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 17621 |
16908 16908 |
15378 15378 |
15846 15846 |
||||||||
| PubChem |
643976 643976 |
439153 439153 |
1038 1038 |
5893 5893 |
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| 1noxA |
|
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|
|
|
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 |
|
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|
|
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| 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, |
| Created | Updated |
|---|---|
| 2004-07-12 | 2009-02-26 |