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Q9KWS1 (ACDH_PSESP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:amnH
OrganismPseudomonas sp.
Taxonomic identifier306 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length316 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 2-aminophenol. Ref.1

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
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 – 316316Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000383027

Regions

Nucleotide binding13 – 164NAD By similarity
Nucleotide binding162 – 1709NAD By similarity

Sites

Active site1311Acyl-thioester intermediate By similarity
Binding site2901NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KWS1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1A709C936C057242

FASTA31633,170
        10         20         30         40         50         60 
MSDDRLSVAI IGSGNIGTDL MIKIMRNSKL LKVGAMVGID PKSDGLARAQ RLGVPTTAEG 

        70         80         90        100        110        120 
VDGLLDMPAF RDIKIAFDAT SAGAQAIHNQ KLQAHGVRVI DLTPAAIGPY VIPVVNFDQH 

       130        140        150        160        170        180 
VDAPNINMVT CGGQATIPIV HAVSKVSPVH YAEIVASISS KSAGPGTRAN IDEFTETTSK 

       190        200        210        220        230        240 
AILEVGGAAQ GRAIIILNPA EPPLIMRDTV YCFVSAEANI DAITDSVEQM VKSVQEYVPG 

       250        260        270        280        290        300 
YRLKQKVQFE KIVAGNEQNI PGLGWSTGLK VSVFLEVEGA GHYLPSYAGN LDIMTSAGLT 

       310 
VAERIAGSGV QVGGLK 

« Hide

References

[1]"Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme."
Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K.
J. Biol. Chem. 272:14727-14732(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: AP-3.
[2]"Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3."
Takenaka S., Murakami S., Kim Y.J., Aoki K.
Arch. Microbiol. 174:265-272(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AP-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB020521 Genomic DNA. Translation: BAB03537.1.

3D structure databases

ProteinModelPortalQ9KWS1.
SMRQ9KWS1. Positions 3-308.
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_PSESP
AccessionPrimary (citable) accession number: Q9KWS1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 54 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