Reviewed, UniProtKB/Swiss-Prot Q5SKZ7 (NQO15_THET8)

Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit 15
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I chain 15
    NDH-1 subunit 15

Gene names

Name:	nqo15
Ordered Locus Names:	TTHA0496

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

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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 nqo15 subunit has probably a role in complex stabilization, and may be also involved in the storage of iron for iron-sulfur cluster regeneration in the complex.
Catalytic activity	NADH + quinone = NAD(+) + quinol.
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. Nqo15 is bound to the side of the complex near the N-terminus of nqo3, where it interacts with subunits nqo3, nqo2, nqo1, nqo9 and nqo4.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Domain	Has a similar fold to the mitochondrial iron chaperone frataxin.
Sequence similarities	Belongs to the complex I nqo15 family.

Ontologies

Keywords
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: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC 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

Initiator methionine

1

1

Removed

Chain

2 – 129

128

NADH-quinone oxidoreductase subunit 15

PRO_0000233014

Secondary structure

1

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129

Helix Strand Turn

Details...

Helix

4 – 27

24

Beta strand

30 – 36

7

Helix

38 – 41

4

Beta strand

53 – 60

8

Beta strand

66 – 72

7

Beta strand

82 – 86

5

Turn

87 – 90

4

Beta strand

91 – 98

8

Turn

99 – 101

3

Beta strand

102 – 109

8

Helix

112 – 126

15

Sequences

	Sequence		Length	Mass (Da)
	Q5SKZ7-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A944E174C0DE152C	FASTA	129	14,788
	10 20 30 40 50 60 MSASSERELY EAWVELLSWM REYAQAKGVR FEKEADFPDF IYRMERPYDL PTTIMTASLS 70 80 90 100 110 120 DGLGEPFLLA DVSPRHAKLK RIGLRLPRAH IHLHAHYEPG KGLVTGKIPL TKERFFALAD RAREALAFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"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 2-9, CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
[3]	"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), FUNCTION, SUBUNIT, ELECTRON TRANSFER MECHANISM.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AP008226 Genomic DNA. Translation: BAD70319.1.

RefSeq

YP_143762.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FUG	X-ray	3.30	7/H/Q/Z	1-129	[»]

ModBase

Search...

Genome annotation databases

GeneID

3169322.

GenomeReviews

Gene locus TTHA0496 in contig AP008226_GR.

KEGG

ttj:TTHA0496.

NMPDR

fig|300852.3.peg.607.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q5SKZ7.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0496-MON.

Family and domain databases

ProtoNet

Search...

Entry information

Entry name

NQO15_THET8

Accession

Primary (citable) accession number: Q5SKZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	January 23, 2007
Last modified:	November 4, 2008
This is version 27 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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