Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B5XQJ3 (ACDH_KLEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Name:mhpF
Ordered Locus Names:KPK_2205
OrganismKlebsiella pneumoniae (strain 342) [Complete proteome] [HAMAP]
Taxonomic identifier507522 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length316 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

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01657

Subunit structure

Interacts with MhpE By similarity. 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_process3-phenylpropionate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 316316Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_1000187037

Regions

Nucleotide binding11 – 144NAD By similarity
Nucleotide binding162 – 1709NAD By similarity

Sites

Active site1311Acyl-thioester intermediate By similarity
Binding site2891NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B5XQJ3 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 62F323FDC2838496

FASTA31632,861
        10         20         30         40         50         60 
MRKRKVAIIG SGNIGTDLMI KILRHGQHLE MAVMVGIDPQ SDGLARARRM GVATTHEGVG 

        70         80         90        100        110        120 
GLMQMAEFAD IDFVFDATSA GAHIKNDAAL REAKPGIRVI DLTPAAIGPY CVPVVNLAAN 

       130        140        150        160        170        180 
LHQGNVNMVT CGGQATIPMV AAVSRVAKVH YAEIVASIAS QSAGPGTRAN IDEFTETTSQ 

       190        200        210        220        230        240 
AIEKVGGAGK GKAIIVLNPA EPPLMMRDTV YVLSELASQE AIAASIAEMA AAVQAYVPGY 

       250        260        270        280        290        300 
RLKQQVQFEV IPEDKPVNLP GIGCFSGLKT AVYLEVEGAA HYLPAYAGNL DIMTSAALAT 

       310 
AEQMAGAMHS AAGATA 

« Hide

References

[1]"Complete genome sequence of the N2-fixing broad host range endophyte Klebsiella pneumoniae 342 and virulence predictions verified in mice."
Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., Methe B.A.
PLoS Genet. 4:E1000141-E1000141(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 342.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000964 Genomic DNA. Translation: ACI11884.1.
RefSeqYP_002238041.1. NC_011283.1.

3D structure databases

ProteinModelPortalB5XQJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING507522.KPK_2205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI11884; ACI11884; KPK_2205.
GeneID6938949.
KEGGkpe:KPK_2205.
PATRIC20437866. VBIKlePne121904_2309.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAHLKHAPL.
OrthoDBEOG6H1PXH.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycKPNE507522:GI0B-2206-MONOMER.
UniPathwayUPA00714.

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_KLEP3
AccessionPrimary (citable) accession number: B5XQJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 25, 2008
Last modified: February 19, 2014
This is version 43 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

PATHWAY comments

Index of metabolic and biosynthesis pathways