Reviewed,
UniProtKB/Swiss-Prot A7ZI98 (MHPF_ECO24)
Last modified
November 25, 2008.
Version 11.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetaldehyde dehydrogenase EC=1.2.1.10 Alternative name(s): Acetaldehyde dehydrogenase [acetylating] | ||||
| Gene names |
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| Organism | Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 331111 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 316 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the terminal reaction in meta-cleavage pathways, that is, the transformation of acetaldehyde into acetyl coenzyme A By similarity. |
| Catalytic activity | Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH. |
| Pathway | Aromatic compound metabolism; 3-phenylpropionic acid degradation. |
| Subunit structure | Interacts with mhpE By similarity. |
| Sequence similarities | Belongs to the acetaldehyde dehydrogenase family. MhpF subfamily. |
Ontologies
Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | amino acid metabolic process Inferred from electronic annotation. Source: InterPro aromatic compound catabolic processInferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro acetaldehyde dehydrogenase (acetylating) activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 316 | 316 | Acetaldehyde dehydrogenase | PRO_0000337979 | |||
Sequences
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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 | |
|---|---|
| CP000800 Genomic DNA. Translation: ABV17887.1. | |
| RefSeq | YP_001461527.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5586084. |
| GenomeReviews | Gene locus EcE24377A_0375 in contig CP000800_GR. |
| KEGG | ecw:EcE24377A_0375. |
Organism-specific databases | |
| CMR | Search... |
Family and domain databases | |
| HAMAP | MF_01657. [Tree] |
| InterPro | IPR003361. Acetylald_dehydrogenase. IPR015426. Acetylald_DHase_C. IPR000534. Semialdehyde_DHase_NAD-bd. [Graphical view] |
| PANTHER | PTHR21123. Acetylald_dh. 1 hit. |
| Pfam | PF09290. AcetDehyd-dimer. 1 hit. PF01118. Semialdhyde_dh. 1 hit. [Graphical view] |
| PIRSF | PIRSF015689. Actaldh_dh_actl. 1 hit. |
| TIGRFAMs | TIGR03215. ac_ald_DH_ac. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MHPF_ECO24 | ||||||||
| Accession | Primary (citable) accession number: A7ZI98 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

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