Acetaldehyde dehydrogenase - Pseudomonas sp. (strain CF600)

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Q52060 (ACDH_PSEUF) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 66. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetaldehyde dehydrogenase
EC=1.2.1.10

Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]

Gene names

Name:

dmpF

Encoded on

Plasmid pVI150

Organism

Pseudomonas sp. (strain CF600)

Taxonomic identifier

79676 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria ›

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from direct assay Ref.2. Source: UniProtKB cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro phenol-containing compound catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from direct assay Ref.3 Ref.2. Source: UniProtKB NADP binding Inferred from direct assay Ref.2. Source: UniProtKB acetaldehyde dehydrogenase (acetylating) activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 312

312

Acetaldehyde dehydrogenase HAMAP-Rule MF_01657

PRO_0000404201

Regions

Nucleotide binding

12 – 15

NAD HAMAP-Rule MF_01657

Nucleotide binding

163 – 171

NAD HAMAP-Rule MF_01657

Sites

Active site

132

Acyl-thioester intermediate By similarity

Binding site

290

NAD

Secondary structure

312

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q52060 [UniParc].

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

FASTA

312

32,685

        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

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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.

PIR

S24419.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NVM	X-ray	1.70	B/D/F/H	1-312	[»]

ProteinModelPortal

Q52060.

SMR

Q52060. Positions 1-312.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q52060. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12780.

UniPathway

UPA00728.

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...

Other

EvolutionaryTrace

Q52060.

Entry information

Entry name

ACDH_PSEUF

Accession

Primary (citable) accession number: Q52060

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 8, 2011
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents