A0A1P8RA13 · A0A1P8RA13_9EURY
- ProteinShikimate dehydrogenase (NADP(+))
- GenearoE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids267 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic activity
- shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14-16 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: SLS | ||||||
Binding site | 61 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 65 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 76 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 85 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 101 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 125-129 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GAGGA | ||||||
Binding site | 211 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 213 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 234 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 241 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NADP binding | |
Molecular Function | shikimate 3-dehydrogenase (NADP+) activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process | |
Biological Process | shikimate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameShikimate dehydrogenase (NADP(+))
- EC number
- Short namesSDH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natronorubrum
Accessions
- Primary accessionA0A1P8RA13
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-87 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LLGNPVGHSLSPPLHEAAYDELGLEARYVTFEPEPEAIDAAVEGADALGITGLNVTIPFKRDVLECVEADELATRIGAVNTI | ||||||
Domain | 115-187 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: TLADARAVVVGAGGAGRAIAFGLADAGATVDVANRTESTAHDLADEVPNATGYGLDSLERIVADADVLVNATS | ||||||
Domain | 234-264 | SDH C-terminal | ||||
Sequence: GAWMLLYQGVEALELWTGRDAPVDAMNEALR |
Sequence similarities
Belongs to the shikimate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length267
- Mass (Da)27,739
- Last updated2017-04-12 v1
- ChecksumAC415D71EAF8EA6F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP019327 EMBL· GenBank· DDBJ | APX95530.1 EMBL· GenBank· DDBJ | Genomic DNA |