel, Japan]
Yano T., Chu S.S., Sled' V.D., Ohnishi T., Yagi T.;
"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.";
J. Biol. Chem. 272:4201-4211(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
"Complete genome sequence of Thermus thermophilus HB8.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[3]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
DOI=10.1021/bi0600998; PubMed=16584177 [NCBI, ExPASy, EBI, Israel, Japan]
Hinchliffe P., Carroll J., Sazanov L.A.;
"Identification of a novel subunit of respiratory complex I from Thermus thermophilus.";
Biochemistry 45:4413-4420(2006).
[4]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT, AND ELECTRON TRANSFER MECHANISM.
DOI=10.1126/science.1123809; PubMed=16469879 [NCBI, ExPASy, EBI, Israel, Japan]
Sazanov L.A., Hinchliffe P.;
"Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.";
Science 311:1430-1436(2006).
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 role of the nqo9 subunit appears to provide a 'connecting chain' of two clusters between cluster N5 and the terminal cluster N2, and to stabilize the structure of the complex by interacting with other subunits.
  • CATALYTIC ACTIVITY: NADH + quinone = NAD+ + quinol.
  • COFACTOR: Binds 2 4Fe-4S clusters per subunit. The 4Fe-4S clusters are referred to as N6a and N6b.
  • SUBUNIT: 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.
  • SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
  • SIMILARITY: Belongs to the complex I 23 kDa subunit family.
  • SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U52917; AAA97946.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008226; BAD69915.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T11906; T11906.
RefSeq YP_143358.1; -.
3D structure databases
PDB
2FUG; X-ray; 3.30 A; 9/G/P/Y=1-182.[ExPASy / RCSB / EBI]
PDBsum 2FUG; -.
ModBase Q56224.
Enzyme and pathway databases
BioCyc TTHE300852:TTHA0092-MON; -.
Ontologies
GO
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from HAMAP).
GO:0019684; Biological process: photosynthesis, light reaction (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01351; -; 1.
PBIL [Tree]
InterPro IPR001450; 4Fe4S_Fe_S_bd.
IPR010226; NADH_quinone_OxRdtase_I.
Graphical view of domain structure.
Pfam PF00037; Fer4; 2.
Pfam graphical view of domain structure.
PRINTS PR00353; 4FE4SFRDOXIN.
TIGRFAMs TIGR01971; NuoI; 1.
PROSITE PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q56224.
Genome annotation databases
GeneID 3167944; -.
GenomeReviews AP008226_GR; TTHA0092.
KEGG ttj:TTHA0092; -.
Phylogenomic databases
HOGENOM Q56224; -.
Genome annotation databases
CMR Q56224; TTHA0092.
Other
ProtoNet Q56224.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   182  182     NADH-quinone oxidoreductase subunit 9. PRO_0000118721
DOMAIN   43    73  31     4Fe-4S ferredoxin-type 1. 
DOMAIN   89   118  30     4Fe-4S ferredoxin-type 2. 
METAL   53    53        Iron-sulfur 1 (4Fe-4S). 
METAL   56    56        Iron-sulfur 1 (4Fe-4S). 
METAL   59    59        Iron-sulfur 1 (4Fe-4S). 
METAL   63    63        Iron-sulfur 2 (4Fe-4S). 
METAL   98    98        Iron-sulfur 2 (4Fe-4S). 
METAL   101   101        Iron-sulfur 2 (4Fe-4S). 
METAL   104   104        Iron-sulfur 2 (4Fe-4S). 
METAL   108   108        Iron-sulfur 1 (4Fe-4S). 
STRAND   40    43  4      
HELIX   58    62  5      
STRAND   68    74  7      
STRAND   77    79  3      
STRAND   81    94  14      
TURN   95    97  3      
HELIX   103   107  5      
STRAND   109   111  3      
STRAND   113   115  3      
HELIX   126   128  3      
STRAND   129   131  3      
TURN   134   136  3      
HELIX   144   153  10      
STRAND   160   162  3      
TURN   169   172  4      
Sequence information
Length: 182 AA [This is the length of the unprocessed precursor] Molecular weight: 20080 Da [This is the MW of the unprocessed precursor] CRC64: 054A9F7942C64C66 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTLKALAQSL GITLKYLFSK PVTVPYPDAP VALKPRFHGR HVLTRHPNGL EKCIGCSLCA 

        70         80         90        100        110        120 
AACPAYAIYV EPAENDPENP VSAGERYAKV YEINMLRCIF CGLCEEACPT GAIVLGYDFE 

       130        140        150        160        170        180 
MADYEYSDLV YGKEDMLVDV VGTKPQRREA KRTGKPVKVG YVVPYVRPEL EGFKAPTEGG 


KR 

Q56224 in FASTA format

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