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Protein

L-2,3-butanediol dehydrogenase

Gene

budC

Organism
Corynebacterium glutamicum (Brevibacterium saccharolyticum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol (L-BD) in the presence of NADH. To a lesser extent, can also catalyze the irreversible reduction of diacetyl to (S)-acetoin. Cannot oxidize meso-BD, D-BD, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, and n-propanol. Cannot reduce (R)-acetoin, acetol, dihydroxyacetone and 2,4-pentanedione.2 Publications

Catalytic activityi

(2S,3S)-butane-2,3-diol + NAD+ = (S)-acetoin + NADH.1 Publication
(S)-acetoin + NAD+ = diacetyl + NADH.2 Publications

Enzyme regulationi

Slightly activated by Ba2+, Ca2+, Mn2+, Mg2+, and Co2+, while Hg2+ and Cu2+ cause marked inhibition of the activity. Ni2+, Zn2+ and Cd2+ have no effect on the catalytic activity. Is also slightly inhibited by lactate, pyruvate, succinate, acetate and formate.1 Publication

Kineticsi

  1. KM=0.10 mM for NADH (at pH 6.0)1 Publication
  2. KM=0.44 mM for (S)-acetoin (at pH 6.0)1 Publication
  3. KM=0.07 mM for NAD+ (at pH 10.5)1 Publication
  4. KM=0.22 mM for (S,S)-butane-2,3-diol (at pH 10.5)1 Publication

    pH dependencei

    Optimum pH is 10.5 for the oxidative reaction with L-BD and 6.0 for the reductive reaction with (S)-acetoin. Stable from pH 7.0 to 9.0.1 Publication

    Temperature dependencei

    Stable up to 37 degrees Celsius but is rapidly inactivated over 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei33NAD1 Publication1
    Binding sitei37NAD1 Publication1
    Binding sitei88NAD; via carbonyl oxygen1 Publication1
    Active sitei154Proton acceptorPROSITE-ProRule annotationBy similarity1
    Binding sitei154NAD1 Publication1
    Binding sitei158NAD1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi12 – 14NAD1 Publication3
    Nucleotide bindingi61 – 62NAD1 Publication2
    Nucleotide bindingi184 – 189NAD1 Publication6

    GO - Molecular functioni

    • (S,S)-butanediol dehydrogenase activity Source: UniProtKB
    • diacetyl reductase ((S)-acetoin forming) activity Source: UniProtKB-EC
    • NAD+ binding Source: UniProtKB
    • NADH binding Source: UniProtKB

    GO - Biological processi

    • acetoin catabolic process Source: InterPro
    • acetoin metabolic process Source: UniProtKB
    • butanediol metabolic process Source: UniProtKB
    • protein homotetramerization Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi1.1.1.76. 960.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-2,3-butanediol dehydrogenase (EC:1.1.1.76)
    Short name:
    L-BDH
    Alternative name(s):
    (S,S)-butanediol dehydrogenase
    Diacetyl reductase [(S)-acetoin forming]1 Publication (EC:1.1.1.3041 Publication)
    Gene namesi
    Name:budC1 Publication
    OrganismiCorynebacterium glutamicum (Brevibacterium saccharolyticum)
    Taxonomic identifieri1718 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi142I → Q: Loss of L-BD oxidizing activity, and does not gain the ability to use meso-BD as substrate; when associated with N-148. 1 Publication1
    Mutagenesisi142I → Q: Loss of L-BD oxidizing activity. Does not gain the ability to use meso-BD as substrate. 1 Publication1
    Mutagenesisi148F → N: Loss of L-BD oxidizing activity, and does not gain the ability to use meso-BD as substrate; when associated with Q-142. 1 Publication1
    Mutagenesisi148F → N: Loss of L-BD oxidizing activity. Does not gain the ability to use meso-BD as substrate. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004189721 – 258L-2,3-butanediol dehydrogenaseAdd BLAST258

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    STRINGi196627.cg2958.

    Structurei

    Secondary structure

    1258
    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 – 33Combined sources6
    Helixi35 – 37Combined sources3
    Helixi38 – 49Combined sources12
    Turni50 – 52Combined sources3
    Beta strandi55 – 59Combined sources5
    Helixi65 – 79Combined sources15
    Beta strandi84 – 87Combined sources4
    Helixi97 – 99Combined sources3
    Helixi102 – 112Combined sources11
    Helixi114 – 120Combined sources7
    Beta strandi137 – 139Combined sources3
    Helixi142 – 144Combined sources3
    Helixi152 – 163Combined sources12
    Helixi173 – 175Combined sources3
    Beta strandi178 – 184Combined sources7
    Helixi190 – 203Combined sources14
    Helixi209 – 214Combined sources6
    Turni215 – 217Combined sources3
    Helixi226 – 237Combined sources12
    Helixi239 – 241Combined sources3
    Beta strandi248 – 255Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3A28X-ray2.00A/B/C/D/E/F/G/H1-258[»]
    3WYEX-ray1.58A/B86-120[»]
    A/B137-163[»]
    A/B184-238[»]
    ProteinModelPortaliQ9ZNN8.
    SMRiQ9ZNN8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZNN8.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CHR. Bacteria.
    ENOG410XNW1. LUCA.
    KOiK03366.

    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.
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02415. 23BDH. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ZNN8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKVAMVTGG AQGIGRGISE KLAADGFDIA VADLPQQEEQ AAETIKLIEA
    60 70 80 90 100
    ADQKAVFVGL DVTDKANFDS AIDEAAEKLG GFDVLVNNAG IAQIKPLLEV
    110 120 130 140 150
    TEEDLKQIYS VNVFSVFFGI QAASRKFDEL GVKGKIINAA SIAAIQGFPI
    160 170 180 190 200
    LSAYSTTKFA VRGLTQAAAQ ELAPKGHTVN AYAPGIVGTG MWEQIDAELS
    210 220 230 240 250
    KINGKPIGEN FKEYSSSIAL GRPSVPEDVA GLVSFLASEN SNYVTGQVML

    VDGGMLYN
    Length:258
    Mass (Da):27,108
    Last modified:May 1, 1999 - v1
    Checksum:i96A81BD2AE33E55E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB009078 Genomic DNA. Translation: BAA36159.1.

    Genome annotation databases

    KEGGiag:BAA36159.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB009078 Genomic DNA. Translation: BAA36159.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3A28X-ray2.00A/B/C/D/E/F/G/H1-258[»]
    3WYEX-ray1.58A/B86-120[»]
    A/B137-163[»]
    A/B184-238[»]
    ProteinModelPortaliQ9ZNN8.
    SMRiQ9ZNN8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi196627.cg2958.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAA36159.

    Phylogenomic databases

    eggNOGiENOG4105CHR. Bacteria.
    ENOG410XNW1. LUCA.
    KOiK03366.

    Enzyme and pathway databases

    BRENDAi1.1.1.76. 960.

    Miscellaneous databases

    EvolutionaryTraceiQ9ZNN8.

    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.
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02415. 23BDH. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiBUDC_CORGT
    AccessioniPrimary (citable) accession number: Q9ZNN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: May 1, 1999
    Last modified: November 2, 2016
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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.