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

Acetaldehyde dehydrogenase

Gene

TTHB247

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of acetaldehyde or propanal to acetyl-CoA or propanoyl-CoA, respectively, using NAD+ and coenzyme A. The aldehyde substrates can be directly channeled from the aldolase TTHB246 to the dehydrogenase TTHB247. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.1 Publication

Catalytic activityi

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

Kineticsi

The catalytic efficiency is similar when using acetaldehyde or propanaldehyde as substrate.

  1. KM=5.5 mM for acetaldehyde (at pH 8 and 25 degrees Celsius)1 Publication
  2. KM=6.4 mM for propanaldehyde (at pH 8 and 25 degrees Celsius)1 Publication
  3. KM=15.4 mM for acetaldehyde (when TTHB247 is in complex with the aldolase TTHB246, at pH 8 and 25 degrees Celsius)1 Publication
  4. KM=16.1 mM for propanaldehyde (when TTHB247 is in complex with the aldolase TTHB246, at pH 8 and 25 degrees Celsius)1 Publication

    Temperature dependencei

    Has a half-life of only 1.6 hours at 50 degrees Celsius. When TTHB247 is in complex with TTHB246, its half-life is increased by approximately 4 hours.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei127 – 1271Acyl-thioester intermediateBy similarity
    Binding sitei278 – 2781NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 154NADBy similarity
    Nucleotide bindingi158 – 1669NADBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-2270-MONOMER.
    BRENDAi1.2.1.87. 2305.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetaldehyde dehydrogenase (EC:1.2.1.10)
    Alternative name(s):
    Acetaldehyde dehydrogenase [acetylating]
    Propanal dehydrogenase (CoA-propanoylating) (EC:1.2.1.87)
    Propanaldehyde dehydrogenase
    Gene namesi
    Ordered Locus Names:TTHB247
    Encoded oniPlasmid pTT270 Publication
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532 Componenti: Plasmid pTT27

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 307307Acetaldehyde dehydrogenasePRO_0000387749Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer. Can also form a heterotetramer composed of two aldolase (TTHB246) and two dehydrogenase (TTHB247) subunits. Upon complex formation, the aldolase shows a 5-fold increase in substrate affinity, while the dehydrogenase shows a 3-fold decrease; the kcat values of each enzyme are reduced by 2-fold when they are in a complex.1 Publication

    Protein-protein interaction databases

    STRINGi300852.TTHB247.

    Structurei

    3D structure databases

    ProteinModelPortaliQ53WH9.
    SMRiQ53WH9. Positions 1-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acetaldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG4569.
    HOGENOMiHOG000052149.
    KOiK04073.
    OMAiHQGNVNM.
    OrthoDBiEOG6H1PXH.
    PhylomeDBiQ53WH9.

    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.

    Q53WH9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSERVKVAIL GSGNIGTDLM YKLLKNPGHM ELVAVVGIDP KSEGLARARA
    60 70 80 90 100
    LGLEASHEGI AYILERPEIK IVFDATSAKA HVRHAKLLRE AGKIAIDLTP
    110 120 130 140 150
    AARGPYVVPP VNLKEHLDKD NVNLITCGGQ ATIPLVYAVH RVAPVLYAEM
    160 170 180 190 200
    VSTVASRSAG PGTRQNIDEF TFTTARGLEA IGGAKKGKAI IILNPAEPPI
    210 220 230 240 250
    LMTNTVRCIP EDEGFDREAV VASVRAMERE VQAYVPGYRL KADPVFERLP
    260 270 280 290 300
    TPWGERTVVS MLLEVEGAGD YLPKYAGNLD IMTASARRVG EVFAQHLLGK

    PVEEVVA
    Length:307
    Mass (Da):33,115
    Last modified:May 24, 2005 - v1
    Checksum:i7778943730EC4177
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AP008227 Genomic DNA. Translation: BAD72043.1.
    RefSeqiWP_011229062.1. NC_006462.1.
    YP_145486.1. NC_006462.1.

    Genome annotation databases

    EnsemblBacteriaiBAD72043; BAD72043; BAD72043.
    GeneIDi3169218.
    KEGGittj:TTHB247.
    PATRICi23959444. VBITheThe93045_2203.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AP008227 Genomic DNA. Translation: BAD72043.1.
    RefSeqiWP_011229062.1. NC_006462.1.
    YP_145486.1. NC_006462.1.

    3D structure databases

    ProteinModelPortaliQ53WH9.
    SMRiQ53WH9. Positions 1-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi300852.TTHB247.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD72043; BAD72043; BAD72043.
    GeneIDi3169218.
    KEGGittj:TTHB247.
    PATRICi23959444. VBITheThe93045_2203.

    Phylogenomic databases

    eggNOGiCOG4569.
    HOGENOMiHOG000052149.
    KOiK04073.
    OMAiHQGNVNM.
    OrthoDBiEOG6H1PXH.
    PhylomeDBiQ53WH9.

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-2270-MONOMER.
    BRENDAi1.2.1.87. 2305.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    2. "Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes."
      Baker P., Hillis C., Carere J., Seah S.Y.
      Biochemistry 51:1942-1952(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, COMPLEX WITH TTHB246, ALDEHYDE CHANNELING.
      Strain: HB8 / ATCC 27634 / DSM 579.

    Entry informationi

    Entry nameiACDH_THET8
    AccessioniPrimary (citable) accession number: Q53WH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 3, 2009
    Last sequence update: May 24, 2005
    Last modified: May 27, 2015
    This is version 66 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

    Complete proteome, Plasmid, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.