Q60049 (NOX_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH dehydrogenase
EC=1.6.99.3

Alternative name(s):
H(2)O(2)-forming NADH oxidase
NADH:oxygen oxidoreductase

Gene names

Name:	nox
Ordered Locus Names:	TTHA0425

Organism

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

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Can oxidize either NADH or NADPH with a preference for NADH. Can catalyze electron transfer from NADH to various electron acceptors which include, in addition to molecular oxygen, cytochrome c, 2,6 dichlorphenolindophenol, methylene blue, ferricyanide or P-nitroblue tetrazolium.
Catalytic activity	NADH + acceptor = NAD+ + reduced acceptor.
Cofactor	Binds 1 FMN per subunit.
Subunit structure	Homodimer. Ref.5
Sequence similarities	Belongs to the nitroreductase family.
Biophysicochemical properties	pH dependence: Optimum pH is 5.0. Temperature dependence: Thermostable.

Ontologies

Keywords
Ligand	FMN Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular_function	NADH dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 205

205

NADH dehydrogenase

PRO_0000072721

Regions

Nucleotide binding

17 – 21

5

FMN

Nucleotide binding

158 – 159

2

FMN

Sites

Binding site

73

1

FMN

Binding site

195

1

FMN

Experimental info

Sequence conflict

174

1

H → R in CAA42707. Ref.1

Sequence conflict

174

1

H → R in AAB25458. Ref.1

Secondary structure

1

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205

Helix Strand Turn

Details...

Helix

10 – 16

7

Helix

30 – 40

11

Helix

46 – 48

3

Beta strand

52 – 57

6

Helix

60 – 69

10

Turn

70 – 72

3

Helix

75 – 78

4

Beta strand

79 – 87

9

Helix

89 – 94

6

Helix

95 – 98

4

Helix

107 – 121

15

Helix

125 – 149

25

Beta strand

153 – 157

5

Helix

162 – 169

8

Beta strand

176 – 188

13

Helix

198 – 201

4

Sequences

	Sequence		Length	Mass (Da)
	Q60049 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 012742DFA85B50E5	FASTA	205	22,730
	10 20 30 40 50 60 MEATLPVLDA KTAALKRRSI RRYRKDPVPE GLLREILEAA LRAPSAWNLQ PWRIVVVRDP 70 80 90 100 110 120 ATKRALREAA FGQAHVEEAP VVLVLYADLE DALAHLDEVI HPGVQGERRE AQKQAIQRAF 130 140 150 160 170 180 AAMGQEARKA WASGQSYILL GYLLLLLEAY GLGSVPMLGF DPERVRAILG LPSHAAIPAL 190 200 VALGYPAEEG YPSHRLPLER VVLWR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of the gene encoding a H2O2-forming NADH oxidase from the extreme thermophilic Thermus thermophilus HB8 and its expression in Escherichia coli." Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M. Eur. J. Biochem. 205:875-879(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Erratum Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M. Eur. J. Biochem. 211:909-909(1993) [PubMed] [Europe PMC] [Abstract]
[3]	"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.
[4]	"Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8." Park H.-J., Reiser C.O.A., Kondruweit S., Erdmann H., Schmid R.D., Sprinzl M. Eur. J. Biochem. 205:881-885(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32, CHARACTERIZATION.
[5]	"Crystal structure of NADH oxidase from Thermus thermophilus." Hecht H.J., Erdmann H., Park H.J., Sprinzl M., Schmid R.D. Nat. Struct. Biol. 2:1109-1114(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) IN COMPLEX WITH FMN, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X60110 Genomic DNA. Translation: CAA42707.1.
S55441 Genomic DNA. Translation: AAB25458.1.
AP008226 Genomic DNA. Translation: BAD70248.1.

RefSeq

YP_143691.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NOX	X-ray	1.59	A	1-205	[»]

ProteinModelPortal

Q60049.

SMR

Q60049. Positions 6-205.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA0425.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD70248; BAD70248; BAD70248.

GeneID

3168975.

KEGG

ttj:TTHA0425.

PATRIC

23955821. VBITheThe93045_0425.

Phylogenomic databases

eggNOG

COG0778.

HOGENOM

HOG000146732.

OMA

DENAYDL.

ProtClustDB

CLSK881064.

Family and domain databases

Gene3D

3.40.109.10. 1 hit.

InterPro

IPR000415. Nitroreductase-like.
[Graphical view]

Pfam

PF00881. Nitroreductase. 1 hit.
[Graphical view]

SUPFAM

SSF55469. Nitroreductase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q60049.

Entry information

Entry name

NOX_THET8

Accession

Primary (citable) accession number: Q60049
Secondary accession number(s): Q53306, Q5SL68

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program