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Reviewed, UniProtKB/Swiss-Prot A7ZI98 (ACDH_ECO24)

Last modified February 9, 2010. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: EcE24377A_0375
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [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 MF_01657

Catalytic activity

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

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01657

Subunit structure

Interacts with mhpE By similarity. HAMAP MF_01657

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Acetaldehyde dehydrogenase HAMAP MF_01657
PRO_0000337979

Sequences

Sequence LengthMass (Da)Tools
A7ZI98-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: A6918BDA5EF4876B

FASTA31633,442
        10         20         30         40         50         60 
MSKRKVAIIG SGNIGTDLMI KILRHGQHLE MAVMVGIDPQ SDGLARARRM GVATTHEGVI 

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

       130        140        150        160        170        180 
VDQLNVNMVT CGGQATIPMV AAVSRVARVH 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]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV17887.1.
RefSeqYP_001461527.1.

3D structure databases

SMRA7ZI98. Positions 3-308.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZI98.

Genome annotation databases

GeneID5586084.
GenomeReviewsGene locus EcE24377A_0375 in contig CP000800_GR.
KEGGecw:EcE24377A_0375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHBG300125.
OMAHVKNDAF.

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]
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 nameACDH_ECO24
AccessionPrimary (citable) accession number: A7ZI98
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 23, 2007
Last modified: February 9, 2010
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents