Q53WH9 (ACDH_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetaldehyde dehydrogenase
EC=1.2.1.10

Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]
Propanaldehyde dehydrogenase

Gene names

Ordered Locus Names:

TTHB247

Encoded on

Plasmid pTT27

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of acetaldehyde or propanaldehyde 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 Propanaldehyde + 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 process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Plasmid Reference proteome
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: HAMAP acetaldehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Acetaldehyde dehydrogenase HAMAP-Rule MF_01657		PRO_0000387749
Regions
	Nucleotide binding	12 – 15	4	NAD By similarity
	Nucleotide binding	158 – 166	9	NAD By similarity
Sites
	Active site	127	1	Acyl-thioester intermediate By similarity
	Binding site	278	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q53WH9 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 7778943730EC4177	FASTA	307	33,115
	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

References

	« Hide 'large scale' referencesShow '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.
RefSeq	YP_145486.1. NC_006462.1.
3D structure databases
ProteinModelPortal	Q53WH9.
SMR	Q53WH9. Positions 1-299.
ModBase	Search...
Protein-protein interaction databases
STRING	300852.TTHB247.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAD72043; BAD72043; BAD72043.
GeneID	3169218.
KEGG	ttj:TTHB247.
PATRIC	23959444. VBITheThe93045_2203.
Phylogenomic databases
eggNOG	COG4569.
HOGENOM	HOG000052149.
KO	K04073.
OMA	IRASHEG.
ProtClustDB	PRK08300.
Enzyme and pathway databases
BioCyc	TTHE300852:GH8R-2270-MONOMER.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_01657. Ac_ald_DH_ac.
InterPro	IPR003361. Acetaldehyde_dehydrogenase. IPR015426. Acetylaldehyde_DH_C. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. [Graphical view]
PANTHER	PTHR21123. PTHR21123. 1 hit.
Pfam	PF09290. AcetDehyd-dimer. 1 hit. PF01118. Semialdhyde_dh. 1 hit. [Graphical view]
PIRSF	PIRSF015689. Actaldh_dh_actl. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACDH_THET8

Accession

Primary (citable) accession number: Q53WH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 3, 2009
Last sequence update:	May 24, 2005
Last modified:	May 29, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program