Q8FCR6 (DHAS_ECOL6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 67.
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: Aspartate-semialdehyde dehydrogenase Short name=ASA dehydrogenase Short name=ASADH EC=1.2.1.11 Alternative name(s): Aspartate-beta-semialdehyde dehydrogenase | ||||
| Gene names |
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| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 367 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate By similarity. HAMAP MF_02121 |
| Catalytic activity | L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. HAMAP MF_02121 |
| Pathway | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. HAMAP MF_02121 Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. HAMAP MF_02121 Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. HAMAP MF_02121 |
| Subunit structure | Homodimer By similarity. HAMAP MF_02121 |
| Sequence similarities | Belongs to the aspartate-semialdehyde dehydrogenase family. |
| Sequence caution | The sequence AAN82658.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 367 | 367 | Aspartate-semialdehyde dehydrogenase HAMAP MF_02121 | PRO_0000141371 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 13 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 37 – 38 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 165 – 166 | 2 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 135 | 1 | Acyl-thioester intermediate By similarity | ||||||
| Active site | 274 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 73 | 1 | NADP By similarity | ||||||
| Binding site | 102 | 1 | Phosphate By similarity | ||||||
| Binding site | 162 | 1 | Substrate By similarity | ||||||
| Binding site | 193 | 1 | NADP; via carbonyl oxygen By similarity | ||||||
| Binding site | 241 | 1 | Substrate By similarity | ||||||
| Binding site | 244 | 1 | Phosphate By similarity | ||||||
| Binding site | 267 | 1 | Substrate By similarity | ||||||
| Binding site | 350 | 1 | NADP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 135 | 1 | S-cysteinyl cysteine; in inhibited form By similarity | ||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN82658.1. Different initiation. |
| RefSeq | NP_756084.2. NC_004431.1. |
3D structure databases | |
| ProteinModelPortal | Q8FCR6. |
| SMR | Q8FCR6. Positions 1-367. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000040842; EBESCP00000039191; EBESCG00000039892. |
| GeneID | 1036947. |
| GenomeReviews | Gene locus c4220 in contig AE014075_GR. |
| KEGG | ecc:c4220. |
| PATRIC | 18286186. VBIEscCol75197_3969. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000010426. |
| HOGENOM | HBG289760. |
| OMA | IDGLCVR. |
| ProtClustDB | PRK06598. |
Family and domain databases | |
| HAMAP | MF_02121. ASADH. [Tree] |
| InterPro | IPR000319. Asp-semialdehyde_DH_CS. IPR011534. Asp_ADH_gamma-type. IPR012080. Asp_semialdehyde_DH. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00133. |
| Pfam | PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view] |
| PIRSF | PIRSF000148. ASA_dh. 1 hit. |
| SMART | SM00859. Semialdhyde_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01745. Asd_gamma. 1 hit. |
| PROSITE | PS01103. ASD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHAS_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: Q8FCR6 | ||||||||
| 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 |

Clusters with