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Q1LNS3 (ACDH1_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetaldehyde dehydrogenase 1

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 1
Gene names
Ordered Locus Names:Rmet_1320
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01657

Catalytic activity

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. HAMAP-Rule MF_01657

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

acetaldehyde dehydrogenase (acetylating) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Acetaldehyde dehydrogenase 1 HAMAP-Rule MF_01657
PRO_0000387714

Regions

Nucleotide binding161 – 1699NAD By similarity

Sites

Active site1301Acyl-thioester intermediate By similarity
Binding site2721NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LNS3 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: EF590C5280B84A9F

FASTA30332,332
        10         20         30         40         50         60 
MKKIKCALIG PGNIGTDLLA KLKRSSVLEP VWMVGIDPES EGLNRARELG IKTTAEGVDG 

        70         80         90        100        110        120 
LLPHVLADGV QIAFDATSAY VHAENARKLN ALGVMMIDLT PAAIGPYCVP PVNLKEHLGK 

       130        140        150        160        170        180 
REMNVNMVTC GGQATIPMVA AVSRVQPVAY GEIVATVSSR SVGPGTRKNI DEFTRTTAGA 

       190        200        210        220        230        240 
VEKVGGARKG KAIIIINPAE PPLMMRDTIH CLTETEPDQQ RIAESIHAMI EEVQKYVPGY 

       250        260        270        280        290        300 
RLVNGPVFDG KRVTVFMEVA GLGDYLPTYA GNLDIMTAAA ARTAEMFAEE MIAGNLTLEP 


VVA 

« Hide

References

[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000352 Genomic DNA. Translation: ABF08203.1.
RefSeqYP_583472.1. NC_007973.1.

3D structure databases

ProteinModelPortalQ1LNS3.
SMRQ1LNS3. Positions 2-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266264.Rmet_1320.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF08203; ABF08203; Rmet_1320.
GeneID4038123.
KEGGrme:Rmet_1320.
PATRIC20287248. VBIRalMet4734_1726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAQRSEWLE.
OrthoDBEOG6H1PXH.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycCMET266264:GJ5G-1381-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01657. Ac_ald_DH_ac.
InterProIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACDH1_RALME
AccessionPrimary (citable) accession number: Q1LNS3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families