Reviewed,
UniProtKB/Swiss-Prot A7ZLN7 (ABDH_ECO24)
Last modified
November 3, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Gamma-aminobutyraldehyde dehydrogenase EC=1.2.1.19 Alternative name(s): 1-pyrroline dehydrogenase 4-aminobutanal dehydrogenase Short name=ABALDH | ||||
| 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 | 474 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4-aminobutanoate (GABA) By similarity. |
| Catalytic activity | 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH. HAMAP MF_01275 |
| Pathway | Amine and polyamine degradation; putrescine degradation; 4-aminobutanoate from 4-aminobutanal: step 1/1. HAMAP MF_01275 |
| Subunit structure | Homotetramer By similarity. |
| Miscellaneous | 4-aminobutanal is also called gamma-aminobutyraldehyde. HAMAP MF_01275 |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW putrescine catabolic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: HAMAP aminobutyraldehyde dehydrogenase activityInferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptorInferred 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 – 474 | 474 | Gamma-aminobutyraldehyde dehydrogenase HAMAP MF_01275 | PRO_1000067391 | |||||
Regions | |||||||||
| Nucleotide binding | 172 – 175 | 4 | NAD By similarity | ||||||
| Nucleotide binding | 225 – 231 | 7 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 246 | 1 | By similarity | ||||||
| Active site | 280 | 1 | Nucleophile By similarity | ||||||
| Binding site | 146 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 209 | 1 | NAD By similarity | ||||||
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: ABV19711.1. | |
| RefSeq | YP_001462716.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7ZLN7. |
Genome annotation databases | |
| GeneID | 5586995. |
| GenomeReviews | Gene locus EcE24377A_1624 in contig CP000800_GR. |
| KEGG | ecw:EcE24377A_1624. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | GYYFQPT. |
Family and domain databases | |
| HAMAP | MF_01275. [Tree] |
| InterPro | IPR017749. 1-pyrroline_dehydrogenase. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [Graphical view] |
| Gene3D | G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| PANTHER | PTHR11699. Aldehyde_dehyd. 1 hit. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03374. ABALDH. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ABDH_ECO24 | ||||||||
| Accession | Primary (citable) accession number: A7ZLN7 | ||||||||
| 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 |

Clusters with


