Reviewed, UniProtKB/Swiss-Prot Q56222 (NQO1_THET8)

Names and origin

Protein names

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

Gene names

Name:	nqo1
Ordered Locus Names:	TTHA0089

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	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 nqo1 subunit contains the NADH-binding site and the primary electron acceptor FMN.
Catalytic activity	NADH + quinone = NAD+ + quinol.
Cofactor	Binds 1 FMN per subunit. Binds 1 4Fe-4S cluster per subunit. This 4Fe-4S cluster is referred to as N3.
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. Ref.3 Ref.4
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Domain	The subunit can be separated roughly into four domains: an N-terminal domain (residues 7 to 72) ending with a glycine-rich loop, followed by a Rossman-fold domain (73 to 240), a ubiquitin-like domain (241 to 335) and a C-terminal four-helical bundle containing cluster N3 (336 to 438).
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding 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-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 438

438

NADH-quinone oxidoreductase subunit 1

PRO_0000118567

Regions

Nucleotide binding

66 – 69

4

NAD Probable

Nucleotide binding

92 – 96

5

FMN

Nucleotide binding

180 – 185

6

NAD Probable

Nucleotide binding

218 – 220

3

FMN

Sites

Metal binding

353

1

Iron-sulfur (4Fe-4S)

Metal binding

356

1

Iron-sulfur (4Fe-4S)

Metal binding

359

1

Iron-sulfur (4Fe-4S)

Metal binding

400

1

Iron-sulfur (4Fe-4S)

Binding site

75

1

FMN

Binding site

97

1

NAD Probable

Secondary structure

1

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438

Helix Strand Turn

Details...

Helix

29 – 33

5

Turn

34 – 38

5

Helix

39 – 47

9

Helix

50 – 58

9

Turn

59 – 61

3

Helix

72 – 77

6

Beta strand

81 – 83

3

Beta strand

88 – 93

6

Helix

103 – 109

7

Helix

111 – 124

14

Beta strand

128 – 134

7

Helix

139 – 154

16

Beta strand

157 – 161

5

Beta strand

169 – 175

7

Helix

180 – 183

4

Helix

185 – 192

8

Beta strand

202 – 204

3

Turn

206 – 208

3

Helix

211 – 213

3

Beta strand

216 – 220

5

Helix

221 – 232

12

Helix

235 – 239

5

Beta strand

240 – 242

3

Beta strand

247 – 260

14

Beta strand

262 – 267

6

Helix

272 – 276

5

Turn

277 – 280

4

Beta strand

283 – 285

3

Beta strand

287 – 291

5

Helix

304 – 307

4

Turn

313 – 320

8

Beta strand

327 – 332

6

Helix

337 – 351

15

Helix

357 – 361

5

Helix

362 – 366

5

Helix

367 – 374

8

Helix

381 – 395

15

Helix

402 – 426

25

Sequences

	Sequence		Length	Mass (Da)
	Q56222-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 73ADB3AF31BBE4C0	FASTA	438	48,632
	10 20 30 40 50 60 MTGPILSGLD PRFERTLYAH VGKEGSWTLD YYLRHGGYET AKRVLKEKTP DEVIEEVKRS 70 80 90 100 110 120 GLRGRGGAGF PTGLKWSFMP KDDGKQHYLI CNADESEPGS FKDRYILEDV PHLLIEGMIL 130 140 150 160 170 180 AGYAIRATVG YIYVRGEYRR AADRLEQAIK EARARGYLGK NLFGTDFSFD LHVHRGAGAY 190 200 210 220 230 240 ICGEETALMN SLEGLRANPR LKPPFPAQSG LWGKPTTINN VETLASVVPI MERGADWFAQ 250 260 270 280 290 300 MGTEQSKGMK LYQISGPVKR PGVYELPMGT TFRELIYEWA GGPLEPIQAI IPGGSSTPPL 310 320 330 340 350 360 PFTEEVLDTP MSYEHLQAKG SMLGTGGVIL IPERVSMVDA MWNLTRFYAH ESCGKCTPCR 370 380 390 400 410 420 EGVAGFMVNL FAKIGTGQGE EKDVENLEAL LPLIEGRSFC PLADAAVWPV KGSLRHFKDQ 430 YLALAREKRP VPRPSLWR

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: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, EPR SPECTROSCOPY, 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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U52917 Genomic DNA. Translation: AAA97943.1.
AP008226 Genomic DNA. Translation: BAD69912.1.

PIR

T11903.

RefSeq

YP_143355.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FUG	X-ray	3.30	1/A/J/S	1-438	[»]

ModBase

Search...

Protein family/group databases

TCDB

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

Genome annotation databases

GeneID

3168453.

GenomeReviews

Gene locus TTHA0089 in contig AP008226_GR.

KEGG

ttj:TTHA0089.

NMPDR

fig|300852.3.peg.120.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q56222.

OMA

Q56222. DRYILED.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0089-MON.

Family and domain databases

InterPro

IPR001949. NADH-UbQ_OxRdtase_51KDa_CS.
IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
IPR011537. NADH-UbQ_OxRdtase_suF.
IPR011538. NADH_UbQ_OxRdtase_51KDa_su.
IPR019554. Soluble_ligand_bd.
[Graphical view]

Pfam

PF01512. Complex1_51K. 1 hit.
PF10589. NADH_4Fe-4S. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01959. nuoF_fam. 1 hit.

PROSITE

PS00644. COMPLEX1_51K_1. 1 hit.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

NQO1_THET8

Accession

Primary (citable) accession number: Q56222
Secondary accession number(s): Q5SM54

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 64 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)