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Q49KG0 (ACDH_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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]
Gene names
Name:cbzQ
Encoded onPlasmid pKW1
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds By similarity. HAMAP-Rule MF_01657

Catalytic activity

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. HAMAP-Rule MF_01657

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termPlasmid
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 – 312312Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000337983

Regions

Nucleotide binding12 – 154NAD By similarity
Nucleotide binding163 – 1719NAD By similarity

Sites

Active site1321Acyl-thioester intermediate By similarity
Binding site2901NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49KG0 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 51B57FFE9CF24B43

FASTA31232,710
        10         20         30         40         50         60 
MTTKRKVAIV GSGNVGTDLM IKILRNAEHL EMAVMVGIDP ASDGLARAGR MGVATTHEGV 

        70         80         90        100        110        120 
AGLVKMPEFA DVDFVFDATS AGAHVKNDAL LRATKPGIRV IDLTPAAIGP YCVPVVNLEQ 

       130        140        150        160        170        180 
HVNAENLNMV TCGGQATIPM VAAVSRVAKV HYAEIVASIA SKSAGPGTRA NIDEFTETTS 

       190        200        210        220        230        240 
KAIEAIGGAA KGKAIIIMNP AEPPLMMRDT VYVLSEAADQ DHVEASIEEM VAAVNAYVPG 

       250        260        270        280        290        300 
YRLKQKVQFE VIPDTAPLNI PGHGEFSGLK TSVFIEVEGA AHYLPAYAGN LDIMTSAALA 

       310 
TAERMAQSMS QA 

« Hide

References

[1]"GJ31 meta-operon."
Reineke W., Kunze M.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GJ31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY831461 Genomic DNA. Translation: AAX50131.1.

3D structure databases

ProteinModelPortalQ49KG0.
SMRQ49KG0. Positions 1-312.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PSEPU
AccessionPrimary (citable) accession number: Q49KG0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 42 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