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Q56222

- NQO1_THET8

UniProt

Q56222 - NQO1_THET8

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Protein

NADH-quinone oxidoreductase subunit 1

Gene

nqo1

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

Protein has several cofactor binding sites:
  • FMNNote: Binds 1 FMN per subunit.
  • [4Fe-4S] clusterNote: 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 – 971NADCurated
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 – 694NADCurated
Nucleotide bindingi92 – 965FMN
Nucleotide bindingi180 – 1856NADCurated
Nucleotide bindingi218 – 2203FMN

GO - Molecular functioni

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

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

1
438
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi18 – 203Combined sources
Turni24 – 274Combined sources
Helixi29 – 346Combined sources
Turni35 – 384Combined sources
Helixi39 – 468Combined sources
Helixi50 – 589Combined sources
Turni59 – 613Combined sources
Turni65 – 684Combined sources
Helixi72 – 765Combined sources
Beta strandi81 – 833Combined sources
Beta strandi88 – 925Combined sources
Helixi103 – 1097Combined sources
Helixi111 – 12515Combined sources
Beta strandi129 – 1346Combined sources
Helixi139 – 15416Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 1643Combined sources
Beta strandi169 – 1757Combined sources
Helixi180 – 1834Combined sources
Helixi185 – 1928Combined sources
Beta strandi202 – 2043Combined sources
Turni206 – 2083Combined sources
Helixi211 – 2133Combined sources
Beta strandi216 – 2205Combined sources
Helixi221 – 2255Combined sources
Helixi227 – 2326Combined sources
Helixi235 – 2395Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi244 – 26017Combined sources
Beta strandi262 – 2676Combined sources
Helixi272 – 2776Combined sources
Turni278 – 2803Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi287 – 2915Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi300 – 3023Combined sources
Helixi304 – 3074Combined sources
Turni313 – 3164Combined sources
Helixi317 – 3193Combined sources
Beta strandi324 – 3329Combined sources
Helixi337 – 35115Combined sources
Helixi357 – 3604Combined sources
Helixi361 – 3655Combined sources
Helixi366 – 3749Combined sources
Turni375 – 3773Combined sources
Helixi381 – 39414Combined sources
Helixi402 – 42625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

Belongs to the complex I 51 kDa subunit family.Curated

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

        10         20         30         40         50
MTGPILSGLD PRFERTLYAH VGKEGSWTLD YYLRHGGYET AKRVLKEKTP
60 70 80 90 100
DEVIEEVKRS GLRGRGGAGF PTGLKWSFMP KDDGKQHYLI CNADESEPGS
110 120 130 140 150
FKDRYILEDV PHLLIEGMIL AGYAIRATVG YIYVRGEYRR AADRLEQAIK
160 170 180 190 200
EARARGYLGK NLFGTDFSFD LHVHRGAGAY ICGEETALMN SLEGLRANPR
210 220 230 240 250
LKPPFPAQSG LWGKPTTINN VETLASVVPI MERGADWFAQ MGTEQSKGMK
260 270 280 290 300
LYQISGPVKR PGVYELPMGT TFRELIYEWA GGPLEPIQAI IPGGSSTPPL
310 320 330 340 350
PFTEEVLDTP MSYEHLQAKG SMLGTGGVIL IPERVSMVDA MWNLTRFYAH
360 370 380 390 400
ESCGKCTPCR EGVAGFMVNL FAKIGTGQGE EKDVENLEAL LPLIEGRSFC
410 420 430
PLADAAVWPV KGSLRHFKDQ YLALAREKRP VPRPSLWR
Length:438
Mass (Da):48,632
Last modified:November 1, 1997 - v1
Checksum:i73ADB3AF31BBE4C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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: November 26, 2014
This is version 108 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