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Q2T7T0 (ACDH_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:mhpF
Ordered Locus Names:BTH_II0569
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length297 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 – 297297Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000387642

Regions

Nucleotide binding15 – 184NAD By similarity
Nucleotide binding162 – 1709NAD By similarity

Sites

Active site1301Acyl-thioester intermediate By similarity
Binding site2721NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2T7T0 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: F9C07F405011D23B

FASTA29732,241
        10         20         30         40         50         60 
MKNKSSRTRV AILGSGSIGL DLMFKVKASE HFDLKFVVGR HANSDGLKLA RSCNVETSSD 

        70         80         90        100        110        120 
GLDFLKENED AYDLVFDATS AAAHKVNNGF FSGAGKFVID LTPAKLGRLC VPCINLDDIG 

       130        140        150        160        170        180 
AEQNVNLITC GGQASLPLAY ALKQAVDEIE YLEVVSAIAS RSAGIATREN IDEYMTTTEY 

       190        200        210        220        230        240 
ALAQFSGAKK TKAILNINPA EPGVRMQTTL YAHARYRDFD RVRACVAEMV EKVREYVPGY 

       250        260        270        280        290 
RLVVEPIESQ GRITISLTVR GRGDYLPEYA GNLDIINCAA LAVASHRHAT ARLGATQ 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000085 Genomic DNA. Translation: ABC35657.1.
RefSeqYP_438769.1. NC_007650.1.

3D structure databases

ProteinModelPortalQ2T7T0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING271848.BTH_II0569.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC35657; ABC35657; BTH_II0569.
GeneID3844872.
KEGGbte:BTH_II0569.
PATRIC19298640. VBIBurTha36512_0651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAREVQKYV.
OrthoDBEOG6H1PXH.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-3913-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 nameACDH_BURTA
AccessionPrimary (citable) accession number: Q2T7T0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 60 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