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Protein

Acetaldehyde dehydrogenase

Gene

Ajs_0223

Organism
Acidovorax sp. (strain JS42)
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 sitei131 – 1311Acyl-thioester intermediateUniRule annotation
Binding sitei273 – 2731NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1709NADUniRule 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

BioCyciASP232721:GHWE-223-MONOMER.

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
Ordered Locus Names:Ajs_0223
OrganismiAcidovorax sp. (strain JS42)
Taxonomic identifieri232721 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax
ProteomesiUP000000645 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Acetaldehyde dehydrogenasePRO_0000387614Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi232721.Ajs_0223.

Structurei

3D structure databases

ProteinModelPortaliA1W2K2.
SMRiA1W2K2. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
OMAiHQGNVNM.
OrthoDBiEOG6H1PXH.

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.

A1W2K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQKIKCALI GPGNIGTDLL AKLQRSPVLE PVWMVGIDPE SDGLKRAREM
60 70 80 90 100
GIKTTHEGVD GLIPHMKADG VQIVFDATSA YVHAENSRKV NAQGALMIDL
110 120 130 140 150
TPAAIGPFCV PPVNLKEHVG KAEMNVNMVT CGGQATIPMV AAVSRVQPVA
160 170 180 190 200
YGEIVATVSS RSAGPGTRKN IDEFTRTTAG AIEKVGGAQK GKAIIIINPA
210 220 230 240 250
DPPLIMRDTV HCLVEGEPDK EAITRSIHDM LAEVQKYVPG YKLVNGPVFD
260 270 280 290 300
GNRVSVFLEV EGLGDYLPKY AGNLDIMTAA AARTAEMFAE EILAGKLTLQ

AA
Length:302
Mass (Da):32,064
Last modified:February 6, 2007 - v1
Checksum:iE02DD0256AD16092
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000539 Genomic DNA. Translation: ABM40477.1.
RefSeqiWP_011803689.1. NC_008782.1.
YP_984553.1. NC_008782.1.

Genome annotation databases

EnsemblBacteriaiABM40477; ABM40477; Ajs_0223.
KEGGiajs:Ajs_0223.
PATRICi20685662. VBIAciSp27161_0390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000539 Genomic DNA. Translation: ABM40477.1.
RefSeqiWP_011803689.1. NC_008782.1.
YP_984553.1. NC_008782.1.

3D structure databases

ProteinModelPortaliA1W2K2.
SMRiA1W2K2. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi232721.Ajs_0223.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM40477; ABM40477; Ajs_0223.
KEGGiajs:Ajs_0223.
PATRICi20685662. VBIAciSp27161_0390.

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
OMAiHQGNVNM.
OrthoDBiEOG6H1PXH.

Enzyme and pathway databases

BioCyciASP232721:GHWE-223-MONOMER.

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. "Complete sequence of chromosome 1 of Acidovorax sp. JS42."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
    , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JS42.

Entry informationi

Entry nameiACDH_ACISJ
AccessioniPrimary (citable) accession number: A1W2K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: February 6, 2007
Last modified: April 1, 2015
This is version 56 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

Complete proteome, Reference proteome

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.