Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alcohol dehydrogenase

Gene

adh

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional alcohol dehydrogenase exhibiting NAD+-dependent dehydrogenase activities for 2,3-butanediol, ethanol and acetaldehyde, and reductase activities for acetoin (NADH-dependent), and diacetyl and acetaldehyde (independently of whether NADH or NADPH is the reductant). The rate of oxidation of 2,3-butanediol is much higher than for the oxidation of ethanol. Has acetaldehyde dehydrogenase activity leading to acetate formation. May function in the release of excess reducing power in the absence of exogenous hydrogen acceptors such as oxygen.2 Publications

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.2 Publications
(R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH.2 Publications
An aldehyde + NAD+ + H2O = a carboxylate + NADH.2 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Kineticsi

  1. KM=0.67 mM for acetaldehyde (with NADH as cosubstrate)1 Publication
  2. KM=0.69 mM for acetaldehyde (with NADPH as cosubstrate)1 Publication
  3. KM=0.56 mM for acetoin (with NADH as cosubstrate)1 Publication
  4. KM=1.42 mM for acetoin (with NADPH as cosubstrate)1 Publication
  5. KM=0.56 mM for diacetyl (with NADH as cosubstrate)1 Publication
  6. KM=1.10 mM for diacetyl (with NADPH as cosubstrate)1 Publication
  7. KM=18.2 mM for erythro-2,3-butanediol (with NAD as cosubstrate)1 Publication
  8. KM=5.00 mM for ethanol (with NAD as cosubstrate)1 Publication
  9. KM=22.2 mM for threo-2,3-butanediol(with NAD as cosubstrate)1 Publication
  10. KM=0.011 mM for NADH (with acetaldehyde as cosubstrate)1 Publication
  11. KM=0.012 mM for NADH (with acetoin as cosubstrate)1 Publication
  12. KM=0.011 mM for NADH (with diacetyl as cosubstrate)1 Publication
  13. KM=0.009 mM for NAD (with ethanol as cosubstrate)1 Publication
  14. KM=0.138 mM for NAD (with erythro-2,3-butanediol as cosubstrate)1 Publication
  15. KM=0.145 mM for NAD (with threo-2,3-butanediol as cosubstrate)1 Publication
  16. KM=0.053 mM for NADPH (with acetaldehyde as cosubstrate)1 Publication
  17. KM=0.047 mM for NADPH (with acetoin as cosubstrate)1 Publication
  18. KM=0.050 mM for NADPH (with diacetyl as cosubstrate)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi41Zinc; catalyticBy similarity1
    Metal bindingi62Zinc; catalyticBy similarity1
    Metal bindingi63Zinc; catalyticBy similarity1
    Metal bindingi167Zinc; catalyticBy similarity1

    GO - Molecular functioni

    Keywordsi

    Molecular functionOxidoreductase
    LigandMetal-binding, NAD, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase (EC:1.1.1.12 Publications, EC:1.1.1.42 Publications, EC:1.2.1.32 Publications)
    Gene namesi
    Name:adh
    Ordered Locus Names:H16_A0757
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    Proteomesi
    • UP000008210 Componenti: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00004290322 – 366Alcohol dehydrogenaseAdd BLAST365

    Expressioni

    Inductioni

    By limited oxygen supply.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi381666.H16_A0757.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0KDL6.
    SMRiQ0KDL6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CPQ. Bacteria.
    COG1063. LUCA.
    HOGENOMiHOG000294694.
    OMAiHTVWEGA.

    Family and domain databases

    InterProiView protein in InterPro
    IPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    PfamiView protein in Pfam
    PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    SMARTiView protein in SMART
    SM00829. PKS_ER. 1 hit.
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.
    PROSITEiView protein in PROSITE
    PS00059. ADH_ZINC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q0KDL6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTAMMKAAVF VEPGRIELAD KPIPDIGPND ALVRITTTTI CGTDVHILKG
    60 70 80 90 100
    EYPVAKGLTV GHEPVGIIEK LGSAVTGYRE GQRVIAGAIC PNFNSYAAQD
    110 120 130 140 150
    GVASQDGSYL MASGQCGCHG YKATAGWRFG NMIDGTQAEY VLVPDAQANL
    160 170 180 190 200
    TPIPDGLTDE QVLMCPDIMS TGFKGAENAN IRIGDTVAVF AQGPIGLCAT
    210 220 230 240 250
    AGARLCGATT IIAIDGNDHR LEIARKMGAD VVLNFRNCDV VDEVMKLTGG
    260 270 280 290 300
    RGVDASIEAL GTQATFEQSL RVLKPGGTLS SLGVYSSDLT IPLSAFAAGL
    310 320 330 340 350
    GDHKINTALC PGGKERMRRL INVIESGRVD LGALVTHQYR LDDIVAAYDL
    360
    FANQRDGVLK IAIKPH
    Length:366
    Mass (Da):38,544
    Last modified:October 3, 2006 - v1
    Checksum:iF414508D73EFAAF8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM260479 Genomic DNA. Translation: CAJ91905.1.
    RefSeqiWP_010812995.1. NC_008313.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ91905; CAJ91905; H16_A0757.
    KEGGireh:H16_A0757.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM260479 Genomic DNA. Translation: CAJ91905.1.
    RefSeqiWP_010812995.1. NC_008313.1.

    3D structure databases

    ProteinModelPortaliQ0KDL6.
    SMRiQ0KDL6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi381666.H16_A0757.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAJ91905; CAJ91905; H16_A0757.
    KEGGireh:H16_A0757.

    Phylogenomic databases

    eggNOGiENOG4105CPQ. Bacteria.
    COG1063. LUCA.
    HOGENOMiHOG000294694.
    OMAiHTVWEGA.

    Family and domain databases

    InterProiView protein in InterPro
    IPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    PfamiView protein in Pfam
    PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    SMARTiView protein in SMART
    SM00829. PKS_ER. 1 hit.
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.
    PROSITEiView protein in PROSITE
    PS00059. ADH_ZINC. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiADH_CUPNH
    AccessioniPrimary (citable) accession number: Q0KDL6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: October 3, 2006
    Last modified: June 7, 2017
    This is version 75 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 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.