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Q60049

- NOX_THET8

UniProt

Q60049 - NOX_THET8

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Protein

NADH dehydrogenase

Gene

nox

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

NADH + acceptor = NAD+ + reduced acceptor.

Cofactori

Binds 1 FMN per subunit.

pH dependencei

Optimum pH is 5.0.

Temperature dependencei

Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731FMN1 Publication
Binding sitei195 – 1951FMN1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 215FMN1 Publication
Nucleotide bindingi158 – 1592FMN1 Publication

GO - Molecular functioni

  1. NADH dehydrogenase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NAD

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-446-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase (EC:1.6.99.3)
Alternative name(s):
H(2)O(2)-forming NADH oxidase
NADH:oxygen oxidoreductase
Gene namesi
Name:nox
Ordered Locus Names:TTHA0425
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205NADH dehydrogenasePRO_0000072721Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0425.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 167
Helixi30 – 4011
Helixi46 – 483
Beta strandi52 – 576
Helixi60 – 6910
Turni70 – 723
Helixi75 – 784
Beta strandi79 – 879
Helixi89 – 946
Helixi95 – 984
Helixi107 – 12115
Helixi125 – 14925
Beta strandi153 – 1575
Helixi162 – 1698
Beta strandi176 – 18813
Helixi198 – 2014

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NOXX-ray1.59A1-205[»]
ProteinModelPortaliQ60049.
SMRiQ60049. Positions 6-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60049.

Family & Domainsi

Sequence similaritiesi

Belongs to the nitroreductase family.Curated

Phylogenomic databases

eggNOGiCOG0778.
HOGENOMiHOG000146732.
OMAiANYPRSM.
OrthoDBiEOG6N947Z.
PhylomeDBiQ60049.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequencei

Sequence statusi: Complete.

Q60049 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEATLPVLDA KTAALKRRSI RRYRKDPVPE GLLREILEAA LRAPSAWNLQ
60 70 80 90 100
PWRIVVVRDP ATKRALREAA FGQAHVEEAP VVLVLYADLE DALAHLDEVI
110 120 130 140 150
HPGVQGERRE AQKQAIQRAF AAMGQEARKA WASGQSYILL GYLLLLLEAY
160 170 180 190 200
GLGSVPMLGF DPERVRAILG LPSHAAIPAL VALGYPAEEG YPSHRLPLER

VVLWR
Length:205
Mass (Da):22,730
Last modified:March 29, 2005 - v2
Checksum:i012742DFA85B50E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741H → R in CAA42707. (PubMed:1577004)Curated
Sequence conflicti174 – 1741H → R in AAB25458. (PubMed:1577004)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60110 Genomic DNA. Translation: CAA42707.1.
S55441 Genomic DNA. Translation: AAB25458.1.
AP008226 Genomic DNA. Translation: BAD70248.1.
RefSeqiWP_011227925.1. NC_006461.1.
YP_143691.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70248; BAD70248; BAD70248.
GeneIDi3168975.
KEGGittj:TTHA0425.
PATRICi23955821. VBITheThe93045_0425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60110 Genomic DNA. Translation: CAA42707.1 .
S55441 Genomic DNA. Translation: AAB25458.1 .
AP008226 Genomic DNA. Translation: BAD70248.1 .
RefSeqi WP_011227925.1. NC_006461.1.
YP_143691.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NOX X-ray 1.59 A 1-205 [» ]
ProteinModelPortali Q60049.
SMRi Q60049. Positions 6-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA0425.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70248 ; BAD70248 ; BAD70248 .
GeneIDi 3168975.
KEGGi ttj:TTHA0425.
PATRICi 23955821. VBITheThe93045_0425.

Phylogenomic databases

eggNOGi COG0778.
HOGENOMi HOG000146732.
OMAi ANYPRSM.
OrthoDBi EOG6N947Z.
PhylomeDBi Q60049.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-446-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q60049.

Family and domain databases

Gene3Di 3.40.109.10. 1 hit.
InterProi IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view ]
Pfami PF00881. Nitroreductase. 1 hit.
[Graphical view ]
SUPFAMi SSF55469. SSF55469. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiNOX_THET8
AccessioniPrimary (citable) accession number: Q60049
Secondary accession number(s): Q53306, Q5SL68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 29, 2005
Last modified: October 29, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3