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Protein

NADP-dependent isopropanol dehydrogenase

Gene

adh

Organism
Clostridium beijerinckii (Clostridium MP)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is active with acetaldehyde and propionaldehyde.2 Publications

Catalytic activityi

Propan-2-ol + NADP+ = acetone + NADPH.2 Publications

Cofactori

Zn2+3 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

Kineticsi

  1. KM=5.7 mM for 2-butanol1 Publication
  2. KM=10 mM for isopropanol1 Publication
  3. KM=5.2 mM for 2-pentanol1 Publication
  4. KM=1 mM for acetone1 Publication
  5. KM=1.5 mM for 2-butanone1 Publication
  6. KM=0.03 mM for NADPH1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi37Zinc; catalytic3 Publications1
    Metal bindingi59Zinc; catalytic3 Publications1
    Metal bindingi60Zinc; catalytic3 Publications1
    Metal bindingi150Zinc; catalytic3 Publications1
    Binding sitei218NADP1 Publication1
    Binding sitei340NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi175 – 178NADP1 Publication4
    Nucleotide bindingi198 – 200NADP1 Publication3
    Nucleotide bindingi265 – 267NADP1 Publication3

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NADP, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADP-dependent isopropanol dehydrogenase (EC:1.1.1.80)
    Alternative name(s):
    CbADH
    Gene namesi
    Name:adh
    OrganismiClostridium beijerinckii (Clostridium MP)
    Taxonomic identifieri1520 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001607391 – 351NADP-dependent isopropanol dehydrogenaseAdd BLAST351

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Structurei

    Secondary structure

    1351
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 8Combined sources7
    Beta strandi11 – 16Combined sources6
    Beta strandi27 – 34Combined sources8
    Helixi38 – 46Combined sources9
    Beta strandi53 – 56Combined sources4
    Beta strandi61 – 68Combined sources8
    Beta strandi80 – 83Combined sources4
    Beta strandi90 – 92Combined sources3
    Helixi93 – 96Combined sources4
    Helixi100 – 102Combined sources3
    Turni106 – 109Combined sources4
    Turni113 – 115Combined sources3
    Beta strandi119 – 128Combined sources10
    Helixi129 – 132Combined sources4
    Helixi142 – 146Combined sources5
    Turni147 – 150Combined sources4
    Helixi151 – 161Combined sources11
    Beta strandi170 – 173Combined sources4
    Helixi177 – 187Combined sources11
    Turni188 – 190Combined sources3
    Beta strandi194 – 197Combined sources4
    Helixi201 – 210Combined sources10
    Beta strandi213 – 216Combined sources4
    Helixi218 – 220Combined sources3
    Helixi223 – 230Combined sources8
    Turni231 – 233Combined sources3
    Beta strandi236 – 241Combined sources6
    Helixi248 – 255Combined sources8
    Beta strandi256 – 264Combined sources9
    Beta strandi270 – 277Combined sources8
    Turni278 – 281Combined sources4
    Helixi282 – 284Combined sources3
    Beta strandi289 – 293Combined sources5
    Helixi298 – 310Combined sources13
    Helixi316 – 319Combined sources4
    Beta strandi320 – 326Combined sources7
    Helixi327 – 329Combined sources3
    Helixi330 – 339Combined sources10
    Beta strandi345 – 350Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1JQBX-ray1.97A/B/C/D1-351[»]
    1KEVX-ray2.05A/B/C/D1-351[»]
    1PEDX-ray2.15A/B/C/D1-351[»]
    2B83X-ray2.25A/B/C/D1-351[»]
    3FPLX-ray1.90A1-152[»]
    A296-351[»]
    3FSRX-ray2.20A/B/C/D152-295[»]
    3FTNX-ray2.19A/B/C/D152-295[»]
    ProteinModelPortaliP25984.
    SMRiP25984.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25984.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25984-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKGFAMLGIN KLGWIEKERP VAGSYDAIVR PLAVSPCTSD IHTVFEGALG
    60 70 80 90 100
    DRKNMILGHE AVGEVVEVGS EVKDFKPGDR VIVPCTTPDW RSLEVQAGFQ
    110 120 130 140 150
    QHSNGMLAGW KFSNFKDGVF GEYFHVNDAD MNLAILPKDM PLENAVMITD
    160 170 180 190 200
    MMTTGFHGAE LADIQMGSSV VVIGIGAVGL MGIAGAKLRG AGRIIGVGSR
    210 220 230 240 250
    PICVEAAKFY GATDILNYKN GHIVDQVMKL TNGKGVDRVI MAGGGSETLS
    260 270 280 290 300
    QAVSMVKPGG IISNINYHGS GDALLIPRVE WGCGMAHKTI KGGLCPGGRL
    310 320 330 340 350
    RAEMLRDMVV YNRVDLSKLV THVYHGFDHI EEALLLMKDK PKDLIKAVVI

    L
    Length:351
    Mass (Da):37,716
    Last modified:December 4, 2007 - v2
    Checksum:iE1E925D37D7513B7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF157307 Genomic DNA. Translation: AAA23199.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF157307 Genomic DNA. Translation: AAA23199.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1JQBX-ray1.97A/B/C/D1-351[»]
    1KEVX-ray2.05A/B/C/D1-351[»]
    1PEDX-ray2.15A/B/C/D1-351[»]
    2B83X-ray2.25A/B/C/D1-351[»]
    3FPLX-ray1.90A1-152[»]
    A296-351[»]
    3FSRX-ray2.20A/B/C/D152-295[»]
    3FTNX-ray2.19A/B/C/D152-295[»]
    ProteinModelPortaliP25984.
    SMRiP25984.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25984.

    Family and domain databases

    Gene3Di3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiADH_CLOBE
    AccessioniPrimary (citable) accession number: P25984
    Secondary accession number(s): Q9R559
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: December 4, 2007
    Last modified: November 2, 2016
    This is version 100 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, 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.