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Protein

NADH-quinone oxidoreductase subunit 14

Gene

nqo14

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.

Catalytic activityi

NADH + a quinone = NAD+ + a quinol.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Transport

Keywords - Ligandi

NAD

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 14 (EC:1.6.5.11UniRule annotation)
Alternative name(s):
NADH dehydrogenase I chain 14
NDH-1 subunit 14
Gene namesi
Name:nqo14
Ordered Locus Names:TTHA0097
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei1 – 21HelicalUniRule annotationAdd BLAST21
Transmembranei30 – 50HelicalUniRule annotationAdd BLAST21
Transmembranei57 – 77HelicalUniRule annotationAdd BLAST21
Transmembranei79 – 99HelicalUniRule annotationAdd BLAST21
Transmembranei104 – 124HelicalUniRule annotationAdd BLAST21
Transmembranei137 – 157HelicalUniRule annotationAdd BLAST21
Transmembranei172 – 192HelicalUniRule annotationAdd BLAST21
Transmembranei204 – 224HelicalUniRule annotationAdd BLAST21
Transmembranei230 – 250HelicalUniRule annotationAdd BLAST21
Transmembranei257 – 277HelicalUniRule annotationAdd BLAST21
Transmembranei280 – 300HelicalUniRule annotationAdd BLAST21
Transmembranei322 – 342HelicalUniRule annotationAdd BLAST21
Transmembranei360 – 380HelicalUniRule annotationAdd BLAST21
Transmembranei400 – 420HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001176871 – 427NADH-quinone oxidoreductase subunit 14Add BLAST427

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.

Protein-protein interaction databases

DIPiDIP-59272N.
STRINGi300852.TTHA0097.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 16Combined sources15
Turni17 – 19Combined sources3
Helixi22 – 42Combined sources21
Turni43 – 45Combined sources3
Beta strandi51 – 56Combined sources6
Helixi57 – 75Combined sources19
Helixi83 – 99Combined sources17
Helixi104 – 121Combined sources18
Helixi127 – 157Combined sources31
Helixi170 – 186Combined sources17
Helixi195 – 202Combined sources8
Helixi205 – 225Combined sources21
Helixi230 – 249Combined sources20
Helixi254 – 269Combined sources16
Helixi270 – 273Combined sources4
Turni274 – 276Combined sources3
Helixi279 – 302Combined sources24
Helixi309 – 312Combined sources4
Helixi315 – 318Combined sources4
Helixi320 – 334Combined sources15
Helixi340 – 355Combined sources16
Helixi358 – 370Combined sources13
Helixi372 – 379Combined sources8
Helixi381 – 383Combined sources3
Helixi396 – 414Combined sources19
Turni416 – 419Combined sources4
Helixi420 – 422Combined sources3
Beta strandi423 – 425Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HE8X-ray3.30I/N1-427[»]
4HEAX-ray3.30N/V1-427[»]
ProteinModelPortaliQ56229.
SMRiQ56229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 2 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CNR. Bacteria.
COG1007. LUCA.
HOGENOMiHOG000100794.
KOiK00343.
OMAiYALATWR.
PhylomeDBiQ56229.

Family and domain databases

HAMAPiMF_00445. NDH1_NuoN_1. 1 hit.
InterProiIPR010096. NADH-Q_OxRdtase_suN/2.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q56229-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLAILAVFS VALTLLGFVL PPQGVKRATL LGLALALASL LLTWGKPFAF
60 70 80 90 100
GPYAVDGVSQ VFTLLALLGA LWTVGLVRSG RFEFYLLVLY AALGMHLLAS
110 120 130 140 150
TRHLLLMLVA LEALSLPLYA LATWRRGQGL EAALKYFLLG ALAAAFFLYG
160 170 180 190 200
AALFYGATGS LVLGAPGEGP LYALALGLLL VGLGFKAALA PFHFWTPDVY
210 220 230 240 250
QGSPTPVVLF MATSVKAAAF AALLRVAAPP EALALLVALS VVVGNLAALA
260 270 280 290 300
QKEAKRLLAY SSIAHAGYMA LALYTGNAQA LGFYLLTYVL ATGLAFAVLS
310 320 330 340 350
QISPDRVPLE ALRGLYRKDP LLGLAFLVAM LSLLGLPPLA GFWGKYLAFA
360 370 380 390 400
EAARAGAWGV LVLALVTSAV SAYYYLGLGL AVFARPEETP FRPGPPWARA
410 420
AVVAAGVLLL ALGLLPGLVL PALAAGG
Length:427
Mass (Da):44,436
Last modified:March 29, 2005 - v2
Checksum:i9AD943608E5C2759
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti81R → G in AAA97951 (PubMed:9020134).Curated1
Sequence conflicti157A → D in AAA97951 (PubMed:9020134).Curated1
Sequence conflicti233L → V in AAA97951 (PubMed:9020134).Curated1
Sequence conflicti407 – 427VLLLA…LAAGG → SSSSPWGSSPASSSPPWPRG VKITP in AAA97951 (PubMed:9020134).CuratedAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52917 Genomic DNA. Translation: AAA97951.1.
AP008226 Genomic DNA. Translation: BAD69920.1.
PIRiT11911.
RefSeqiWP_011227707.1. NC_006461.1.
YP_143363.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD69920; BAD69920; BAD69920.
GeneIDi3169623.
KEGGittj:TTHA0097.
PATRICi23955125. VBITheThe93045_0095.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52917 Genomic DNA. Translation: AAA97951.1.
AP008226 Genomic DNA. Translation: BAD69920.1.
PIRiT11911.
RefSeqiWP_011227707.1. NC_006461.1.
YP_143363.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HE8X-ray3.30I/N1-427[»]
4HEAX-ray3.30N/V1-427[»]
ProteinModelPortaliQ56229.
SMRiQ56229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59272N.
STRINGi300852.TTHA0097.

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

EnsemblBacteriaiBAD69920; BAD69920; BAD69920.
GeneIDi3169623.
KEGGittj:TTHA0097.
PATRICi23955125. VBITheThe93045_0095.

Phylogenomic databases

eggNOGiENOG4105CNR. Bacteria.
COG1007. LUCA.
HOGENOMiHOG000100794.
KOiK00343.
OMAiYALATWR.
PhylomeDBiQ56229.

Family and domain databases

HAMAPiMF_00445. NDH1_NuoN_1. 1 hit.
InterProiIPR010096. NADH-Q_OxRdtase_suN/2.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNQO14_THET8
AccessioniPrimary (citable) accession number: Q56229
Secondary accession number(s): Q5SM46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 29, 2005
Last modified: November 2, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.