Reviewed, UniProtKB/Swiss-Prot Q48436 (BUDC_KLEPN)

Names and origin

Protein names

Recommended name:
    Acetoin(diacetyl) reductase
      Short name=AR
    EC=1.1.1.5
Alternative name(s):
    Acetoin dehydrogenase
    Meso-2,3-butanediol dehydrogenase

Gene names

Name:

budC

Organism

Klebsiella pneumoniae

Taxonomic identifier

573 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible reduction of acetoin to 2,3-butanediol in the presence of NADH.
Catalytic activity	Acetoin + NAD(+) = diacetyl + NADH.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	acetoin catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetoin dehydrogenase activity Inferred from electronic annotation. Source: InterPro binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 256

256

Acetoin(diacetyl) reductase

PRO_0000054537

Regions

Nucleotide binding

6 – 33

28

NAD

Sites

Active site

152

1

Proton acceptor

Binding site

59

1

NAD

Binding site

139

1

Substrate

Binding site

156

1

NAD

Experimental info

Sequence conflict

52 – 54

3

RAM → HAV in BAA13085. Ref.1

Secondary structure

1

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256

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Turn

9 – 11

3

Helix

13 – 24

12

Beta strand

28 – 34

7

Helix

36 – 48

13

Beta strand

53 – 57

5

Helix

63 – 76

14

Beta strand

82 – 85

4

Helix

95 – 97

3

Helix

100 – 110

11

Helix

112 – 128

17

Beta strand

132 – 137

6

Helix

140 – 142

3

Helix

150 – 170

21

Helix

171 – 173

3

Beta strand

175 – 182

8

Beta strand

184 – 187

4

Helix

188 – 201

14

Helix

207 – 213

7

Helix

224 – 235

12

Helix

237 – 239

3

Beta strand

246 – 254

9

Sequences

	Sequence		Length	Mass (Da)
	Q48436-1 [UniParc]. Last modified April 11, 2003. Version 2. Checksum: B250F184C665ACAF	FASTA	256	26,642
	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

References

[1]	Ui S. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IAM 1063.
[2]	"Expression of the Klebsiella pneumoniae CG21 acetoin reductase gene in Clostridium acetobutylicum ATCC 824." Wardwell S.A., Yang Y.T., Chang H.-Y., San K.Y., Rudolph F.B., Bennett G.N. J. Ind. Microbiol. Biotechnol. 27:220-227(2001) [PubMed: 11687934] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CG21.
[3]	"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." Otagiri M., Kurisu G., Ui S., Takusagawa Y., Ohkuma M., Kudo T., Kusunoki M. J. Biochem. 129:205-208(2001) [PubMed: 11173520] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D86412 Genomic DNA. Translation: BAA13085.1.
AF098800 Genomic DNA. Translation: AAC78679.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GEG	X-ray	1.70	A/B/C/D/E/F/G/H	1-256	[»]

ModBase

Search...

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]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

TIGRFAMs

TIGR02415. 23BDH. 1 hit.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BUDC_KLEPN

Accession

Primary (citable) accession number: Q48436
Secondary accession number(s): Q9R878

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	April 11, 2003
Last modified:	November 25, 2008
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)