Reviewed,
UniProtKB/Swiss-Prot Q8ZPC9 (ABDH_SALTY)
Last modified
June 16, 2009.
Version 46.
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 | Salmonella typhimurium [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 90371 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
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_0000269700 | |||||
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] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
Cross-references
Sequence databases | |
|---|---|
| AE008770 Genomic DNA. Translation: AAL20515.1. Different initiation. | |
| RefSeq | NP_460556.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1O02 based on UniProtKB P05091. |
| SMR | Q8ZPC9. Positions 1-474. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1253115. |
| GenomeReviews | Gene locus STM1597 in contig AE006468_GR. |
| KEGG | stm:STM1597. |
| NMPDR | fig|99287.1.peg.1546. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8ZPC9. |
Enzyme and pathway databases | |
| BioCyc | STYP99287:STM1597-MON. |
| BRENDA | 1.2.1.19. 2. |
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_SALTY | ||||||||
| Accession | Primary (citable) accession number: Q8ZPC9 | ||||||||
| 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


