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Q120P0 (ACDH_POLSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]
Gene names
Ordered Locus Names:Bpro_5135
Encoded onPlasmid pPOLSJ1
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length314 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
Plasmid
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 – 314314Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000387704

Regions

Nucleotide binding14 – 174NAD By similarity
Nucleotide binding163 – 1719NAD By similarity

Sites

Active site1321Acyl-thioester intermediate By similarity
Binding site2911NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q120P0 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 7394F6A96D63FA43

FASTA31432,808
        10         20         30         40         50         60 
MTKSQRLQVA IIGSGNIGTD LMIKVMRNSK HLSMGAMVGI DAASDGLARA GRLGVPVTHE 

        70         80         90        100        110        120 
GITGLVGLPN FGDIRIAFDA TSAGAHAGHN EVLQRHGVKV IDLTPAAIGP YVIPVVNLEE 

       130        140        150        160        170        180 
QLSSPNINMV TCGGQATIPI VRAVSQIARV RYAEIVASIA SKSAGPGTRA NIDEFTETTS 

       190        200        210        220        230        240 
AAIVSVGRAE HGKAIIVLNP AEPSLMMRDT VFCLVDADAD QEAIRLSVRD MVRSVAAYVP 

       250        260        270        280        290        300 
GYRLKQDVQF DVIPDKAPVN VPGIGRVSGL KVSVFLEVEG AAHYLPAYAG NLDIMTSAAL 

       310 
AAADKIAASL ITAR 

« Hide

References

[1]"Complete sequence of plasmid 1 of Polaromonas sp. JS666."
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., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000317 Genomic DNA. Translation: ABE47002.1.
RefSeqYP_551900.1. NC_007949.1.

3D structure databases

ProteinModelPortalQ120P0.
SMRQ120P0. Positions 4-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING296591.Bpro_5135.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE47002; ABE47002; Bpro_5135.
GeneID4016057.
KEGGpol:Bpro_5135.
PATRIC22963511. VBIPolSp102244_5200.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAHARHEQL.
OrthoDBEOG6H1PXH.

Enzyme and pathway databases

BioCycPSP296591:GHI4-550-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 nameACDH_POLSJ
AccessionPrimary (citable) accession number: Q120P0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 59 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