Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q52060

- ACDH_PSEUF

UniProt

Q52060 - ACDH_PSEUF

Protein

Acetaldehyde dehydrogenase

Gene

dmpF

Organism
Pseudomonas sp. (strain CF600)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Can also act on propanal and butanal to form propanoyl-CoA and butanoyl-CoA, respectively. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower.1 Publication

    Catalytic activityi

    Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.1 Publication

    Enzyme regulationi

    Is not activated by Mn2+, Mg2+, Ca2+, Zn2+ or Co2+.1 Publication

    pH dependencei

    Activity increases gradually over the pH range 6.5-8.5.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei132 – 1321Acyl-thioester intermediateBy similarity
    Binding sitei290 – 2901NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 154NAD1 Publication
    Nucleotide bindingi163 – 1719NAD1 Publication

    GO - Molecular functioni

    1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB
    2. NAD binding Source: UniProtKB
    3. NADP binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. aromatic compound catabolic process Source: UniProtKB
    2. phenol-containing compound catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12780.
    UniPathwayiUPA00728.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetaldehyde dehydrogenase (EC:1.2.1.10)
    Alternative name(s):
    Acetaldehyde dehydrogenase [acetylating]
    Gene namesi
    Name:dmpF
    Encoded oniPlasmid pVI1500 Publication
    OrganismiPseudomonas sp. (strain CF600)
    Taxonomic identifieri79676 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Acetaldehyde dehydrogenasePRO_0000404201Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer composed of two DmpG (aldolase) and two DmpF (dehydrogenase) subunits, which allows a direct channeling of acetaldehyde between the two active sites.2 Publications

    Protein-protein interaction databases

    IntActiQ52060. 1 interaction.

    Structurei

    Secondary structure

    1
    312
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Helixi14 – 2613
    Beta strandi28 – 369
    Helixi43 – 508
    Beta strandi55 – 584
    Helixi59 – 657
    Helixi67 – 715
    Beta strandi72 – 776
    Helixi81 – 9414
    Beta strandi99 – 1024
    Helixi114 – 1174
    Turni118 – 1236
    Beta strandi125 – 1284
    Helixi132 – 14514
    Beta strandi150 – 16011
    Helixi161 – 1633
    Helixi166 – 1694
    Helixi172 – 18514
    Beta strandi190 – 19910
    Beta strandi207 – 21711
    Helixi220 – 23516
    Beta strandi241 – 2455
    Beta strandi248 – 2525
    Beta strandi258 – 2603
    Turni261 – 2633
    Beta strandi264 – 2663
    Beta strandi268 – 27710
    Beta strandi282 – 2843
    Helixi289 – 31022

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NVMX-ray1.70B/D/F/H1-312[»]
    ProteinModelPortaliQ52060.
    SMRiQ52060. Positions 1-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ52060.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acetaldehyde dehydrogenase family.Curated

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_01657. Ac_ald_DH_ac.
    InterProiIPR003361. Acetaldehyde_dehydrogenase.
    IPR015426. Acetylaldehyde_DH_C.
    IPR016040. NAD(P)-bd_dom.
    IPR000534. Semialdehyde_DH_NAD-bd.
    [Graphical view]
    PfamiPF09290. AcetDehyd-dimer. 1 hit.
    PF01118. Semialdhyde_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
    SMARTiSM00859. Semialdhyde_dh. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q52060-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNQKLKVAII GSGNIGTDLM IKVLRNAKYL EMGAMVGIDA ASDGLARAQR    50
    MGVTTTYAGV EGLIKLPEFA DIDFVFDATS ASAHVQNEAL LRQAKPGIRL 100
    IDLTPAAIGP YCVPVVNLEE HLGKLNVNMV TCGGQATIPM VAAVSRVAKV 150
    HYAEIVASIS SKSAGPGTRA NIDEFTETTS KAIEVIGGAA KGKAIIIMNP 200
    AEPPLIMRDT VYVLSAAADQ AAVAASVAEM VQAVQAYVPG YRLKQQVQFD 250
    VIPESAPLNI PGLGRFSGLK TSVFLEVEGA AHYLPAYAGN LDIMTSAALA 300
    TAERMAQSML NA 312
    Length:312
    Mass (Da):32,685
    Last modified:November 1, 1996 - v1
    Checksum:i2B38A98CE97B50DC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60835 Genomic DNA. Translation: CAA43226.1.
    PIRiS24419.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60835 Genomic DNA. Translation: CAA43226.1 .
    PIRi S24419.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NVM X-ray 1.70 B/D/F/H 1-312 [» ]
    ProteinModelPortali Q52060.
    SMRi Q52060. Positions 1-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q52060. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00728 .
    BioCyci MetaCyc:MONOMER-12780.

    Miscellaneous databases

    EvolutionaryTracei Q52060.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_01657. Ac_ald_DH_ac.
    InterProi IPR003361. Acetaldehyde_dehydrogenase.
    IPR015426. Acetylaldehyde_DH_C.
    IPR016040. NAD(P)-bd_dom.
    IPR000534. Semialdehyde_DH_NAD-bd.
    [Graphical view ]
    Pfami PF09290. AcetDehyd-dimer. 1 hit.
    PF01118. Semialdhyde_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015689. Actaldh_dh_actl. 1 hit.
    SMARTi SM00859. Semialdhyde_dh. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR03215. ac_ald_DH_ac. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600."
      Shingler V., Marklund U., Powlowski J.
      J. Bacteriol. 174:711-724(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: CF600.
    2. "Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600."
      Powlowski J., Sahlman L., Shingler V.
      J. Bacteriol. 175:377-385(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-6, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, INTERACTION WITH DMPG, PH DEPENDENCE.
      Strain: CF600.
    3. "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate."
      Manjasetty B.A., Powlowski J., Vrielink A.
      Proc. Natl. Acad. Sci. U.S.A. 100:6992-6997(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPG AND NAD, SUBUNIT, REACTION MECHANISM.
      Strain: CF600.

    Entry informationi

    Entry nameiACDH_PSEUF
    AccessioniPrimary (citable) accession number: Q52060
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    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, Plasmid

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3