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Q47B12 (ACDH3_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 MF_01657

Catalytic activity

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

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Acetaldehyde dehydrogenase 3 HAMAP MF_01657
PRO_0000337978

Regions

Nucleotide binding163 – 1719NAD By similarity

Sites

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]"Complete sequence of Dechloromonas aromatica RCB."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
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...

Protein-protein interaction databases

STRINGQ47B12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3566585.
GenomeReviewsGene locus Daro_3239 in contig CP000089_GR.
KEGGdar:Daro_3239.
NMPDRfig|159087.4.peg.3778.
PATRIC21605152. VBIDecAro89105_3221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHBG300125.
OMAASRPINI.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycDARO159087:DARO_3239-MONOMER.

Family and domain databases

HAMAPMF_01657. Ac_ald_DH_ac.
[Tree]
InterProIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK04073.
PANTHERPTHR21123. Acetylald_dh. 1 hit.
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: January 25, 2012
This is version 48 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