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Protein

NADH-quinone oxidoreductase subunit 15

Gene

nqo15

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 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 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.1 Publication

Catalytic activityi

NADH + quinone = NAD+ + quinol.

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. NADH dehydrogenase (quinone) activity Source: UniProtKB-EC
  3. quinone binding Source: UniProtKB-KW

GO - Biological processi

  1. iron-sulfur cluster assembly Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-521-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 15 (EC:1.6.99.5)
Alternative name(s):
NADH dehydrogenase I chain 15
NDH-1 subunit 15
Gene namesi
Name:nqo15
Ordered Locus Names:TTHA0496
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: 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
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 129128NADH-quinone oxidoreductase subunit 15PRO_0000233014Add
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. 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 nqo4.2 Publications

Protein-protein interaction databases

DIPiDIP-59273N.
STRINGi300852.TTHA0496.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2622Combined sources
Beta strandi31 – 366Combined sources
Helixi38 – 414Combined sources
Beta strandi53 – 608Combined sources
Beta strandi62 – 643Combined sources
Beta strandi66 – 727Combined sources
Beta strandi75 – 795Combined sources
Beta strandi82 – 865Combined sources
Turni87 – 904Combined sources
Beta strandi91 – 988Combined sources
Turni99 – 1013Combined sources
Beta strandi102 – 1054Combined sources
Helixi112 – 12615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FUGX-ray3.307/H/Q/Z1-129[»]
2YBBelectron microscopy19.0071-129[»]
3I9VX-ray3.107/H1-129[»]
3IAMX-ray3.107/H1-129[»]
3IASX-ray3.157/H/Q/Z1-129[»]
3M9SX-ray4.507/J1-129[»]
4HEAX-ray3.307/I1-129[»]
ProteinModelPortaliQ5SKZ7.
SMRiQ5SKZ7. Positions 3-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SKZ7.

Family & Domainsi

Domaini

Has a similar fold to the mitochondrial iron chaperone frataxin.

Sequence similaritiesi

Belongs to the complex I nqo15 family.Curated

Phylogenomic databases

eggNOGiNOG43023.
HOGENOMiHOG000099234.
OMAiIYRMERP.
OrthoDBiEOG6NGVT2.

Family and domain databases

InterProiIPR002908. Frataxin/CyaY.
IPR021093. NADH_quinone_OxRdtase_su15.
[Graphical view]
PfamiPF11497. NADH_Oxid_Nqo15. 1 hit.
[Graphical view]
SUPFAMiSSF55387. SSF55387. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5SKZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASSERELY EAWVELLSWM REYAQAKGVR FEKEADFPDF IYRMERPYDL
60 70 80 90 100
PTTIMTASLS DGLGEPFLLA DVSPRHAKLK RIGLRLPRAH IHLHAHYEPG
110 120
KGLVTGKIPL TKERFFALAD RAREALAFA
Length:129
Mass (Da):14,788
Last modified:January 23, 2007 - v3
Checksum:iA944E174C0DE152C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70319.1.
RefSeqiYP_143762.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70319; BAD70319; BAD70319.
GeneIDi3169322.
KEGGittj:TTHA0496.
PATRICi23955967. VBITheThe93045_0494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70319.1.
RefSeqiYP_143762.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FUGX-ray3.307/H/Q/Z1-129[»]
2YBBelectron microscopy19.0071-129[»]
3I9VX-ray3.107/H1-129[»]
3IAMX-ray3.107/H1-129[»]
3IASX-ray3.157/H/Q/Z1-129[»]
3M9SX-ray4.507/J1-129[»]
4HEAX-ray3.307/I1-129[»]
ProteinModelPortaliQ5SKZ7.
SMRiQ5SKZ7. Positions 3-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59273N.
STRINGi300852.TTHA0496.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70319; BAD70319; BAD70319.
GeneIDi3169322.
KEGGittj:TTHA0496.
PATRICi23955967. VBITheThe93045_0494.

Phylogenomic databases

eggNOGiNOG43023.
HOGENOMiHOG000099234.
OMAiIYRMERP.
OrthoDBiEOG6NGVT2.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-521-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SKZ7.

Family and domain databases

InterProiIPR002908. Frataxin/CyaY.
IPR021093. NADH_quinone_OxRdtase_su15.
[Graphical view]
PfamiPF11497. NADH_Oxid_Nqo15. 1 hit.
[Graphical view]
SUPFAMiSSF55387. SSF55387. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "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: PROTEIN SEQUENCE OF 2-9, CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
  3. "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), FUNCTION, SUBUNIT, ELECTRON TRANSFER MECHANISM.

Entry informationi

Entry nameiNQO15_THET8
AccessioniPrimary (citable) accession number: Q5SKZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 69 of the entry and version 3 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.