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Q9S153 (ACDH3_COMTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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 3

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 3
Gene names
Name:mhpF
OrganismComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifier285 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

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 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
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 3 HAMAP-Rule MF_01657
PRO_0000387652

Regions

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

Sites

Active site1321Acyl-thioester intermediate By similarity
Binding site2891NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9S153 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A107BBAF90A009EF

FASTA31633,136
        10         20         30         40         50         60 
MTRKLKAAII GSGNIGTDLM IKILRHGKNI EMGAMVGIDP HSDGLARASR MGVATTHEGV 

        70         80         90        100        110        120 
EGLTRMPGFA EIDFVFDATS AGAHVKNDAF LRSLKPGIRM IDLTPAAIGP YCIPVVNGDM 

       130        140        150        160        170        180 
HLDAPNVNMV TCGGQATIPM VAAVSRVAKV HYGEIIASIA SKSAGPGTRA NIDEFTETTS 

       190        200        210        220        230        240 
KAIEVVGGAT KGKAIIIMNP AEPPLIMRDT VYTLSALADE AAIAASVEQM AAAVQSYVPG 

       250        260        270        280        290        300 
YRLKQQVQFD RIDTPIRIPG VGNALTGLKT SIFLEVEGAA HYLPAYAGNL DIMTSAGLRT 

       310 
AEHMAERMLA TLAVAA 

« Hide

References

[1]"Genetic organization and characteristics of the 3-(3-hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni TA441."
Arai H., Yamamoto T., Ohishi T., Shimizu T., Nakata T., Kudo T.
Microbiology 145:2813-2820(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TA441.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB024335 Genomic DNA. Translation: BAA82883.1.

3D structure databases

ProteinModelPortalQ9S153.
SMRQ9S153. Positions 1-309.
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 nameACDH3_COMTE
AccessionPrimary (citable) accession number: Q9S153
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 51 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