EzCatDB: S00386
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DB codeS00386
CATH domainDomain 13.40.109.10 : NADH OxidaseCatalytic domain
E.C.1.6.99.3

CATH domainRelated DB codes (homologues)
3.40.109.10 : NADH OxidaseS00385,S00387,S00388

Enzyme Name
UniProtKBKEGG

Q60049
Protein nameNADH dehydrogenase (EC 1.6.99.3) (HNADH 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
Synonyms2)O(2)-forming NADH oxidase
NADH:oxygen oxidoreductase
RefSeqYP_143691.1 (Protein)
NC_006461.1 (DNA/RNA sequence)
PfamPF00881 (Nitroreductase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00190Oxidative phosphorylation

UniProtKB:Accession NumberQ60049
Entry nameNOX_THET8
ActivityNADH + acceptor = NAD(+) + reduced acceptor.
SubunitHomodimer.
Subcellular location
CofactorBinds 1 FMN per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00061C00004C00080C00028C00003C00030
CompoundFMNNADHH+AcceptorNAD+Reduced acceptor
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideothersothersamide group,amine group,nucleotideothers
ChEBI17621
16908
15378

15846

PubChem643976
439153
1038

5893

              
1noxABound:FMNUnbound UnboundUnboundUnbound

Active-site residues
pdb
        
1noxA

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.1111-1112
[5]p.4895-4896

references
[1]
PubMed ID8478921
JournalJ Mol Biol
Year1993
Volume230
Pages1086-8
AuthorsErdmann H, Hecht HJ, Park HJ, Sprinzl M, Schomburg D, Schmid RD
TitleCrystallization and preliminary X-ray diffraction studies of a NADH oxidase from Thermus thermophilus HB8.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS)
Medline ID96110872
PubMed ID8846223
JournalNat Struct Biol
Year1995
Volume2
Pages1109-14
AuthorsHecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD
TitleCrystal structure of NADH oxidase from Thermus thermophilus.
Related PDB1nox
Related UniProtKBQ60049
[3]
PubMed ID11488599
JournalArch Biochem Biophys
Year2001
Volume392
Pages251-6
AuthorsMorre DJ, Sedlak D, Tang X, Chueh PJ, Geng T, Morre DM
TitleSurface NADH oxidase of HeLa cells lacks intrinsic membrane binding motifs.
[4]
PubMed ID11917145
JournalProtein Eng
Year2002
Volume15
Pages91-100
AuthorsBhattacharyya R, Samanta U, Chakrabarti P
TitleAromatic-aromatic interactions in and around alpha-helices.
[5]
PubMed ID14653815
JournalEur J Biochem
Year2003
Volume270
Pages4887-97
AuthorsZoldak G, Sut'ak R, Antalik M, Sprinzl M, Sedlak E
TitleRole of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus.
[6]
PubMed ID14686918
JournalEur J Biochem
Year2004
Volume271
Pages48-57
AuthorsZoldak G, Sprinzl M, Sedlak E
TitleModulation of activity of NADH oxidase from Thermus thermophilus through change in flexibility in the enzyme active site induced by Hofmeister series anions.

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).

createdupdated
2004-07-122009-02-26


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