Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetaldehyde dehydrogenase 1

Gene

tesF

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
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 sitei132 – 1321Acyl-thioester intermediateUniRule annotation
Binding sitei274 – 2741NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi163 – 1719NADUniRule 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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16930.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenase 1UniRule annotation (EC:1.2.1.10UniRule annotation)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 1UniRule annotation
Gene namesi
Name:tesF
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Acetaldehyde dehydrogenase 1PRO_0000387650Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ83VZ4.
SMRiQ83VZ4. Positions 1-295.
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.

Q83VZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQKKIKCAL IGPGNIGTDL LMKLQRSPIL EPVWMVGIDP ESDGLKRARE
60 70 80 90 100
MGIKTTADGV DGLLPFVKED GIQIAFDATS AYVHAENSRK LNELGVLMID
110 120 130 140 150
LTPAAIGPYC VPSVNLAEKV AEKAMNVNMV TCGGQATIPM VAAVSRVQAV
160 170 180 190 200
SYGEIVATVS SRSVGPGTRK NIDEFTRTTS GAVEKIGGAQ KGKAIIVINP
210 220 230 240 250
AEPPLIMRDT IHCLTVDTPK PAEIEASVHA MIKEVQKYVP GYKLVNGPVI
260 270 280 290 300
DGNRVSIYME VEGLGDYLPK YAGNLDIMTA AAARTAEMFA EEILAGRFEL

AEAAVAV
Length:307
Mass (Da):32,667
Last modified:June 1, 2003 - v1
Checksum:iF19FDF0742DB27B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB063482 Genomic DNA. Translation: BAC67695.1.
RefSeqiWP_004341179.1. NZ_AWTP01000024.1.

Genome annotation databases

GeneIDi8564087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB063482 Genomic DNA. Translation: BAC67695.1.
RefSeqiWP_004341179.1. NZ_AWTP01000024.1.

3D structure databases

ProteinModelPortaliQ83VZ4.
SMRiQ83VZ4. Positions 1-295.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8564087.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16930.

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. "Gene encoding the hydrolase for the product of the meta-cleavage reaction in testosterone degradation by Comamonas testosteroni."
    Horinouchi M., Hayashi T., Koshino H., Yamamoto T., Kudo T.
    Appl. Environ. Microbiol. 69:2139-2152(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: TA441.

Entry informationi

Entry nameiACDH1_COMTE
AccessioniPrimary (citable) accession number: Q83VZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: June 1, 2003
Last modified: April 1, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.