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UniProtKB/Swiss-Prot entry Q56222


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

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Entry information
Entry name NQO1_THET8
Primary accession number Q56222
Secondary accession number Q5SM54
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 57)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit 1
Synonyms EC 1.6.99.5
NADH dehydrogenase I chain 1
NDH-1 subunit 1
Gene name
Name: nqo1
OrderedLocusNames: TTHA0089
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]
PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, EPR SPECTROSCOPY, 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 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.
  • COFACTOR: Binds 1 4Fe-4S cluster per subunit. This 4Fe-4S cluster is referred to as N3.
  • 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.
  • 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).
  • SIMILARITY: Belongs to the complex I 51 kDa subunit 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; AAA97943.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008226; BAD69912.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T11903; T11903.
RefSeq YP_143355.1; -.
3D structure databases
PDB
2FUG; X-ray; 3.30 A; 1/A/J/S=1-438.[ExPASy / RCSB / EBI]
PDBsum 2FUG; -.
ModBase Q56222.
Enzyme and pathway databases
BioCyc TTHE300852:TTHA0089-MON; -.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR001949; NADH-ubq_OxRdtase_51KDa_CS.
IPR011538; NADH-UbQ_OxRdtase_51KDa_su.
IPR011537; NADH-UbQ_OxRdtase_F_su.
Graphical view of domain structure.
Pfam PF01512; Complex1_51K; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01959; nuoF_fam; 1.
PROSITE PS00644; COMPLEX1_51K_1; 1.
PS00645; COMPLEX1_51K_2; 1.
BLOCKS Q56222.
Genome annotation databases
GeneID 3168453; -.
GenomeReviews AP008226_GR; TTHA0089.
KEGG ttj:TTHA0089; -.
NMPDR fig|300852.3.peg.120; -.
Phylogenomic databases
HOGENOM Q56222; -.
Genome annotation databases
CMR Q56222; TTHA0089.
Other
ProtoNet Q56222.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Cell membrane; Complete proteome; Direct protein sequencing; Flavoprotein; FMN; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   438  438     NADH-quinone oxidoreductase subunit 1. PRO_0000118567
NP_BIND   66    69  4     NAD (Probable). 
NP_BIND   92    96  5     FMN. 
NP_BIND   180   185  6     NAD (Probable). 
NP_BIND   218   220  3     FMN. 
METAL   353   353        Iron-sulfur (4Fe-4S). 
METAL   356   356        Iron-sulfur (4Fe-4S). 
METAL   359   359        Iron-sulfur (4Fe-4S). 
METAL   400   400        Iron-sulfur (4Fe-4S). 
BINDING   75    75        FMN. 
BINDING   97    97        NAD (Probable). 
HELIX   29    33  5      
TURN   34    38  5      
HELIX   39    47  9      
HELIX   50    58  9      
TURN   59    61  3      
HELIX   72    77  6      
STRAND   81    83  3      
STRAND   88    93  6      
HELIX   103   109  7      
HELIX   111   124  14      
STRAND   128   134  7      
HELIX   139   154  16      
STRAND   157   161  5      
STRAND   169   175  7      
HELIX   180   183  4      
HELIX   185   192  8      
STRAND   202   204  3      
TURN   206   208  3      
HELIX   211   213  3      
STRAND   216   220  5      
HELIX   221   232  12      
HELIX   235   239  5      
STRAND   240   242  3      
STRAND   247   260  14      
STRAND   262   267  6      
HELIX   272   276  5      
TURN   277   280  4      
STRAND   283   285  3      
STRAND   287   291  5      
HELIX   304   307  4      
TURN   313   320  8      
STRAND   327   332  6      
HELIX   337   351  15      
HELIX   357   361  5      
HELIX   362   366  5      
HELIX   367   374  8      
HELIX   381   395  15      
HELIX   402   426  25      
Sequence information
Length: 438 AA [This is the length of the unprocessed precursor] Molecular weight: 48632 Da [This is the MW of the unprocessed precursor] CRC64: 73ADB3AF31BBE4C0 [This is a checksum on the sequence]
        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 

Q56222 in FASTA format

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