NADH-quinone oxidoreductase subunit 4 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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Reviewed, UniProtKB/Swiss-Prot Q56220 (NQO4_THET8)

Last modified June 16, 2009. Version 61. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit 4
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I chain 4
    NDH-1 subunit 4

Gene names

Name:	nqo4
Ordered Locus Names:	TTHA0087

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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 nqo4 subunit may contain the quinone-binding site. HAMAP MF_01358
Catalytic activity	NADH + quinone = NAD⁺ + quinol. HAMAP MF_01358
Subunit structure	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. Subunit nqo4 interacts extensively with nqo6. Ref.3 Ref.4
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. HAMAP MF_01358
Sequence similarities	Belongs to the complex I 49 kDa subunit family.

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Ontologies

Keywords
Biological process	Transport
Cellular component	Cell membrane Membrane
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: HAMAP photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 409

409

NADH-quinone oxidoreductase subunit 4 HAMAP MF_01358

PRO_0000118617

Secondary structure

409

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q56220-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 161AA0C796D62ED3
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FASTA

409

46,371

        10         20         30         40         50         60 
MREEFLEEIP LDAPPEEAKE LRTEVMTLNV GPQHPSTHGV LRLMVTLSGE EVLEVVPHIG 

        70         80         90        100        110        120 
YLHTGFEKTM EHRTYLQNIT YTPRMDYLHS FAHDLAYALA VEKLLGAVVP PRAETIRVIL 

       130        140        150        160        170        180 
NELSRLASHL VFLGTGLLDL GALTPFFYAF RERETILDLF EWVTGQRFHH NYIRIGGVKE 

       190        200        210        220        230        240 
DLPEEFVPEL KKLLEVLPHR IDEYEALFAE SPIFYERARG VGVIPPEVAI DLGLTGGSLR 

       250        260        270        280        290        300 
ASGVNYDVRK AYPYSGYETY TFDVPLGERG DVFDRMLVRI REMRESVKII KQALERLEPG 

       310        320        330        340        350        360 
PVRDPNPQIT PPPRHLLETS MEAVIYHFKH YTEGFHPPKG EVYVPTESAR GELGYYIVSD 

       370        380        390        400 
GGSMPYRVKV RAPSFVNLQS LPYACKGEQV PDMVAIIASL DPVMGDVDR

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9020134] [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].
[3]	"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: 16584177] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-8, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
[4]	"Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus." Sazanov L.A., Hinchliffe P. Science 311:1430-1436(2006) [PubMed: 16469879] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT, ELECTRON TRANSFER MECHANISM.

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Cross-references

Sequence databases

U52917 Genomic DNA. Translation: AAA97941.1.
AP008226 Genomic DNA. Translation: BAD69910.1.

PIR

T11901.

RefSeq

YP_143353.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FUG	X-ray	3.30	4/D/M/V	1-409	[»]

ModBase

Search...

Protein family/group databases

TCDB

3.D.1.3.1. proton-translocating NADH dehydrogenase (NDH) family.

Genome annotation databases

GeneID

3168206.

GenomeReviews

Gene locus TTHA0087 in contig AP008226_GR.

KEGG

ttj:TTHA0087.

NMPDR

fig|300852.3.peg.118.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q56220.

OMA

Q56220. PYTDRLN.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0087-MON.

Family and domain databases

HAMAP

MF_01358.
[Tree]

InterPro

IPR010219. NADH_DH_1_dsu.
IPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_su-49kDa_CS.
[Graphical view]

Pfam

PF00346. Complex1_49kDa. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01962. NuoD. 1 hit.

PROSITE

PS00535. COMPLEX1_49K. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

NQO4_THET8

Accession

Primary (citable) accession number: Q56220
Secondary accession number(s): Q5SM56

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families