Reviewed, UniProtKB/Swiss-Prot Q72GC9 (NQO6_THET2)

Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit 6
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit 6
    NDH-1 subunit 6

Gene names

Name:	nqo6
Ordered Locus Names:	TT_C1919

Organism

Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]

Taxonomic identifier

262724 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP MF_01356
Cofactor	Binds 1 4Fe-4S cluster per subunit. This 4Fe-4S cluster is referred to as N2 By similarity.
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 nqo6 interacts extensively with nqo4 By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: HAMAP photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP
Cellular component	internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: HAMAP quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 181	181	NADH-quinone oxidoreductase subunit 6 HAMAP MF_01356		PRO_0000358501
Sites
	Metal binding	45	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	46	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	111	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	140	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72GC9-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A1E030366E6692F1	FASTA	181	20,239
	10 20 30 40 50 60 MALKDLFERD VQELEREGIL FTTLEKLVAW GRSNSLWPAT FGLACCAIEM MASTDARNDL 70 80 90 100 110 120 ARFGSEVFRA SPRQADVMIV AGRLSKKMAP VMRRVWEQMP DPKWVISMGA CASSGGMFNN 130 140 150 160 170 180 YAIVQNVDSV VPVDVYVPGC PPRPEALIYA VMQLQKKVRG QAYNERGERL PPVAAWKRTR G

References

[1]

"The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017221 Genomic DNA. Translation: AAS82261.1.
RefSeq	YP_005888.1.
3D structure databases
SMR	Q72GC9. Positions 15-175.
ModBase	Search...
Protein-protein interaction databases
STRING	Q72GC9.
Genome annotation databases
GeneID	2775039.
GenomeReviews	Gene locus TT_C1919 in contig AE017221_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q72GC9.
OMA	LINWART.
Enzyme and pathway databases
BioCyc	TTHE262724:TT_C1919-MON.
Family and domain databases
HAMAP	MF_01356. [Tree]
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UbQ_OxRdtase_20kDa_su. IPR014406. NiFe_hyd_3_ssu/Q_oxred_NuoB. [Graphical view]
PANTHER	PTHR11995:SF2. NADH_DH_20kDa. 1 hit. PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit.
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
TIGRFAMs	TIGR01957. nuoB_fam. 1 hit.
PROSITE	PS01150. COMPLEX1_20K. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NQO6_THET2

Accession

Primary (citable) accession number: Q72GC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 34 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)