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Q53WH9 (ACDH_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Ordered Locus Names:TTHB247
Encoded onPlasmid pTT27
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. Ref.2

Propanal + CoA + NAD+ = propanoyl-CoA + NADH. Ref.2

Subunit structure

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. Ref.2

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=5.5 mM for acetaldehyde (at pH 8 and 25 degrees Celsius) Ref.2

KM=6.4 mM for propanaldehyde (at pH 8 and 25 degrees Celsius)

KM=15.4 mM for acetaldehyde (when TTHB247 is in complex with the aldolase TTHB246, at pH 8 and 25 degrees Celsius)

KM=16.1 mM for propanaldehyde (when TTHB247 is in complex with the aldolase TTHB246, at pH 8 and 25 degrees Celsius)

Temperature dependence:

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.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Plasmid
Reference proteome
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

acetaldehyde dehydrogenase (acetylating) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000387749

Regions

Nucleotide binding12 – 154NAD By similarity
Nucleotide binding158 – 1669NAD By similarity

Sites

Active site1271Acyl-thioester intermediate By similarity
Binding site2781NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q53WH9 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 7778943730EC4177

FASTA30733,115
        10         20         30         40         50         60 
MSERVKVAIL GSGNIGTDLM YKLLKNPGHM ELVAVVGIDP KSEGLARARA LGLEASHEGI 

        70         80         90        100        110        120 
AYILERPEIK IVFDATSAKA HVRHAKLLRE AGKIAIDLTP AARGPYVVPP VNLKEHLDKD 

       130        140        150        160        170        180 
NVNLITCGGQ ATIPLVYAVH RVAPVLYAEM VSTVASRSAG PGTRQNIDEF TFTTARGLEA 

       190        200        210        220        230        240 
IGGAKKGKAI IILNPAEPPI LMTNTVRCIP EDEGFDREAV VASVRAMERE VQAYVPGYRL 

       250        260        270        280        290        300 
KADPVFERLP TPWGERTVVS MLLEVEGAGD YLPKYAGNLD IMTASARRVG EVFAQHLLGK 


PVEEVVA 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008227 Genomic DNA. Translation: BAD72043.1.
RefSeqYP_145486.1. NC_006462.1.

3D structure databases

ProteinModelPortalQ53WH9.
SMRQ53WH9. Positions 1-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHB247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD72043; BAD72043; BAD72043.
GeneID3169218.
KEGGttj:TTHB247.
PATRIC23959444. VBITheThe93045_2203.

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAHLKHAPL.
OrthoDBEOG6H1PXH.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-2270-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01657. Ac_ald_DH_ac.
InterProIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACDH_THET8
AccessionPrimary (citable) accession number: Q53WH9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 24, 2005
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families