Skip Header

Contribute Send feedback
Read comments (?) or add your own

A4JPX8 (ACDH1_BURVG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. 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
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:Bcep1808_5385
OrganismBurkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) [Complete proteome] [HAMAP]
Taxonomic identifier269482 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length315 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 MF_01657

Catalytic activity

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. HAMAP 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-KW

cellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

acetaldehyde dehydrogenase (acetylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Acetaldehyde dehydrogenase 1 HAMAP MF_01657
PRO_0000337976

Regions

Nucleotide binding15 – 184NAD By similarity
Nucleotide binding166 – 1749NAD By similarity

Sites

Binding site2931NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A4JPX8 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 8195AFD83A71D876

FASTA31532,679
        10         20         30         40         50         60 
MATDNTRCKA AIIGSGNIGT DLMIKIMRSG KHLEIAAMVG IDPASDGLAR AARLGVATTH 

        70         80         90        100        110        120 
EGVEGLARLP VFDEIDFVFD ATSAGAHVKN DAFLRALKPG IRMIDLTPAA IGPYCVPVVN 

       130        140        150        160        170        180 
LDAHLDAPNV NMVTCGGQAT IPMVAAVSRV AKVHYAEIVA SISSKSAGPG TRANIDEFTE 

       190        200        210        220        230        240 
TTSKALEAVG GAGKGKAIIV LNPAEPPLMM RDTVYLLSEA ADRALIEASV SEMAAAVQAY 

       250        260        270        280        290        300 
VPGYRLKQSV QFDDIPAAAP LHIPGLGRFS GLKTSIFVEV EGAAHYLPAY AGNLDIMTSA 

       310 
ALATAERMAA SLVNA

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G4 / LMG 22486.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000615 Genomic DNA. Translation: ABO58331.1.
RefSeqYP_001117796.1. NC_009255.1.

3D structure databases

ProteinModelPortalA4JPX8.
SMRA4JPX8. Positions 5-315.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4JPX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4951603.
GenomeReviewsGene locus Bcep1808_5385 in contig CP000615_GR.
KEGGbvi:Bcep1808_5385.
PATRIC19318236. VBIBurVie89221_4132.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHBG300125.
OMAHVKNDAF.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycBVIE269482:BCEP1808_5385-MONOMER.

Family and domain databases

HAMAPMF_01657. Ac_ald_DH_ac.
[Tree]
InterProIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK04073.
PANTHERPTHR21123. Acetylald_dh. 1 hit.
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_BURVG
AccessionPrimary (citable) accession number: A4JPX8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 1, 2007
Last modified: December 14, 2011
This is version 42 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents