Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q60049 (NOX_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence 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
   LigandFlavoprotein
FMN
NAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Molecular_functionNADH dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205NADH dehydrogenase
PRO_0000072721

Regions

Nucleotide binding17 – 215FMN
Nucleotide binding158 – 1592FMN

Sites

Binding site731FMN
Binding site1951FMN

Experimental info

Sequence conflict1741H → R in CAA42707. Ref.1
Sequence conflict1741H → R in AAB25458. Ref.1

Secondary structure

.............................. 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60049 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 012742DFA85B50E5

FASTA20522,730
        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 

« Hide

References

« Hide '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.
RefSeqYP_143691.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NOXX-ray1.59A1-205[»]
ProteinModelPortalQ60049.
SMRQ60049. Positions 6-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA0425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70248; BAD70248; BAD70248.
GeneID3168975.
KEGGttj:TTHA0425.
PATRIC23955821. VBITheThe93045_0425.

Phylogenomic databases

eggNOGCOG0778.
HOGENOMHOG000146732.
OMAANYPRSM.
OrthoDBEOG6N947Z.
PhylomeDBQ60049.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-446-MONOMER.

Family and domain databases

Gene3D3.40.109.10. 1 hit.
InterProIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMSSF55469. SSF55469. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ60049.

Entry information

Entry nameNOX_THET8
AccessionPrimary (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: July 9, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references