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Protein

Diacetyl reductase [(S)-acetoin forming]

Gene

budC

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei59 – 591NAD1 Publication
Binding sitei139 – 1391Substrate
Active sitei152 – 1521Proton acceptor
Binding sitei156 – 1561NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 3328NAD1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8762.
RETL1328306-WGS:GSTH-6818-MONOMER.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Diacetyl reductase [(S)-acetoin forming]PRO_0000054537Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi272620.KPN_02061.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Turni9 – 113Combined sources
Helixi13 – 2513Combined sources
Beta strandi28 – 347Combined sources
Helixi36 – 4712Combined sources
Turni48 – 503Combined sources
Beta strandi53 – 575Combined sources
Helixi63 – 7715Combined sources
Beta strandi82 – 854Combined sources
Helixi95 – 973Combined sources
Helixi100 – 11011Combined sources
Helixi119 – 12810Combined sources
Beta strandi132 – 1343Combined sources
Helixi140 – 1423Combined sources
Helixi162 – 1709Combined sources
Helixi171 – 1733Combined sources
Beta strandi175 – 1817Combined sources
Beta strandi184 – 1874Combined sources
Helixi188 – 20114Combined sources
Helixi207 – 2137Combined sources
Helixi224 – 23512Combined sources
Helixi237 – 2393Combined sources
Beta strandi246 – 2549Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ48436.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CHR. Bacteria.
ENOG410XNW1. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014007. 23BDH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02415. 23BDH. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 543RAM → HAV in BAA13085 (Ref. 1) Curated

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_LWLM01000001.1.

Cross-referencesi

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_LWLM01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272620.KPN_02061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CHR. Bacteria.
ENOG410XNW1. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8762.
RETL1328306-WGS:GSTH-6818-MONOMER.
BRENDAi1.1.1.304. 2814.

Miscellaneous databases

EvolutionaryTraceiQ48436.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014007. 23BDH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02415. 23BDH. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBUDC_KLEPN
AccessioniPrimary (citable) accession number: Q48436
Secondary accession number(s): Q9R878
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 11, 2003
Last modified: July 6, 2016
This is version 91 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.