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Q56222

- NQO1_THET8

UniProt

Q56222 - NQO1_THET8

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Protein
NADH-quinone oxidoreductase subunit 1
Gene
nqo1, TTHA0089
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

NADH + quinone = NAD+ + quinol.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751FMN
Binding sitei97 – 971NAD Inferred
Metal bindingi353 – 3531Iron-sulfur (4Fe-4S)
Metal bindingi356 – 3561Iron-sulfur (4Fe-4S)
Metal bindingi359 – 3591Iron-sulfur (4Fe-4S)
Metal bindingi400 – 4001Iron-sulfur (4Fe-4S)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 694NAD Inferred
Nucleotide bindingi92 – 965FMN
Nucleotide bindingi180 – 1856NAD Inferred
Nucleotide bindingi218 – 2203FMN

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. FMN binding Source: InterPro
  3. NAD binding Source: InterPro
  4. NADH dehydrogenase (ubiquinone) activity Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. quinone binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    4Fe-4S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-93-MONOMER.

    Protein family/group databases

    TCDBi3.D.1.3.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH-quinone oxidoreductase subunit 1 (EC:1.6.99.5)
    Alternative name(s):
    NADH dehydrogenase I chain 1
    NDH-1 subunit 1
    Gene namesi
    Name:nqo1
    Ordered Locus Names:TTHA0089
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438NADH-quinone oxidoreductase subunit 1
    PRO_0000118567Add
    BLAST

    Keywords - PTMi

    Quinone

    Interactioni

    Subunit structurei

    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.2 Publications

    Protein-protein interaction databases

    DIPiDIP-59259N.
    STRINGi300852.TTHA0089.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi18 – 203
    Turni24 – 274
    Helixi29 – 346
    Turni35 – 384
    Helixi39 – 468
    Helixi50 – 589
    Turni59 – 613
    Turni65 – 684
    Helixi72 – 765
    Beta strandi81 – 833
    Beta strandi88 – 925
    Helixi103 – 1097
    Helixi111 – 12515
    Beta strandi129 – 1346
    Helixi139 – 15416
    Beta strandi157 – 1593
    Helixi162 – 1643
    Beta strandi169 – 1757
    Helixi180 – 1834
    Helixi185 – 1928
    Beta strandi202 – 2043
    Turni206 – 2083
    Helixi211 – 2133
    Beta strandi216 – 2205
    Helixi221 – 2255
    Helixi227 – 2326
    Helixi235 – 2395
    Beta strandi240 – 2423
    Beta strandi244 – 26017
    Beta strandi262 – 2676
    Helixi272 – 2776
    Turni278 – 2803
    Beta strandi283 – 2853
    Beta strandi287 – 2915
    Beta strandi293 – 2975
    Beta strandi300 – 3023
    Helixi304 – 3074
    Turni313 – 3164
    Helixi317 – 3193
    Beta strandi324 – 3329
    Helixi337 – 35115
    Helixi357 – 3604
    Helixi361 – 3655
    Helixi366 – 3749
    Turni375 – 3773
    Helixi381 – 39414
    Helixi402 – 42625

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ56222.
    SMRiQ56222. Positions 7-438.

    Miscellaneous databases

    EvolutionaryTraceiQ56222.

    Family & Domainsi

    Domaini

    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 similaritiesi

    Phylogenomic databases

    eggNOGiCOG1894.
    HOGENOMiHOG000251534.
    KOiK00335.
    OMAiHEIGMVP.
    OrthoDBiEOG6W9XGK.
    PhylomeDBiQ56222.

