B1LFH3 (ABDH_ECOSM) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 31.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 439855 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 474 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_01275 |
| 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. HAMAP MF_01275 |
| 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 | putrescine catabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | 1-pyrroline dehydrogenase activity Inferred from electronic annotation. Source: EC NAD bindingInferred from electronic annotation. Source: InterPro aminobutyraldehyde dehydrogenase activityInferred from electronic annotation. Source: EC |
| 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_1000140274 | |||||
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] | "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5." Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R. J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SMS-3-5 / SECEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000970 Genomic DNA. Translation: ACB17411.1. |
| RefSeq | YP_001743784.1. NC_010498.1. |
3D structure databases | |
| ProteinModelPortal | B1LFH3. |
| SMR | B1LFH3. Positions 1-474. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B1LFH3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000061341; EBESCP00000058983; EBESCG00000060388. |
| GeneID | 6146236. |
| GenomeReviews | Gene locus EcSMS35_1729 in contig CP000970_GR. |
| KEGG | ecm:EcSMS35_1729. |
| PATRIC | 18432323. VBIEscCol6161_1884. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009175. |
| HOGENOM | HBG752218. |
| OMA | CRIYAQQ. |
| ProtClustDB | PRK13473. |
Enzyme and pathway databases | |
| BioCyc | ECOL439855:ECSMS35_1729-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01275. Aldedh_Prr. [Tree] |
| InterPro | IPR017749. 1-pyrroline_dehydrogenase. IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| KO | K00137. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| 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_ECOSM | ||||||||
| Accession | Primary (citable) accession number: B1LFH3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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