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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331NAD1 Publication
    Binding sitei37 – 371NAD1 Publication
    Binding sitei88 – 881NAD; via carbonyl oxygen1 Publication
    Active sitei154 – 1541Proton acceptorPROSITE-ProRule annotationBy similarity
    Binding sitei154 – 1541NAD1 Publication
    Binding sitei158 – 1581NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 143NAD1 Publication
    Nucleotide bindingi61 – 622NAD1 Publication
    Nucleotide bindingi184 – 1896NAD1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi142 – 1421I → 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 Publication
    Mutagenesisi142 – 1421I → Q: Loss of L-BD oxidizing activity. Does not gain the ability to use meso-BD as substrate. 1 Publication
    Mutagenesisi148 – 1481F → 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 Publication
    Mutagenesisi148 – 1481F → N: Loss of L-BD oxidizing activity. Does not gain the ability to use meso-BD as substrate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 258258L-2,3-butanediol dehydrogenasePRO_0000418972Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    STRINGi196627.cg2958.

    Structurei

    Secondary structure

    1
    258
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85Combined sources
    Turni9 – 113Combined sources
    Helixi13 – 2513Combined sources
    Beta strandi28 – 336Combined sources
    Helixi35 – 373Combined sources
    Helixi38 – 4912Combined sources
    Turni50 – 523Combined sources
    Beta strandi55 – 595Combined sources
    Helixi65 – 7915Combined sources
    Beta strandi84 – 874Combined sources
    Helixi97 – 993Combined sources
    Helixi102 – 11211Combined sources
    Helixi114 – 1207Combined sources
    Beta strandi137 – 1393Combined sources
    Helixi142 – 1443Combined sources
    Helixi152 – 16312Combined sources
    Helixi173 – 1753Combined sources
    Beta strandi178 – 1847Combined sources
    Helixi190 – 20314Combined sources
    Helixi209 – 2146Combined sources
    Turni215 – 2173Combined sources
    Helixi226 – 23712Combined sources
    Helixi239 – 2413Combined sources
    Beta strandi248 – 2558Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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.
    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
    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.
    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...

    Publicationsi

    1. "Cloning, expression and nucleotide sequence of the L-2,3-butanediol dehydrogenase gene from Brevibacterium saccharolyticum C-1012."
      Ui S., Otagiri M., Mimura A., Dohmae N., Takio K., Ohkuma M., Kudo T.
      J. Ferment. Bioeng. 86:290-295(1998)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, FUNCTION, GENE NAME.
      Strain: C-10121 Publication.
    2. "Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli."
      Takusagawa Y., Otagiri M., Ui S., Ohtsuki T., Mimura A., Ohkuma M., Kudo T.
      Biosci. Biotechnol. Biochem. 65:1876-1878(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, STEREOSPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: C-1012.
    3. "Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases."
      Otagiri M., Ui S., Takusagawa Y., Ohtsuki T., Kurisu G., Kusunoki M.
      FEBS Lett. 584:219-223(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NAD, STEREOSELECTIVITY, MUTAGENESIS OF ILE-142 AND PHE-148.

    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: May 11, 2016
    This is version 70 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.