    Family and domain databases

    InterProiIPR001949. 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]
    PfamiPF01512. Complex1_51K. 1 hit.
    PF10589. NADH_4Fe-4S. 1 hit.
    PF10531. SLBB. 1 hit.
    [Graphical view]
    SMARTiSM00928. NADH_4Fe-4S. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01959. nuoF_fam. 1 hit.
    PROSITEiPS00644. COMPLEX1_51K_1. 1 hit.
    PS00645. COMPLEX1_51K_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q56222-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGPILSGLD PRFERTLYAH VGKEGSWTLD YYLRHGGYET AKRVLKEKTP    50
    DEVIEEVKRS GLRGRGGAGF PTGLKWSFMP KDDGKQHYLI CNADESEPGS 100
    FKDRYILEDV PHLLIEGMIL AGYAIRATVG YIYVRGEYRR AADRLEQAIK 150
    EARARGYLGK NLFGTDFSFD LHVHRGAGAY ICGEETALMN SLEGLRANPR 200
    LKPPFPAQSG LWGKPTTINN VETLASVVPI MERGADWFAQ MGTEQSKGMK 250
    LYQISGPVKR PGVYELPMGT TFRELIYEWA GGPLEPIQAI IPGGSSTPPL 300
    PFTEEVLDTP MSYEHLQAKG SMLGTGGVIL IPERVSMVDA MWNLTRFYAH 350
    ESCGKCTPCR EGVAGFMVNL FAKIGTGQGE EKDVENLEAL LPLIEGRSFC 400
    PLADAAVWPV KGSLRHFKDQ YLALAREKRP VPRPSLWR 438
    Length:438
    Mass (Da):48,632
    Last modified:November 1, 1997 - v1
    Checksum:i73ADB3AF31BBE4C0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52917 Genomic DNA. Translation: AAA97943.1.
    AP008226 Genomic DNA. Translation: BAD69912.1.
    PIRiT11903.
    RefSeqiWP_011227700.1. NC_006461.1.
    YP_143355.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD69912; BAD69912; BAD69912.
    GeneIDi3168453.
    KEGGittj:TTHA0089.
    PATRICi23955109. VBITheThe93045_0087.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52917 Genomic DNA. Translation: AAA97943.1 .
    AP008226 Genomic DNA. Translation: BAD69912.1 .
    PIRi T11903.
    RefSeqi WP_011227700.1. NC_006461.1.
    YP_143355.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FUG X-ray 3.30 1/A/J/S 1-438 [» ]
    2YBB electron microscopy 19.00 1 1-438 [» ]
    3I9V X-ray 3.10 1/A 1-438 [» ]
    3IAM X-ray 3.10 1/A 1-438 [» ]
    3IAS X-ray 3.15 1/A/J/S 1-438 [» ]
    3M9S X-ray 4.50 1/A 1-438 [» ]
    4HEA X-ray 3.30 1/B 1-438 [» ]
    ProteinModelPortali Q56222.
    SMRi Q56222. Positions 7-438.
    ModBasei Search...

    Protein-protein interaction databases

    DIPi DIP-59259N.
    STRINGi 300852.TTHA0089.

    Protein family/group databases

    TCDBi 3.D.1.3.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD69912 ; BAD69912 ; BAD69912 .
    GeneIDi 3168453.
    KEGGi ttj:TTHA0089.
    PATRICi 23955109. VBITheThe93045_0087.

    Phylogenomic databases

    eggNOGi COG1894.
    HOGENOMi HOG000251534.
    KOi K00335.
    OMAi HEIGMVP.
    OrthoDBi EOG6W9XGK.
    PhylomeDBi Q56222.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-93-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q56222.

    Family and domain databases

    InterProi IPR001949. 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 ]
    Pfami PF01512. Complex1_51K. 1 hit.
    PF10589. NADH_4Fe-4S. 1 hit.
    PF10531. SLBB. 1 hit.
    [Graphical view ]
    SMARTi SM00928. NADH_4Fe-4S. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01959. nuoF_fam. 1 hit.
    PROSITEi PS00644. COMPLEX1_51K_1. 1 hit.
    PS00645. COMPLEX1_51K_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    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.

    Entry informationi

    Entry nameiNQO1_THET8
    AccessioniPrimary (citable) accession number: Q56222
    Secondary accession number(s): Q5SM54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: September 3, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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