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Protein

Acetaldehyde dehydrogenase 4

Gene

Daro_3783

Organism
Dechloromonas aromatica (strain RCB)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciDARO159087:GI5B-3861-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenase 4UniRule annotation (EC:1.2.1.10UniRule annotation)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 4UniRule annotation
Gene namesi
Ordered Locus Names:Daro_3783
OrganismiDechloromonas aromatica (strain RCB)
Taxonomic identifieri159087 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
ProteomesiUP000000550 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Acetaldehyde dehydrogenase 4PRO_0000387656Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi159087.Daro_3783.

Structurei

3D structure databases

ProteinModelPortaliQ479G9.
SMRiQ479G9. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
OMAiQRSEWLE.
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.

Q479G9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQKIKCALI GPGNIGTDLL YKLKRSPFLE PVWMIGIDPE SEGLKRAAEM
60 70 80 90 100
GLKTCATGVD GFLPHVLEDN VQIAFDATSA YVHAENSRKL NALGVLMIDL
110 120 130 140 150
TPAAIGPFCV PPVNLKEHVG RREMNVNMVT CGGQATIPMV AAVSRVQPVA
160 170 180 190 200
YGEIVATVSS KSAGPGTRKN IDEFTRTTAG AVEKVGGAKK GKAIIIINPA
210 220 230 240 250
EPPLVMRDTV HCLTETAPDQ AAITESIHAM IKEVQKYVPG YRLVNGPVFD
260 270 280 290 300
GNRVSVYMEV TGLGDFLPTY AGNLDIMTAA GARTAEMFAE EMIKGTLKLE

PVHA
Length:304
Mass (Da):32,459
Last modified:September 13, 2005 - v1
Checksum:i6A8193715761CC5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ48512.1.
RefSeqiWP_011289508.1. NC_007298.1.

Genome annotation databases

EnsemblBacteriaiAAZ48512; AAZ48512; Daro_3783.
KEGGidar:Daro_3783.
PATRICi21606254. VBIDecAro89105_3767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ48512.1.
RefSeqiWP_011289508.1. NC_007298.1.

3D structure databases

ProteinModelPortaliQ479G9.
SMRiQ479G9. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi159087.Daro_3783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ48512; AAZ48512; Daro_3783.
KEGGidar:Daro_3783.
PATRICi21606254. VBIDecAro89105_3767.

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
OMAiQRSEWLE.
OrthoDBiEOG6H1PXH.

Enzyme and pathway databases

BioCyciDARO159087:GI5B-3861-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. "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
    Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
    BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RCB.

Entry informationi

Entry nameiACDH4_DECAR
AccessioniPrimary (citable) accession number: Q479G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: September 13, 2005
Last modified: July 22, 2015
This is version 65 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.