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Q8X5J9 (ACDH_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. 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:Z0450, ECs0406
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_0000337980

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
Q8X5J9 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 6709FAC7425DFFB5

FASTA31633,587
        10         20         30         40         50         60 
MSKRKVAIIG SGNIGTDLMI KILRHDQHLE MAVMVGIDPQ SDGLARARRM GVATTHEGVI 

        70         80         90        100        110        120 
GLMNMPEFAD IDIVFDATSA GAHVKNDAAL REAKPDIRLI DLTPAAIGPY CVPVVNLEEN 

       130        140        150        160        170        180 
VDQLNVNMVT CGGQATIPMV AAVSRVVRVH YAEIIASIAS KSAGPGTRAN IDEFTETTSR 

       190        200        210        220        230        240 
AIEVVGGAAK GKAIIVLNPA EPPLMMRDTV YVLSDEASQD DIEASINEMA EAVQAYVPGY 

       250        260        270        280        290        300 
RLKQRVQFEV IPQDKPVNLP GVGQFSGLKT AVWLEVEGAA HYLPAYAGNL DIMTSSALAT 

       310 
AEKMAQSLAR KAGEAA 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG54702.1.
BA000007 Genomic DNA. Translation: BAB33829.1.
PIRB85530.
F90679.
RefSeqNP_286094.1. NC_002655.2.
NP_308433.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X5J9.
SMRQ8X5J9. Positions 3-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0450.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG54702; AAG54702; Z0450.
BAB33829; BAB33829; BAB33829.
GeneID914508.
957291.
KEGGece:Z0450.
ecs:ECs0406.
PATRIC18349759. VBIEscCol44059_0400.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAHQGNVNM.
OrthoDBEOG6H1PXH.

Enzyme and pathway databases

BioCycECOL386585:GJFA-400-MONOMER.
ECOO157:MHPF-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_ECO57
AccessionPrimary (citable) accession number: Q8X5J9
Secondary accession number(s): Q7AH50
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 85 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