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Q47B12 (ACDH3_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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
Ordered Locus Names:Daro_3239
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length314 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 – 314314Acetaldehyde dehydrogenase 3 HAMAP-Rule MF_01657
PRO_0000337978

Regions

Nucleotide binding163 – 1719NAD By similarity

Sites

Active site1321Acyl-thioester intermediate By similarity
Binding site2911NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47B12 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: BA1845382DFE9832

FASTA31433,113
        10         20         30         40         50         60 
MNKKLKVAII GPGNIGTDLM IKIMRHGEHL EMGAMVGIDP QSDGLARAQR MGVATTHEGV 

        70         80         90        100        110        120 
EGLTRLPVFA DIDIVFDATS AGAHVRNDAF LRSLKPNIRM VDLTPAAIGP YCIPVVNGAA 

       130        140        150        160        170        180 
HDEALNVNMV TCGGQATIPM VAAVSRVAKV HYGEIIASIS SKSAGPGTRA NIDEFTETTS 

       190        200        210        220        230        240 
KAIEAVGGAA KGKAIIILNP AEPPLIMRDT VYCLSELVDE DEIAASVAQM AADVQKYVPG 

       250        260        270        280        290        300 
YRLKQKVQFD IIPASRPINI PGVGQRMSGL KTSVFLEVEG AAHYLPAYAG NLDIMTSAAK 

       310 
TTAERMAARI LSAA 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ47969.1.
RefSeqYP_286439.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47B12.
SMRQ47B12. Positions 1-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_3239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ47969; AAZ47969; Daro_3239.
GeneID3566585.
KEGGdar:Daro_3239.
PATRIC21605152. VBIDecAro89105_3221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAHQGNVNM.
OrthoDBEOG6H1PXH.

Enzyme and pathway databases

BioCycDARO159087:GI5B-3312-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 nameACDH3_DECAR
AccessionPrimary (citable) accession number: Q47B12
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 62 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