DB code: S00320

RLCP classification 9.5010.536200.8010 : Hydride transfer
9.1050.440000.8010 : 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
15688
15687
16908
16583
15378
PubChem 5893
447765
179
439153
650
1038
1gegA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Analogue:BME Unbound Unbound
1gegB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Analogue:BME Unbound Unbound
1gegC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Analogue:BME Unbound Unbound
1gegD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Analogue:BME Unbound Unbound
1gegE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Analogue:BME Unbound Unbound
1gegF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Analogue:BME Unbound Unbound
1gegG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Analogue:BME Unbound Unbound
1gegH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1gegB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1gegC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1gegD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1gegE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1gegF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1gegG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1gegH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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, a regulatory gene of the Klebsiella pneumoniae acoABCD operon.
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, Ser-Tyr-Lys (S00324, S00326, S00329, S00331, S00336 in EzCatDB).

Created Updated
2004-05-12 2011-06-22