Q55512 (DHAS_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 76.
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 |
| ||||
| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) | ||||
| Taxonomic identifier | 1111708 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Synechocystis |
Protein attributes
| Sequence length | 338 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 BAA10869.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 338 | 338 | Aspartate-semialdehyde dehydrogenase HAMAP MF_02121 | PRO_0000141393 | |||||
Regions | |||||||||
| Nucleotide binding | 13 – 16 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 41 – 42 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 160 – 161 | 2 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 130 | 1 | Acyl-thioester intermediate By similarity | ||||||
| Active site | 243 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 101 | 1 | Phosphate By similarity | ||||||
| Binding site | 157 | 1 | Substrate By similarity | ||||||
| Binding site | 214 | 1 | Phosphate By similarity | ||||||
| Binding site | 236 | 1 | Substrate By similarity | ||||||
| Binding site | 316 | 1 | NADP By similarity | ||||||
Sequences
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References
| [1] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000022 Genomic DNA. Translation: BAA10869.1. Different initiation. |
| PIR | S76022. |
| RefSeq | NP_442798.2. NC_000911.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q55512. 2 interactions. |
| STRING | Q55512. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 952082. |
| GenomeReviews | Gene locus slr0549 in contig BA000022_GR. |
| KEGG | syn:slr0549. |
| NMPDR | fig|1148.1.peg.2899. |
Phylogenomic databases | |
| eggNOG | COG0136. |
| HOGENOM | HBG518238. |
| OMA | LELWLCG. |
| PhylomeDB | Q55512. |
Enzyme and pathway databases | |
| BioCyc | SSP1148:SLR0549-MONOMER. |
Family and domain databases | |
| HAMAP | MF_02121. ASADH. [Tree] |
| InterPro | 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHAS_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: Q55512 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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