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Q52060 (ACDH_PSEUF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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]
Gene names
Name:dmpF
Encoded onPlasmid pVI150
OrganismPseudomonas sp. (strain CF600)
Taxonomic identifier79676 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Can also act on propanal and butanal to form propanoyl-CoA and butanoyl-CoA, respectively. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower. Ref.1

Catalytic activity

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

Enzyme regulation

Is not activated by Mn2+, Mg2+, Ca2+, Zn2+ or Co2+. Ref.2

Pathway

Aromatic compound metabolism; phenol degradation. HAMAP-Rule MF_01657

Subunit structure

Heterotetramer composed of two DmpG (aldolase) and two DmpF (dehydrogenase) subunits, which allows a direct channeling of acetaldehyde between the two active sites. Ref.2 Ref.3

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Biophysicochemical properties

pH dependence:

Activity increases gradually over the pH range 6.5-8.5. HAMAP-Rule MF_01657

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000404201

Regions

Nucleotide binding12 – 154NAD HAMAP-Rule MF_01657
Nucleotide binding163 – 1719NAD HAMAP-Rule MF_01657

Sites

Active site1321Acyl-thioester intermediate By similarity
Binding site2901NAD

Secondary structure

..................................................... 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q52060 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2B38A98CE97B50DC

FASTA31232,685
        10         20         30         40         50         60 
MNQKLKVAII GSGNIGTDLM IKVLRNAKYL EMGAMVGIDA ASDGLARAQR MGVTTTYAGV 

        70         80         90        100        110        120 
EGLIKLPEFA DIDFVFDATS ASAHVQNEAL LRQAKPGIRL IDLTPAAIGP YCVPVVNLEE 

       130        140        150        160        170        180 
HLGKLNVNMV TCGGQATIPM VAAVSRVAKV HYAEIVASIS SKSAGPGTRA NIDEFTETTS 

       190        200        210        220        230        240 
KAIEVIGGAA KGKAIIIMNP AEPPLIMRDT VYVLSAAADQ AAVAASVAEM VQAVQAYVPG 

       250        260        270        280        290        300 
YRLKQQVQFD VIPESAPLNI PGLGRFSGLK TSVFLEVEGA AHYLPAYAGN LDIMTSAALA 

       310 
TAERMAQSML NA 

« Hide

References

[1]"Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600."
Shingler V., Marklund U., Powlowski J.
J. Bacteriol. 174:711-724(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: CF600.
[2]"Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600."
Powlowski J., Sahlman L., Shingler V.
J. Bacteriol. 175:377-385(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-6, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, INTERACTION WITH DMPG, PH DEPENDENCE.
Strain: CF600.
[3]"Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate."
Manjasetty B.A., Powlowski J., Vrielink A.
Proc. Natl. Acad. Sci. U.S.A. 100:6992-6997(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPG AND NAD, SUBUNIT, REACTION MECHANISM.
Strain: CF600.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60835 Genomic DNA. Translation: CAA43226.1.
PIRS24419.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVMX-ray1.70B/D/F/H1-312[»]
ProteinModelPortalQ52060.
SMRQ52060. Positions 1-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ52060. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12780.
UniPathwayUPA00728.

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...

Other

EvolutionaryTraceQ52060.

Entry information

Entry nameACDH_PSEUF
AccessionPrimary (citable) accession number: Q52060
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 68 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways