DB code: S00386

CATH domain 3.40.109.10 : NADH Oxidase Catalytic domain
E.C. 1.6.99.3
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.109.10 : NADH Oxidase S00385 S00387 S00388

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q60049 NADH dehydrogenase (EC 1.6.99.3) (H
2)O(2)-forming NADH oxidase
NADH:oxygen oxidoreductase
YP_143691.1 (Protein)
NC_006461.1 (DNA/RNA sequence)
PF00881 (Nitroreductase)
[Graphical View]

KEGG enzyme name
NADH dehydrogenase
cytochrome c reductase
type 1 dehydrogenase
beta-NADH dehydrogenase dinucleotide
diaphorase
dihydrocodehydrogenase I dehydrogenase
dihydronicotinamide adenine dinucleotide dehydrogenase
diphosphopyridine diaphorase
DPNH diaphorase
NADH diaphorase
NADH hydrogenase
NADH oxidoreductase
NADH-menadione oxidoreductase
reduced diphosphopyridine nucleotide diaphorase
NADH:cytochrome c oxidoreductase
NADH2 dehydrogenase
NADH:(acceptor) oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q60049 NOX_THET8 NADH + acceptor = NAD(+) + reduced acceptor. Homodimer. Binds 1 FMN per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00190 Oxidative phosphorylation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00061 C00004 C00080 C00028 C00003 C00030
E.C.
Compound FMN NADH H+ Acceptor NAD+ Reduced acceptor
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide others others amide group,amine group,nucleotide others
ChEBI 17621
16908
15378
15846
PubChem 643976
439153
1038
5893
1noxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FMN Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1noxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.1111-1112
[5]
p.4895-4896

References
[1]
Resource
Comments
Medline ID
PubMed ID 8478921
Journal J Mol Biol
Year 1993
Volume 230
Pages 1086-8
Authors Erdmann H, Hecht HJ, Park HJ, Sprinzl M, Schomburg D, Schmid RD
Title Crystallization and preliminary X-ray diffraction studies of a NADH oxidase from Thermus thermophilus HB8.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS)
Medline ID 96110872
PubMed ID 8846223
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 1109-14
Authors Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD
Title Crystal structure of NADH oxidase from Thermus thermophilus.
Related PDB 1nox
Related UniProtKB Q60049
[3]
Resource
Comments
Medline ID
PubMed ID 11488599
Journal Arch Biochem Biophys
Year 2001
Volume 392
Pages 251-6
Authors Morre DJ, Sedlak D, Tang X, Chueh PJ, Geng T, Morre DM
Title Surface NADH oxidase of HeLa cells lacks intrinsic membrane binding motifs.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11917145
Journal Protein Eng
Year 2002
Volume 15
Pages 91-100
Authors Bhattacharyya R, Samanta U, Chakrabarti P
Title Aromatic-aromatic interactions in and around alpha-helices.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 14653815
Journal Eur J Biochem
Year 2003
Volume 270
Pages 4887-97
Authors Zoldak G, Sut'ak R, Antalik M, Sprinzl M, Sedlak E
Title Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 14686918
Journal Eur J Biochem
Year 2004
Volume 271
Pages 48-57
Authors Zoldak G, Sprinzl M, Sedlak E
Title Modulation of activity of NADH oxidase from Thermus thermophilus through change in flexibility in the enzyme active site induced by Hofmeister series anions.
Related PDB
Related UniProtKB

Comments
There are some NADH dehydrogenases, E.C. 1.6.99.3 (this file = NADH2 oxidase), E.C. 1.6.99.2 (NAD(P)H dehydrogenase, quinone-dependent), E.C. 1.6.99.5 (NADH dehydrogenase, quinone-dependent), E.C. 1.6.5.3 (NADH dehydrogenase, ubiquinone-dependent), 1.6.2.4 (NADP-cytochrome reductase).

Created Updated
2004-07-12 2009-02-26