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B0VXM6 (ACDH_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 30. 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:pheF
Encoded onPlasmid pGGO1
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length294 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 termPlasmid
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 – 294294Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000387626

Regions

Nucleotide binding11 – 144NAD By similarity
Nucleotide binding157 – 1659NAD By similarity

Sites

Active site1261Acyl-thioester intermediate By similarity
Binding site2691NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B0VXM6 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 5F35DB4CBF043B23

FASTA29431,478
        10         20         30         40         50         60 
MSKVKVAILG SGNIGTDLMM KLERSNILQL TAMIGIDPES DGLRRAKEKG YTVISTGIKG 

        70         80         90        100        110        120 
FLEQPELADI VFDATSAKAH IRHAKLLKEA GKTVLDLTPA AVGALVVPPV NLHKHLDEWN 

       130        140        150        160        170        180 
VNLITCGGQA TIPIVHAINR VHPVGYAEIV ATIASKSAGP GTRANIDEFT QTTARGIEKI 

       190        200        210        220        230        240 
GGAKKGKAII ILNPAEPPIM MRNTVYALVE EGKIDENAIV QSILEMVKTV QSYVPGYRIR 

       250        260        270        280        290 
TEPIMDGNKI TVFLEVEGAG DYLPKYSGNL DIMTAAAVKV AEELAKHKLA AQTA 

« Hide

References

[1]"Characterization of the phe-operon responsible for phenol degradation in Geobacillus stearothermophilus."
Jaentges U.K., Omokoko B., Wilkening U., Reiss M., Zimmermann M., Hartmeier W.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 67824 / DSM 6285 / BR219.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ146476 Genomic DNA. Translation: ACA01538.1.

3D structure databases

ProteinModelPortalB0VXM6.
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 nameACDH_GEOSE
AccessionPrimary (citable) accession number: B0VXM6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 30 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