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Q0K3N1 (ACDH2_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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 2

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 2
Gene names
Ordered Locus Names:H16_B0596
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length302 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 termComplete proteome
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 – 302302Acetaldehyde dehydrogenase 2 HAMAP-Rule MF_01657
PRO_0000387713

Regions

Nucleotide binding161 – 1699NAD By similarity

Sites

Active site1301Acyl-thioester intermediate By similarity
Binding site2721NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0K3N1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: C202DC8C45B3C124

FASTA30231,935
        10         20         30         40         50         60 
MNKIRCALIG PGNIGTDLLY KLRRSDILEP VWMVGVEPSS EGLARARELG LKTTSDGIDG 

        70         80         90        100        110        120 
LLPHLEADDI RIAFDATSAY VHAEHSARLT ARGVRVIDLT PAAIGPFCVP PVNLDAHIGS 

       130        140        150        160        170        180 
NEMNVNMVTC GGQATIPMVY AVSRVQPVAY GEIVATVSSR SVGPGTRRNI DEFTRTTAGA 

       190        200        210        220        230        240 
IEAVGGARQG KAIIVINPAE PPLIMRDTIH CLTDDAPDVA AITASVHDMI AEVRKYVPGY 

       250        260        270        280        290        300 
TLKNGPVFDG KRVSIFLEVE GLGDYLPKYA GNLDIMTASA ARTAECIAAA MRAGSAQESA 


NA 

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260480 Genomic DNA. Translation: CAJ95393.1.
RefSeqYP_728758.1. NC_008314.1.

3D structure databases

ProteinModelPortalQ0K3N1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_B0596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ95393; CAJ95393; H16_B0596.
GeneID4456557.
KEGGreh:H16_B0596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMATVIHARV.
OrthoDBEOG6H1PXH.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-4303-MONOMER.

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 nameACDH2_CUPNH
AccessionPrimary (citable) accession number: Q0K3N1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 57 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