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UniProtKB/Swiss-Prot entry Q5SKZ7


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

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Entry information
Entry name NQO15_THET8
Primary accession number Q5SKZ7
Secondary accession numbers None
Integrated into Swiss-Prot on April 18, 2006
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 25)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit 15
Synonyms EC 1.6.99.5
NADH dehydrogenase I chain 15
NDH-1 subunit 15
Gene name
Name: nqo15
OrderedLocusNames: TTHA0496
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 [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.
[2]
PROTEIN SEQUENCE OF 2-9, CHARACTERIZATION, 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).
[3]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), FUNCTION, 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 nqo15 subunit has probably a role in complex stabilization, and may be also involved in the storage of iron for iron-sulfur cluster regeneration in the complex.
  • CATALYTIC ACTIVITY: NADH + quinone = NAD+ + quinol.
  • 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. Nqo15 is bound to the side of the complex near the N-terminus of nqo3, where it interacts with subunits nqo3, nqo2, nqo1, nqo9 and nqo4.
  • SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
  • DOMAIN: Has a similar fold to the mitochondrial iron chaperone frataxin.
  • SIMILARITY: Belongs to the complex I nqo15 family.
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
AP008226; BAD70319.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_143762.1; -.
3D structure databases
PDB
2FUG; X-ray; 3.30 A; 7/H/Q/Z=1-129.[ExPASy / RCSB / EBI]
PDBsum 2FUG; -.
ModBase Q5SKZ7.
Enzyme and pathway databases
BioCyc TTHE300852:TTHA0496-MON; -.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0050136; Molecular function: NADH dehydrogenase (quinone) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
BLOCKS Q5SKZ7.
Genome annotation databases
GeneID 3169322; -.
GenomeReviews AP008226_GR; TTHA0496.
KEGG ttj:TTHA0496; -.
NMPDR fig|300852.3.peg.607; -.
Phylogenomic databases
HOGENOM Q5SKZ7; -.
Genome annotation databases
CMR Q5SKZ7; TTHA0496.
Other
ProtoNet Q5SKZ7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Complete proteome; Direct protein sequencing; Membrane; NAD; Oxidoreductase; Quinone.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   129  128     NADH-quinone oxidoreductase subunit 15. PRO_0000233014
HELIX   4    27  24      
STRAND   30    36  7      
HELIX   38    41  4      
STRAND   53    60  8      
STRAND   66    72  7      
STRAND   82    86  5      
TURN   87    90  4      
STRAND   91    98  8      
TURN   99   101  3      
STRAND   102   109  8      
HELIX   112   126  15      
Sequence information
Length: 129 AA [This is the length of the unprocessed precursor] Molecular weight: 14788 Da [This is the MW of the unprocessed precursor] CRC64: A944E174C0DE152C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSASSERELY EAWVELLSWM REYAQAKGVR FEKEADFPDF IYRMERPYDL PTTIMTASLS 

        70         80         90        100        110        120 
DGLGEPFLLA DVSPRHAKLK RIGLRLPRAH IHLHAHYEPG KGLVTGKIPL TKERFFALAD 


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Q5SKZ7 in FASTA format

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