EzCatDB: S00320
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DB codeS00320
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.304

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,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

Enzyme Name
UniProtKBKEGG

Q48436
Protein nameAcetoin(diacetyl) reductase(S)-acetoin dehydrogenase
diacetyl reductase [(S)-acetoin forming]
SynonymsAR
EC 1.1.1.5
Acetoin dehydrogenase
Meso-2,3-butanediol dehydrogenase
PfamPF00106 (adh_short)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00650Butanoate metabolism

UniProtKB:Accession NumberQ48436
Entry nameBUDC_KLEPN
Activity(S)-acetoin + NAD(+) = diacetyl + NADH.
SubunitHomotetramer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00003C01769C00004C00741C00080
CompoundNAD+(S)-AcetoinNADHDiacetylH+
Typeamide group,amine group,nucleotidecarbohydrateamide group,amine group,nucleotidecarbohydrateothers
ChEBI15846
15687
15688
16908
16583
15378
PubChem5893
447765
179
439153
650
1038
             
1gegABound:NADAnalogue:BMEUnboundUnbound 
1gegBBound:NADAnalogue:BMEUnboundUnbound 
1gegCBound:NADAnalogue:BMEUnboundUnbound 
1gegDBound:NADAnalogue:BMEUnboundUnbound 
1gegEBound:NADAnalogue:BMEUnboundUnbound 
1gegFBound:NADAnalogue:BMEUnboundUnbound 
1gegGBound:NADAnalogue:BMEUnboundUnbound 
1gegHBound:NADAnalogue:BMEUnboundUnbound 

Active-site residues
resource
Swiss-prot;Q48436 & literature [3]
pdbCatalytic residues
         
1gegASER 139;TYR 152;LYS 156
1gegBSER 139;TYR 152;LYS 156
1gegCSER 139;TYR 152;LYS 156
1gegDSER 139;TYR 152;LYS 156
1gegESER 139;TYR 152;LYS 156
1gegFSER 139;TYR 152;LYS 156
1gegGSER 139;TYR 152;LYS 156
1gegHSER 139;TYR 152;LYS 156

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.207-208

references
[1]
PubMed ID2180695
JournalEur J Biochem
Year1990
Volume188
Pages165-74
AuthorsHeidlas J, Tressl R
TitlePurification and properties of two oxidoreductases catalyzing the enantioselective reduction of diacetyl and other diketones from baker's yeast.
[2]
PubMed ID9045805
JournalJ Bacteriol
Year1997
Volume179
Pages1497-504
AuthorsPeng HL, Yang YH, Deng WL, Chang HY
TitleIdentification and characterization of acoK, a regulatory gene of the Klebsiella pneumoniae acoABCD operon.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed ID11173520
JournalJ Biochem (Tokyo)
Year2001
Volume129
Pages205-8
AuthorsOtagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M
TitleCrystal 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 PDB1geg
Related UniProtKBQ48436

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).

createdupdated
2004-05-122011-06-22


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