Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADH-quinone oxidoreductase subunit 13

Gene

nqo13

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

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 13 (EC:1.6.5.11)
Alternative name(s):
NADH dehydrogenase I chain 13
NDH-1 subunit 13
Gene namesi
Name:nqo13
Ordered Locus Names:TTHA0096
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 – 21HelicalSequence analysisAdd BLAST21
Transmembranei23 – 43HelicalSequence analysisAdd BLAST21
Transmembranei47 – 67HelicalSequence analysisAdd BLAST21
Transmembranei69 – 89HelicalSequence analysisAdd BLAST21
Transmembranei91 – 111HelicalSequence analysisAdd BLAST21
Transmembranei115 – 135HelicalSequence analysisAdd BLAST21
Transmembranei144 – 164HelicalSequence analysisAdd BLAST21
Transmembranei190 – 210HelicalSequence analysisAdd BLAST21
Transmembranei258 – 278HelicalSequence analysisAdd BLAST21
Transmembranei284 – 304HelicalSequence analysisAdd BLAST21
Transmembranei308 – 328HelicalSequence analysisAdd BLAST21
Transmembranei354 – 374HelicalSequence analysisAdd BLAST21
Transmembranei390 – 410HelicalSequence analysisAdd BLAST21
Transmembranei430 – 450HelicalSequence analysisAdd 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_00001180381 – 469NADH-quinone oxidoreductase subunit 13Add BLAST469

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-59271N.
STRINGi300852.TTHA0096.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 17Combined sources16
Helixi23 – 40Combined sources18
Beta strandi45 – 47Combined sources3
Beta strandi51 – 56Combined sources6
Turni57 – 59Combined sources3
Beta strandi62 – 65Combined sources4
Helixi69 – 88Combined sources20
Helixi96 – 111Combined sources16
Helixi115 – 124Combined sources10
Helixi126 – 134Combined sources9
Helixi141 – 168Combined sources28
Turni169 – 171Combined sources3
Beta strandi173 – 176Combined sources4
Helixi177 – 182Combined sources6
Turni187 – 189Combined sources3
Helixi190 – 203Combined sources14
Turni204 – 206Combined sources3
Helixi208 – 210Combined sources3
Helixi214 – 220Combined sources7
Helixi226 – 233Combined sources8
Helixi237 – 243Combined sources7
Helixi245 – 248Combined sources4
Helixi250 – 274Combined sources25
Helixi275 – 277Combined sources3
Helixi281 – 301Combined sources21
Helixi305 – 336Combined sources32
Beta strandi340 – 344Combined sources5
Turni347 – 350Combined sources4
Helixi354 – 365Combined sources12
Helixi373 – 387Combined sources15
Helixi389 – 396Combined sources8
Helixi399 – 413Combined sources15
Beta strandi416 – 418Combined sources3
Helixi427 – 445Combined sources19
Turni447 – 453Combined sources7
Helixi454 – 463Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HE8X-ray3.30G/M1-469[»]
4HEAX-ray3.30M/U1-469[»]
ProteinModelPortaliQ56228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 4 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107WFQ. Bacteria.
COG1008. LUCA.
HOGENOMiHOG000100683.
KOiK00342.
OMAiIQTPWSY.
PhylomeDBiQ56228.

Family and domain databases

InterProiIPR010227. NADH_Q_OxRdtase_chainM/4.
IPR003918. NADH_UbQ_OxRdtase.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]
PRINTSiPR01437. NUOXDRDTASE4.
TIGRFAMsiTIGR01972. NDH_I_M. 1 hit.

Sequencei

Sequence statusi: Complete.

Q56228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVLAVLLPV VFGALLLLGL PRALGVLGAG LSFLLNLYLF LTHPGGVAHA
60 70 80 90 100
FQAPLLPGAG VYWAFGLDGL SALFFLTIAL TVFLGALVAR VEGRFLGLAL
110 120 130 140 150
LMEGLLLGLF AARDLLVFYV FFEAALIPAL LMLYLYGGEG RTRALYTFVL
160 170 180 190 200
FTLVGSLPML AAVLGARLLS GSPTFLLEDL LAHPLQEEAA FWVFLGFALA
210 220 230 240 250
FAIKTPLFPL HAWLPPFHQE NHPSGLADAL GTLYKVGVFA FFRFAIPLAP
260 270 280 290 300
EGFAQAQGLL LFLAALSALY GAWVAFAAKD FKTLLAYAGL SHMGVAALGV
310 320 330 340 350
FSGTPEGAMG GLYLLAASGV YTGGLFLLAG RLYERTGTLE IGRYRGLAQS
360 370 380 390 400
APGLAALALI LFLAMVGLPG LSGFPGEFLT LLGAYKASPW LAALAFLSVI
410 420 430 440 450
ASAAYALTAF QKTFWEEGGS GVKDLAGAEW GFALLSVLAL LLMGVFPGYF
460
ARGLHPLAEA FAKLLGGGA
Length:469
Mass (Da):49,219
Last modified:March 29, 2005 - v2
Checksum:i5FD2D14713790224
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti166A → D in AAA97950 (PubMed:9020134).Curated1
Sequence conflicti202A → D in AAA97950 (PubMed:9020134).Curated1
Sequence conflicti240A → D in AAA97950 (PubMed:9020134).Curated1
Sequence conflicti245A → D in AAA97950 (PubMed:9020134).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52917 Genomic DNA. Translation: AAA97950.1.
AP008226 Genomic DNA. Translation: BAD69919.1.
PIRiT11910.
RefSeqiWP_011227706.1. NC_006461.1.
YP_143362.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD69919; BAD69919; BAD69919.
GeneIDi3169618.
KEGGittj:TTHA0096.
PATRICi23955123. VBITheThe93045_0094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52917 Genomic DNA. Translation: AAA97950.1.
AP008226 Genomic DNA. Translation: BAD69919.1.
PIRiT11910.
RefSeqiWP_011227706.1. NC_006461.1.
YP_143362.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HE8X-ray3.30G/M1-469[»]
4HEAX-ray3.30M/U1-469[»]
ProteinModelPortaliQ56228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59271N.
STRINGi300852.TTHA0096.

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

EnsemblBacteriaiBAD69919; BAD69919; BAD69919.
GeneIDi3169618.
KEGGittj:TTHA0096.
PATRICi23955123. VBITheThe93045_0094.

Phylogenomic databases

eggNOGiENOG4107WFQ. Bacteria.
COG1008. LUCA.
HOGENOMiHOG000100683.
KOiK00342.
OMAiIQTPWSY.
PhylomeDBiQ56228.

Family and domain databases

InterProiIPR010227. NADH_Q_OxRdtase_chainM/4.
IPR003918. NADH_UbQ_OxRdtase.
IPR001750. ND/Mrp_mem.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
[Graphical view]
PRINTSiPR01437. NUOXDRDTASE4.
TIGRFAMsiTIGR01972. NDH_I_M. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNQO13_THET8
AccessioniPrimary (citable) accession number: Q56228
Secondary accession number(s): Q5SM47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 29, 2005
Last modified: November 2, 2016
This is version 109 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.