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UniProtKB/Swiss-Prot entry Q48436

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BUDC_KLEPN
Primary accession number Q48436
Secondary accession number Q9R878
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on April 11, 2003 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 50)
Name and origin of the protein
Protein name Acetoin(diacetyl) reductase
Synonyms AR
EC 1.1.1.5
Acetoin dehydrogenase
Meso-2,3-butanediol dehydrogenase
Gene name
Name: budC
From
Klebsiella pneumoniae [TaxID: 573] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Klebsiella.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=IAM 1063;
Ui S.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CG21;
DOI=10.1038/sj/jim/7000179; PubMed=11687934 [NCBI, ExPASy, EBI, Israel, Japan]
Wardwell S.A., Yang Y.T., Chang H.-Y., San K.Y., Rudolph F.B., Bennett G.N.;
"Expression of the Klebsiella pneumoniae CG21 acetoin reductase gene in Clostridium acetobutylicum ATCC 824.";
J. Ind. Microbiol. Biotechnol. 27:220-227(2001).
[3]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.
PubMed=11173520 [NCBI, ExPASy, EBI, Israel, Japan]
Otagiri M., Kurisu G., Ui S., Takusagawa Y., Ohkuma M., Kudo T., Kusunoki M.;
"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.";
J. Biochem. 129:205-208(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D86412; BAA13085.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF098800; AAC78679.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1GEG; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-256.[ExPASy / RCSB / EBI]
PDBsum 1GEG; -.
ModBase Q48436.
Enzyme and pathway databases
BioCyc MetaCyc:MON-8762; -.
Family and domain databases
InterPro IPR014007; 23BDH.
IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
TIGRFAMs TIGR02415; 23BDH; 1.
PROSITE PS00061; ADH_SHORT; 1.
BLOCKS Q48436.
Other
ProtoNet Q48436.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   256  256     Acetoin(diacetyl) reductase. PRO_0000054537
NP_BIND   6    33  28     NAD. 
ACT_SITE   152   152        Proton acceptor. 
BINDING   59    59        NAD. 
BINDING   139   139        Substrate. 
BINDING   156   156        NAD. 
CONFLICT   52    54        RAM -> HAV (in Ref. 1; BAA13085). 
STRAND   4     8  5      
TURN   9    11  3      
HELIX   13    24  12      
STRAND   28    34  7      
HELIX   36    48  13      
STRAND   53    57  5      
HELIX   63    76  14      
STRAND   82    85  4      
HELIX   95    97  3      
HELIX   100   110  11      
HELIX   112   128  17      
STRAND   132   137  6      
HELIX   140   142  3      
HELIX   150   170  21      
HELIX   171   173  3      
STRAND   175   182  8      
STRAND   184   187  4      
HELIX   188   201  14      
HELIX   207   213  7      
HELIX   224   235  12      
HELIX   237   239  3      
STRAND   246   254  9      
Sequence information
Length: 256 AA [This is the length of the unprocessed precursor] Molecular weight: 26642 Da [This is the MW of the unprocessed precursor] CRC64: B250F184C665ACAF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKVALVTGA GQGIGKAIAL RLVKDGFAVA IADYNDATAK AVASEINQAG GRAMAVKVDV 

        70         80         90        100        110        120 
SDRDQVFAAV EQARKTLGGF DVIVNNAGVA PSTPIESITP EIVDKVYNIN VKGVIWGIQA 

       130        140        150        160        170        180 
AVEAFKKEGH GGKIINACSQ AGHVGNPELA VYSSSKFAVR GLTQTAARDL APLGITVNGY 

       190        200        210        220        230        240 
CPGIVKTPMW AEIDRQVSEA AGKPLGYGTA EFAKRITLGR LSEPEDVAAC VSYLASPDSD 

       250 
YMTGQSLLID GGMVFN
Q48436 in FASTA format

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