P0A543 (DHAS_MYCBO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
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 | Mycobacterium bovis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1765 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 345 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 Z18290 differs from that shown. Reason: Frameshift at position 313. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 345 | 345 | Aspartate-semialdehyde dehydrogenase HAMAP MF_02121 | PRO_0000141381 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 14 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 39 – 40 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 160 – 161 | 2 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 130 | 1 | Acyl-thioester intermediate By similarity | ||||||
| Active site | 256 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 99 | 1 | Phosphate By similarity | ||||||
| Binding site | 157 | 1 | Substrate By similarity | ||||||
| Binding site | 227 | 1 | Phosphate By similarity | ||||||
| Binding site | 249 | 1 | Substrate By similarity | ||||||
| Binding site | 325 | 1 | NADP By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria." Cirillo J.D., Weisbrod T.R., Pascopella L., Bloom B.R., Jacobs W.R. Jr. Mol. Microbiol. 11:629-639(1994) [PubMed: 7910936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BCG / Pasteur. |
| [2] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z18290 Genomic DNA. No translation available. BX248347 Genomic DNA. Translation: CAD95921.1. |
| RefSeq | NP_857373.1. NC_002945.3. |
3D structure databases | |
| ProteinModelPortal | P0A543. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000014467; EBMYCP00000014302; EBMYCG00000014465. |
| GeneID | 1093103. |
| GenomeReviews | Gene locus Mb3735c in contig BX248333_GR. |
| KEGG | mbo:Mb3735c. |
| PATRIC | 18009926. VBIMycBov88188_4088. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000017367. |
| HOGENOM | HBG518238. |
| OMA | LELWLCG. |
| ProtClustDB | PRK14874. |
Enzyme and pathway databases | |
| BioCyc | MBOV233413:MB3735C-MONOMER. |
Family and domain databases | |
| HAMAP | MF_02121. ASADH. [Tree] |
| InterPro | IPR000319. Asp-semialdehyde_DH_CS. IPR012080. Asp_semialdehyde_DH. IPR005986. Asp_semialdehyde_DH_beta. 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 | TIGR01296. Asd_B. 1 hit. |
| PROSITE | PS01103. ASD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHAS_MYCBO | ||||||||
| Accession | Primary (citable) accession number: P0A543 Secondary accession number(s): P47730, P97049 | ||||||||
| 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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