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Protein

Acetaldehyde dehydrogenase

Gene

pheF

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261Acyl-thioester intermediateUniRule annotation
Binding sitei269 – 2691NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 144NADUniRule annotation
Nucleotide bindingi157 – 1659NADUniRule annotation

GO - Molecular functioni

  1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB-HAMAP
  2. NAD binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenaseUniRule annotation (EC:1.2.1.10UniRule annotation)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]UniRule annotation
Gene namesi
Name:pheF
Encoded oniPlasmid pGGO10 Publication
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Acetaldehyde dehydrogenasePRO_0000387626Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB0VXM6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.

Sequencei

Sequence statusi: Complete.

B0VXM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVKVAILG SGNIGTDLMM KLERSNILQL TAMIGIDPES DGLRRAKEKG
60 70 80 90 100
YTVISTGIKG FLEQPELADI VFDATSAKAH IRHAKLLKEA GKTVLDLTPA
110 120 130 140 150
AVGALVVPPV NLHKHLDEWN VNLITCGGQA TIPIVHAINR VHPVGYAEIV
160 170 180 190 200
ATIASKSAGP GTRANIDEFT QTTARGIEKI GGAKKGKAII ILNPAEPPIM
210 220 230 240 250
MRNTVYALVE EGKIDENAIV QSILEMVKTV QSYVPGYRIR TEPIMDGNKI
260 270 280 290
TVFLEVEGAG DYLPKYSGNL DIMTAAAVKV AEELAKHKLA AQTA
Length:294
Mass (Da):31,478
Last modified:April 8, 2008 - v1
Checksum:i5F35DB4CBF043B23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ146476 Genomic DNA. Translation: ACA01538.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ146476 Genomic DNA. Translation: ACA01538.1.

3D structure databases

ProteinModelPortaliB0VXM6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiACDH_GEOSE
AccessioniPrimary (citable) accession number: B0VXM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: April 8, 2008
Last modified: October 1, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Plasmid

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.