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UniProtKB/Swiss-Prot entry Q56229


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

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Entry information
Entry name NQO14_THET8
Primary accession number Q56229
Secondary accession number Q5SM46
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on March 29, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 52)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit 14
Synonyms EC 1.6.99.5
NADH dehydrogenase I chain 14
NDH-1 subunit 14
Gene name
Name: nqo14
OrderedLocusNames: TTHA0097
From
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [TaxID: 300852] [HAMAP proteome]
Taxonomy Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
Protein existence 3: Inferred from homology;
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.
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.
  • 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.
  • SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
  • SIMILARITY: Belongs to the complex I subunit 2 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
U52917; AAA97951.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008226; BAD69920.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T11911; T11911.
RefSeq YP_143363.1; -.
3D structure databases
ModBase Q56229.
Enzyme and pathway databases
BioCyc TTHE300852:TTHA0097-MON; -.
Family and domain databases
InterPro IPR003916; NADHub_OxRdtase_5.
IPR001750; Oxidored_q1.
IPR010096; Prot-transl_NADH-Q_OxRdtase_N.
Graphical view of domain structure.
Pfam PF00361; Oxidored_q1; 1.
Pfam graphical view of domain structure.
PRINTS PR01434; NADHDHGNASE5.
TIGRFAMs TIGR01770; NDH_I_N; 1.
BLOCKS Q56229.
Genome annotation databases
GeneID 3169623; -.
GenomeReviews AP008226_GR; TTHA0097.
KEGG ttj:TTHA0097; -.
NMPDR fig|300852.3.peg.128; -.
Phylogenomic databases
HOGENOM Q56229; -.
Genome annotation databases
CMR Q56229; TTHA0097.
Other
ProtoNet Q56229.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; Oxidoreductase; Quinone; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   427  427     NADH-quinone oxidoreductase subunit 14. PRO_0000117687
TRANSMEM   1    21  21     Potential. 
TRANSMEM   30    50  21     Potential. 
TRANSMEM   57    77  21     Potential. 
TRANSMEM   80   100  21     Potential. 
TRANSMEM   104   124  21     Potential. 
TRANSMEM   137   157  21     Potential. 
TRANSMEM   172   192  21     Potential. 
TRANSMEM   204   224  21     Potential. 
TRANSMEM   230   250  21     Potential. 
TRANSMEM   257   277  21     Potential. 
TRANSMEM   280   300  21     Potential. 
TRANSMEM   322   342  21     Potential. 
TRANSMEM   360   380  21     Potential. 
TRANSMEM   400   420  21     Potential. 
CONFLICT   81    81        R -> G (in Ref. 1; AAA97951). 
CONFLICT   157   157        A -> D (in Ref. 1; AAA97951). 
CONFLICT   233   233        L -> V (in Ref. 1; AAA97951). 
CONFLICT   407   427        VLLLALGLLPGLVLPALAAGG -> SSSSPWGSSPASSSPPWPRGVKITP (in Ref. 1; AAA97951). 
Sequence information
Length: 427 AA [This is the length of the unprocessed precursor] Molecular weight: 44436 Da [This is the MW of the unprocessed precursor] CRC64: 9AD943608E5C2759 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTLAILAVFS VALTLLGFVL PPQGVKRATL LGLALALASL LLTWGKPFAF GPYAVDGVSQ 

        70         80         90        100        110        120 
VFTLLALLGA LWTVGLVRSG RFEFYLLVLY AALGMHLLAS TRHLLLMLVA LEALSLPLYA 

       130        140        150        160        170        180 
LATWRRGQGL EAALKYFLLG ALAAAFFLYG AALFYGATGS LVLGAPGEGP LYALALGLLL 

       190        200        210        220        230        240 
VGLGFKAALA PFHFWTPDVY QGSPTPVVLF MATSVKAAAF AALLRVAAPP EALALLVALS 

       250        260        270        280        290        300 
VVVGNLAALA QKEAKRLLAY SSIAHAGYMA LALYTGNAQA LGFYLLTYVL ATGLAFAVLS 

       310        320        330        340        350        360 
QISPDRVPLE ALRGLYRKDP LLGLAFLVAM LSLLGLPPLA GFWGKYLAFA EAARAGAWGV 

       370        380        390        400        410        420 
LVLALVTSAV SAYYYLGLGL AVFARPEETP FRPGPPWARA AVVAAGVLLL ALGLLPGLVL 


PALAAGG 

Q56229 in FASTA format

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