S4Y1T5 · S4Y1T5_SORCE
- ProteinMultifunctional fusion protein
- GenearoK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids536 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic activity
- 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Cofactor
Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Binds 1 divalent metal cation per subunit. Can use either Co2+ or Zn2+.
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17-22 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTGKST | ||||||
Binding site | 21 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 39 | substrate | ||||
Sequence: D | ||||||
Binding site | 63 | substrate | ||||
Sequence: R | ||||||
Binding site | 86 | substrate | ||||
Sequence: G | ||||||
Binding site | 123 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 143 | substrate | ||||
Sequence: R | ||||||
Binding site | 279-283 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GVVTD | ||||||
Binding site | 303-304 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 316 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 325 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 358 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 421 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 438 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-dehydroquinate synthase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | shikimate kinase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameShikimate kinase
- EC number
- Short namesSK
- Recommended name3-dehydroquinate synthase
- EC number
- Short namesDHQS
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Myxococcota > Polyangia > Polyangiales > Polyangiaceae > Sorangium
Accessions
- Primary accessionS4Y1T5
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 242-498 | 3-dehydroquinate synthase | ||||
Sequence: VLTPGEEHKRLAAVEAALTAMLDAGADRDAVVLAHGGGVVTDIGGFAASTLLRGVRWVAAPTTLLSMVDASVGGKTGVDLGPAKNAVGTFHQPSAVVASPAALATETDRAFRSGLAEVVKSACIADPELHALLEREADRVLARDPGLLAELIRRSIAVKAAIVARDERESGDRALLNFGHTLGHALEAEGGFVRLAHGEAVSLGMVAMLRVGCSLGVTDRAAADRVVRLLARLGLPTRIEDEPVSAALRFLSLDKKR |
Sequence similarities
Belongs to the shikimate kinase family.
Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length536
- Mass (Da)55,096
- Last updated2013-10-16 v1
- ChecksumFA68A928C8D7FACA
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003969 EMBL· GenBank· DDBJ | AGP38135.1 EMBL· GenBank· DDBJ | Genomic DNA |