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Q53WH9

- ACDH_THET8

UniProt

Q53WH9 - ACDH_THET8

Protein

Acetaldehyde dehydrogenase

Gene

TTHB247

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    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

    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

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-2270-MONOMER.

    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: 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

    MSERVKVAIL GSGNIGTDLM YKLLKNPGHM ELVAVVGIDP KSEGLARARA    50
    LGLEASHEGI AYILERPEIK IVFDATSAKA HVRHAKLLRE AGKIAIDLTP 100
    AARGPYVVPP VNLKEHLDKD NVNLITCGGQ ATIPLVYAVH RVAPVLYAEM 150
    VSTVASRSAG PGTRQNIDEF TFTTARGLEA IGGAKKGKAI IILNPAEPPI 200
    LMTNTVRCIP EDEGFDREAV VASVRAMERE VQAYVPGYRL KADPVFERLP 250
    TPWGERTVVS MLLEVEGAGD YLPKYAGNLD IMTASARRVG EVFAQHLLGK 300
    PVEEVVA 307
    Length:307
    Mass (Da):33,115
    Last modified:May 24, 2005 - v1
    Checksum:i7778943730EC4177
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008227 Genomic DNA. Translation: BAD72043.1.
    RefSeqiYP_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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008227 Genomic DNA. Translation: BAD72043.1 .
    RefSeqi YP_145486.1. NC_006462.1.

    3D structure databases

    ProteinModelPortali Q53WH9.
    SMRi Q53WH9. Positions 1-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHB247.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD72043 ; BAD72043 ; BAD72043 .
    GeneIDi 3169218.
    KEGGi ttj:TTHB247.
    PATRICi 23959444. VBITheThe93045_2203.

    Phylogenomic databases

    eggNOGi COG4569.
    HOGENOMi HOG000052149.
    KOi K04073.
    OMAi HQGNVNM.
    OrthoDBi EOG6H1PXH.
    PhylomeDBi Q53WH9.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-2270-MONOMER.

    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. "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: October 1, 2014
    This is version 61 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