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Q56228

- NQO13_THET8

UniProt

Q56228 - NQO13_THET8

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Protein

NADH-quinone oxidoreductase subunit 13

Gene

nqo13

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - 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 + quinone = NAD+ + quinol.

GO - Molecular functioni

  1. NADH dehydrogenase (ubiquinone) activity Source: InterPro
  2. quinone binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP synthesis coupled electron transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-100-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 13 (EC:1.6.99.5)
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
ProteomesiUP000000532: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2121HelicalSequence AnalysisAdd
BLAST
Transmembranei23 – 4321HelicalSequence AnalysisAdd
BLAST
Transmembranei47 – 6721HelicalSequence AnalysisAdd
BLAST
Transmembranei69 – 8921HelicalSequence AnalysisAdd
BLAST
Transmembranei91 – 11121HelicalSequence AnalysisAdd
BLAST
Transmembranei115 – 13521HelicalSequence AnalysisAdd
BLAST
Transmembranei144 – 16421HelicalSequence AnalysisAdd
BLAST
Transmembranei190 – 21021HelicalSequence AnalysisAdd
BLAST
Transmembranei258 – 27821HelicalSequence AnalysisAdd
BLAST
Transmembranei284 – 30421HelicalSequence AnalysisAdd
BLAST
Transmembranei308 – 32821HelicalSequence AnalysisAdd
BLAST
Transmembranei354 – 37421HelicalSequence AnalysisAdd
BLAST
Transmembranei390 – 41021HelicalSequence AnalysisAdd
BLAST
Transmembranei430 – 45021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469NADH-quinone oxidoreductase subunit 13PRO_0000118038Add
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.

Protein-protein interaction databases

DIPiDIP-59271N.
STRINGi300852.TTHA0096.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1716Combined sources
Helixi23 – 4018Combined sources
Beta strandi45 – 473Combined sources
Beta strandi51 – 566Combined sources
Turni57 – 593Combined sources
Beta strandi62 – 654Combined sources
Helixi69 – 8820Combined sources
Helixi96 – 11116Combined sources
Helixi115 – 12410Combined sources
Helixi126 – 1349Combined sources
Helixi141 – 16828Combined sources
Turni169 – 1713Combined sources
Beta strandi173 – 1764Combined sources
Helixi177 – 1826Combined sources
Turni187 – 1893Combined sources
Helixi190 – 20314Combined sources
Turni204 – 2063Combined sources
Helixi208 – 2103Combined sources
Helixi214 – 2207Combined sources
Helixi226 – 2338Combined sources
Helixi237 – 2437Combined sources
Helixi245 – 2484Combined sources
Helixi250 – 27425Combined sources
Helixi275 – 2773Combined sources
Helixi281 – 30121Combined sources
Helixi305 – 33632Combined sources
Beta strandi340 – 3445Combined sources
Turni347 – 3504Combined sources
Helixi354 – 36512Combined sources
Helixi373 – 38715Combined sources
Helixi389 – 3968Combined sources
Helixi399 – 41315Combined sources
Beta strandi416 – 4183Combined sources
Helixi427 – 44519Combined sources
Turni447 – 4537Combined sources
Helixi454 – 46310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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

eggNOGiCOG1008.
HOGENOMiHOG000100683.
KOiK00342.
OMAiFFMVGAT.
OrthoDBiEOG647TZ6.
PhylomeDBiQ56228.

Family and domain databases

InterProiIPR010227. NADH_Q_OxRdtase_chainM/4.
IPR001750. NADH_UbQ/plastoQ_OxRdtase.
IPR003918. NADH_UbQ_OxRdtase.
[Graphical view]
PfamiPF00361. Oxidored_q1. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661A → D in AAA97950. (PubMed:9020134)Curated
Sequence conflicti202 – 2021A → D in AAA97950. (PubMed:9020134)Curated
Sequence conflicti240 – 2401A → D in AAA97950. (PubMed:9020134)Curated
Sequence conflicti245 – 2451A → D in AAA97950. (PubMed:9020134)Curated

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 .
PIRi T11910.
RefSeqi WP_011227706.1. NC_006461.1.
YP_143362.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4HE8 X-ray 3.30 G/M 1-469 [» ]
4HEA X-ray 3.30 M/U 1-469 [» ]
ProteinModelPortali Q56228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59271N.
STRINGi 300852.TTHA0096.

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 BAD69919 ; BAD69919 ; BAD69919 .
GeneIDi 3169618.
KEGGi ttj:TTHA0096.
PATRICi 23955123. VBITheThe93045_0094.

Phylogenomic databases

eggNOGi COG1008.
HOGENOMi HOG000100683.
KOi K00342.
OMAi FFMVGAT.
OrthoDBi EOG647TZ6.
PhylomeDBi Q56228.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-100-MONOMER.

Family and domain databases

InterProi IPR010227. NADH_Q_OxRdtase_chainM/4.
IPR001750. NADH_UbQ/plastoQ_OxRdtase.
IPR003918. NADH_UbQ_OxRdtase.
[Graphical view ]
Pfami PF00361. Oxidored_q1. 1 hit.
[Graphical view ]
PRINTSi PR01437. NUOXDRDTASE4.
TIGRFAMsi TIGR01972. NDH_I_M. 1 hit.
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.

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 26, 2014
This is version 98 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

External Data

Dasty 3