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Q5SKZ7

- NQO15_THET8

UniProt

Q5SKZ7 - NQO15_THET8

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Protein

NADH-quinone oxidoreductase subunit 15

Gene
nqo15, TTHA0496
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - 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: 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 – 2622
Beta strandi31 – 366
Helixi38 – 414
Beta strandi53 – 608
Beta strandi62 – 643
Beta strandi66 – 727
Beta strandi75 – 795
Beta strandi82 – 865
Turni87 – 904
Beta strandi91 – 988
Turni99 – 1013
Beta strandi102 – 1054
Helixi112 – 12615

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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.

Phylogenomic databases

eggNOGiNOG43023.
HOGENOMiHOG000099234.
OMAiYIYRMER.
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

MSASSERELY EAWVELLSWM REYAQAKGVR FEKEADFPDF IYRMERPYDL    50
PTTIMTASLS DGLGEPFLLA DVSPRHAKLK RIGLRLPRAH IHLHAHYEPG 100
KGLVTGKIPL TKERFFALAD RAREALAFA 129
Length:129
Mass (Da):14,788
Last modified:January 23, 2007 - v3
Checksum:iA944E174C0DE152C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70319.1.
RefSeqiWP_011227977.1. NC_006461.1.
YP_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:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70319.1 .
RefSeqi WP_011227977.1. NC_006461.1.
YP_143762.1. 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 7/H/Q/Z 1-129 [» ]
2YBB electron microscopy 19.00 7 1-129 [» ]
3I9V X-ray 3.10 7/H 1-129 [» ]
3IAM X-ray 3.10 7/H 1-129 [» ]
3IAS X-ray 3.15 7/H/Q/Z 1-129 [» ]
3M9S X-ray 4.50 7/J 1-129 [» ]
4HEA X-ray 3.30 7/I 1-129 [» ]
ProteinModelPortali Q5SKZ7.
SMRi Q5SKZ7. Positions 3-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59273N.
STRINGi 300852.TTHA0496.

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 BAD70319 ; BAD70319 ; BAD70319 .
GeneIDi 3169322.
KEGGi ttj:TTHA0496.
PATRICi 23955967. VBITheThe93045_0494.

Phylogenomic databases

eggNOGi NOG43023.
HOGENOMi HOG000099234.
OMAi YIYRMER.
OrthoDBi EOG6NGVT2.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-521-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SKZ7.

Family and domain databases

InterProi IPR002908. Frataxin/CyaY.
IPR021093. NADH_quinone_OxRdtase_su15.
[Graphical view ]
Pfami PF11497. NADH_Oxid_Nqo15. 1 hit.
[Graphical view ]
SUPFAMi SSF55387. SSF55387. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 63 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

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