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Protein

Alcohol dehydrogenase 2

Gene

ADH2

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Versatile oxidoreductase that catalyzes the oxidation and reduction of a broad range of substrates. Preferentially oxidizes secondary alcohols. Has highest activity for racemic 2-octanol. Is also an efficient reductase for selected substrates. Substrate selectivity was found for medium chain lipophilic ketones. Has highest activities for 2-octanone, 2-nonanone and 2-decanone. The enzyme is (S)-selective in the reduction direction and produces exclusively the (S)-enantiomer.1 Publication

Catalytic activityi

A secondary alcohol + NAD+ = a ketone + NADH.1 Publication

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Kineticsi

kcat is 1.05 sec(-1) with (S)-2-octanol as substrate and 3.42 sec(-1) for NAD+. kcat is 0.56 sec(-1) for (2)-octanone.
  1. KM=1.42 mM for (S)-2-octanol1 Publication
  2. KM=5.38 mM for (2)-octanone1 Publication
  3. KM=17.8 mM for NAD+1 Publication

    pH dependencei

    Optimum pH is 9.5 for the oxidation reaction, and 6.5 for the reduction reaction.1 Publication

    Temperature dependencei

    Optimum temperature is 28-33 degrees Celsius. Active from 22 to 37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi47Zinc 1; catalyticBy similarity1
    Metal bindingi70Zinc 1; catalyticBy similarity1
    Metal bindingi101Zinc 2By similarity1
    Metal bindingi104Zinc 2By similarity1
    Metal bindingi107Zinc 2By similarity1
    Metal bindingi115Zinc 2By similarity1
    Metal bindingi157Zinc 1; catalyticBy similarity1
    Binding sitei205NADBy similarity1
    Binding sitei210NADBy similarity1
    Binding sitei344NADBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi181 – 187NADBy similarity7
    Nucleotide bindingi272 – 274NADBy similarity3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    LigandMetal-binding, NAD, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase 2 (EC:1.1.1.1)
    Gene namesi
    Name:ADH2
    Ordered Locus Names:YALI0E17787g
    OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
    Taxonomic identifieri284591 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
    Proteomesi
    • UP000001300 Componenti: Chromosome E

    Subcellular locationi

    GO - Cellular componenti

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004252811 – 351Alcohol dehydrogenase 2Add BLAST351

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi4952.XP_504077.1.

    Structurei

    3D structure databases

    ProteinModelPortaliF2Z678.
    SMRiF2Z678.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    InParanoidiF2Z678.
    KOiK13953.
    OMAiRKGAFPH.
    OrthoDBiEOG092C2Q8E.

    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. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiView protein in PROSITE
    PS00059. ADH_ZINC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    F2Z678-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSAPVIPKTQ KGVIFETSGG PLMYKDIPVP VPADDEILVN VKFSGVCHTD
    60 70 80 90 100
    LHAWKGDWPL DTKLPLVGGH EGAGVVVAKG KNVDTFEIGD YAGIKWINKA
    110 120 130 140 150
    CYTCEFCQVA AEPNCPNATM SGYTHDGSFQ QYATANAVQA AHIPKNCDLA
    160 170 180 190 200
    EIAPILCAGI TVYKALKTAA ILAGQWVAVT GAGGGLGTLA VQYAKAMGYR
    210 220 230 240 250
    VLAIDTGADK EKMCKDLGAE VFIDFAKTKD LVKDVQEATK GGPHAVINVS
    260 270 280 290 300
    VSEFAVNQSI EYVRTLGTVV LVGLPAGAVC KSPIFQQVAR SIQIKGSYVG
    310 320 330 340 350
    NRADSQEAIE FFSRGLVKSP IIIIGLSELE KVYKLMEEGK IAGRYVLDTS

    K
    Length:351
    Mass (Da):37,315
    Last modified:May 31, 2011 - v1
    Checksum:iFD626D7D5EAF133B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CR382131 Genomic DNA. Translation: CAG79670.1.
    RefSeqiXP_504077.1. XM_504077.1.

    Genome annotation databases

    EnsemblFungiiCAG79670; CAG79670; YALI0_E17787g.
    GeneIDi2912417.
    KEGGiyli:YALI0E17787g.

    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.

    Entry informationi

    Entry nameiADH2_YARLI
    AccessioniPrimary (citable) accession number: F2Z678
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 19, 2014
    Last sequence update: May 31, 2011
    Last modified: July 5, 2017
    This is version 44 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families