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Protein

Acetaldehyde dehydrogenase

Gene

Reut_B5824

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
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 sitei133 – 1331Acyl-thioester intermediateUniRule annotation
Binding sitei291 – 2911NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 164NADUniRule annotation
Nucleotide bindingi164 – 1729NADUniRule 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

BioCyciCPIN264198:GIW3-5910-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:Reut_B5824
OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Taxonomic identifieri264198 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002697: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Acetaldehyde dehydrogenasePRO_0000337984Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi264198.Reut_B5824.

Structurei

3D structure databases

ProteinModelPortaliQ46NW7.
SMRiQ46NW7. Positions 4-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OMAiTSAGAHR.
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.

Q46NW7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATRKLKAAI IGSGNIGTDL MIKILRHGKH LEMGAMVGID PASDGLARAA
60 70 80 90 100
RMGVATTHEG VEGLISLPNF ADIDVVFDAT SAGAHVKNDA RLREVKPGIR
110 120 130 140 150
MIDLTPAAIG PYCVPVVNLD DRLDALNVNM VTCGGQATIP MVAAVSRVAK
160 170 180 190 200
VHYAEIVASI SSKSAGPGTR ANIDEFTETT SKAIEVIGGA AKGKAIIVLN
210 220 230 240 250
PAEPPLIMRD TVYVLSAAAN RAEVEASIEE MAAAVQQYVP GYRLKQKVQF
260 270 280 290 300
DEIPASAPLN IPGLGKFSGL KTSVFLEVEG AAHYLPAYAG NLDIMTSAAL
310
ATAERMAQAA LTA
Length:313
Mass (Da):32,655
Last modified:September 13, 2005 - v1
Checksum:i2BF10617F942ED0F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000091 Genomic DNA. Translation: AAZ65167.1.
RefSeqiYP_300011.1. NC_007348.1.

Genome annotation databases

EnsemblBacteriaiAAZ65167; AAZ65167; Reut_B5824.
GeneIDi3614066.
KEGGireu:Reut_B5824.
PATRICi20237633. VBIRalEut24049_6607.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000091 Genomic DNA. Translation: AAZ65167.1.
RefSeqiYP_300011.1. NC_007348.1.

3D structure databases

ProteinModelPortaliQ46NW7.
SMRiQ46NW7. Positions 4-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264198.Reut_B5824.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ65167; AAZ65167; Reut_B5824.
GeneIDi3614066.
KEGGireu:Reut_B5824.
PATRICi20237633. VBIRalEut24049_6607.

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OMAiTSAGAHR.
OrthoDBiEOG6H1PXH.

Enzyme and pathway databases

BioCyciCPIN264198:GIW3-5910-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 2 of Ralstonia eutropha JMP134."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JMP134 / LMG 1197.

Entry informationi

Entry nameiACDH_CUPPJ
AccessioniPrimary (citable) accession number: Q46NW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: September 13, 2005
Last modified: February 4, 2015
This is version 67 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

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.