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Protein

Diacetyl reductase [(S)-acetoin forming]

Gene

budC

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible reduction of (S)-acetoin to 2,3-butanediol in the presence of NADH.

Catalytic activityi

(S)-acetoin + NAD+ = diacetyl + NADH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei59NAD1 Publication1
Binding sitei139Substrate1
Active sitei152Proton acceptor1
Binding sitei156NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi6 – 33NAD1 PublicationAdd BLAST28

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandNAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8762
BRENDAi1.1.1.304 2814

Names & Taxonomyi

Protein namesi
Recommended name:
Diacetyl reductase [(S)-acetoin forming] (EC:1.1.1.304)
Alternative name(s):
Acetoin(diacetyl) reductase
Short name:
AR
Meso-2,3-butanediol dehydrogenase
Gene namesi
Name:budC
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

Pathology & Biotechi

Chemistry databases

DrugBankiDB02379 Beta-D-Glucose

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000545371 – 256Diacetyl reductase [(S)-acetoin forming]Add BLAST256

Proteomic databases

PRIDEiQ48436

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Turni9 – 11Combined sources3
Helixi13 – 25Combined sources13
Beta strandi28 – 34Combined sources7
Helixi36 – 47Combined sources12
Turni48 – 50Combined sources3
Beta strandi55 – 57Combined sources3
Helixi63 – 77Combined sources15
Beta strandi82 – 85Combined sources4
Helixi95 – 97Combined sources3
Helixi100 – 110Combined sources11
Helixi122 – 128Combined sources7
Beta strandi132 – 137Combined sources6
Helixi140 – 142Combined sources3
Helixi165 – 170Combined sources6
Helixi171 – 173Combined sources3
Beta strandi175 – 182Combined sources8
Beta strandi184 – 187Combined sources4
Helixi188 – 201Combined sources14
Helixi207 – 213Combined sources7
Helixi224 – 235Combined sources12
Helixi237 – 239Combined sources3
Beta strandi246 – 254Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GEGX-ray1.70A/B/C/D/E/F/G/H1-256[»]
3WYEX-ray1.58A/B1-83[»]
A/B119-134[»]
A/B162-181[»]
A/B237-256[»]
ProteinModelPortaliQ48436
SMRiQ48436
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ48436

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CHR Bacteria
ENOG410XNW1 LUCA

Family and domain databases

InterProiView protein in InterPro
IPR014007 23BDH
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR02415 23BDH, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Complete.

Q48436-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVALVTGA GQGIGKAIAL RLVKDGFAVA IADYNDATAK AVASEINQAG
60 70 80 90 100
GRAMAVKVDV SDRDQVFAAV EQARKTLGGF DVIVNNAGVA PSTPIESITP
110 120 130 140 150
EIVDKVYNIN VKGVIWGIQA AVEAFKKEGH GGKIINACSQ AGHVGNPELA
160 170 180 190 200
VYSSSKFAVR GLTQTAARDL APLGITVNGY CPGIVKTPMW AEIDRQVSEA
210 220 230 240 250
AGKPLGYGTA EFAKRITLGR LSEPEDVAAC VSYLASPDSD YMTGQSLLID

GGMVFN
Length:256
Mass (Da):26,642
Last modified:April 11, 2003 - v2
Checksum:iB250F184C665ACAF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52 – 54RAM → HAV in BAA13085 (Ref. 1) Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86412 Genomic DNA Translation: BAA13085.1
AF098800 Genomic DNA Translation: AAC78679.1
RefSeqiWP_004151179.1, NZ_PTMB01000007.1

Entry informationi

Entry nameiBUDC_KLEPN
AccessioniPrimary (citable) accession number: Q48436
Secondary accession number(s): Q9R878
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 11, 2003
Last modified: May 23, 2018
This is version 104 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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