DB code: S00320
RLCP classification | 9.1050.440000.8010 : Hydride transfer | |
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9.5010.536200.8010 : Hydride transfer | ||
CATH domain | 3.40.50.720 : Rossmann fold | Catalytic domain |
E.C. | 1.1.1.304 | |
CSA | ||
M-CSA | ||
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.40.50.720 : Rossmann fold | S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
---|---|---|---|
Q48436 |
Acetoin(diacetyl) reductase
|
AR
EC 1.1.1.5 Acetoin dehydrogenase Meso-2,3-butanediol dehydrogenase |
PF00106
(adh_short)
[Graphical View] |
KEGG enzyme name |
---|
(S)-acetoin dehydrogenase
diacetyl reductase [(S)-acetoin forming] |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
Q48436 | BUDC_KLEPN | (S)-acetoin + NAD(+) = diacetyl + NADH. | Homotetramer. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00650 | Butanoate metabolism |
Compound table | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||||
KEGG-id | C00003 | C01769 | C00004 | C00741 | C00080 | ||||||
E.C. | |||||||||||
Compound | NAD+ | (S)-Acetoin | NADH | Diacetyl | H+ | ||||||
Type | amide group,amine group,nucleotide | carbohydrate | amide group,amine group,nucleotide | carbohydrate | others | ||||||
ChEBI |
15846 15846 |
15687 15688 15687 15688 |
16908 16908 |
16583 16583 |
15378 15378 |
||||||
PubChem |
5893 5893 |
179 447765 179 447765 |
439153 439153 |
650 650 |
1038 1038 |
||||||
1gegA | Bound:NAD | Analogue:BME | Unbound | Unbound | |||||||
1gegB | Bound:NAD | Analogue:BME | Unbound | Unbound | |||||||
1gegC | Bound:NAD | Analogue:BME | Unbound | Unbound | |||||||
1gegD | Bound:NAD | Analogue:BME | Unbound | Unbound | |||||||
1gegE | Bound:NAD | Analogue:BME | Unbound | Unbound | |||||||
1gegF | Bound:NAD | Analogue:BME | Unbound | Unbound | |||||||
1gegG | Bound:NAD | Analogue:BME | Unbound | Unbound | |||||||
1gegH | Bound:NAD | Analogue:BME | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;Q48436 & literature [3] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1gegA | SER 139;TYR 152;LYS 156 | |||||||||
1gegB | SER 139;TYR 152;LYS 156 | |||||||||
1gegC | SER 139;TYR 152;LYS 156 | |||||||||
1gegD | SER 139;TYR 152;LYS 156 | |||||||||
1gegE | SER 139;TYR 152;LYS 156 | |||||||||
1gegF | SER 139;TYR 152;LYS 156 | |||||||||
1gegG | SER 139;TYR 152;LYS 156 | |||||||||
1gegH | SER 139;TYR 152;LYS 156 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[3]
|
p.207-208 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2180695 |
Journal | Eur J Biochem |
Year | 1990 |
Volume | 188 |
Pages | 165-74 |
Authors | Heidlas J, Tressl R |
Title | Purification and properties of two oxidoreductases catalyzing the enantioselective reduction of diacetyl and other diketones from baker's yeast. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9045805 |
Journal | J Bacteriol |
Year | 1997 |
Volume | 179 |
Pages | 1497-504 |
Authors | Peng HL, Yang YH, Deng WL, Chang HY |
Title |
Identification and characterization of acoK, |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). |
Medline ID | |
PubMed ID | 11173520 |
Journal | J Biochem (Tokyo) |
Year | 2001 |
Volume | 129 |
Pages | 205-8 |
Authors | Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M |
Title | Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms. |
Related PDB | 1geg |
Related UniProtKB | Q48436 |
Comments |
---|
The catalytic mechanism of this enzyme must be similar to those of the homologous enzymes with the catalytic triad, |
Created | Updated |
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2004-05-12 | 2011-06-22 |