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Q49KG0

- ACDH_PSEPU

UniProt

Q49KG0 - ACDH_PSEPU

Protein

Acetaldehyde dehydrogenase

Gene

cbzQ

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.UniRule annotation

    Catalytic activityi

    Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei132 – 1321Acyl-thioester intermediateUniRule annotation
    Binding sitei290 – 2901NADUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 154NADUniRule annotation
    Nucleotide bindingi163 – 1719NADUniRule annotation

    GO - Molecular functioni

    1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB-HAMAP
    2. NAD binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. aromatic compound catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetaldehyde dehydrogenaseUniRule annotation (EC:1.2.1.10UniRule annotation)
    Alternative name(s):
    Acetaldehyde dehydrogenase [acetylating]UniRule annotation
    Gene namesi
    Name:cbzQ
    Encoded oniPlasmid pKW10 Publication
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Acetaldehyde dehydrogenasePRO_0000337983Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ49KG0.
    SMRiQ49KG0. Positions 1-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

    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.

    Q49KG0-1 [UniParc]FASTAAdd to Basket

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    MTTKRKVAIV GSGNVGTDLM IKILRNAEHL EMAVMVGIDP ASDGLARAGR    50
    MGVATTHEGV AGLVKMPEFA DVDFVFDATS AGAHVKNDAL LRATKPGIRV 100
    IDLTPAAIGP YCVPVVNLEQ HVNAENLNMV TCGGQATIPM VAAVSRVAKV 150
    HYAEIVASIA SKSAGPGTRA NIDEFTETTS KAIEAIGGAA KGKAIIIMNP 200
    AEPPLMMRDT VYVLSEAADQ DHVEASIEEM VAAVNAYVPG YRLKQKVQFE 250
    VIPDTAPLNI PGHGEFSGLK TSVFIEVEGA AHYLPAYAGN LDIMTSAALA 300
    TAERMAQSMS QA 312
    Length:312
    Mass (Da):32,710
    Last modified:September 13, 2005 - v1
    Checksum:i51B57FFE9CF24B43
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY831461 Genomic DNA. Translation: AAX50131.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY831461 Genomic DNA. Translation: AAX50131.1 .

    3D structure databases

    ProteinModelPortali Q49KG0.
    SMRi Q49KG0. Positions 1-312.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "GJ31 meta-operon."
      Reineke W., Kunze M.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: GJ31.

    Entry informationi

    Entry nameiACDH_PSEPU
    AccessioniPrimary (citable) accession number: Q49KG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 43 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

    Plasmid

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3