Q9S400 · AROA_STRPN
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids427 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic activity
- 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Competitively inhibited by glyphosate. Activated by ammonium, rubidium or potassium ions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
22 μM | PEP | 7 | 25 | with 100 mM ammonium | ||
31 μM | S3P | 7 | 25 | with 100 mM ammonium | ||
91 μM | PEP | 7 | 25 | with 10 mM ammonium | ||
100 μM | PEP | 7 | 25 | with 1 mM ammonium | ||
118 μM | S3P | 7 | 25 | with 10 mM ammonium | ||
145 μM | S3P | 7 | 25 | with 1 mM ammonium |
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 20 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 21 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 25 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 92 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 120 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 166 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 167 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 168 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 168 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 312 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 312 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 339 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 343 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 385 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-phosphoshikimate 1-carboxyvinyltransferase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-phosphoshikimate 1-carboxyvinyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionQ9S400
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000088304 | 1-427 | 3-phosphoshikimate 1-carboxyvinyltransferase | |||
Sequence: MKLKTNIRHLHGSIRVPGDKSISHRSIIFGSLAEGETKVYDILRGEDVLSTMQVFRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNMGNSGTSIRLISGVLAGADFEVEMFGDDSLSKRPMDRVTLPLKKMGVSISGQTERDLPPLRLKGTKNLRPIHYELPIASAQVKSALMFAALQAKGESVIIEKEYTRNHTEDMLKQFGGHLSVDGKKITVQGPQKLTGQKVVVPGDISSAAFWLVAGLIAPNSRLVLQNVGINETRTGIIDVIRAMGGKLEITEIDPVAKSATLIVESSDLKGTEIGGALIPRLIDELPIIALLATQAQGVTVIKDAEELKVKETDRIQVVADALNSMGADITPTADGMIIKGKSALHGARVNTFGDHRIGMMTAIAALLVADGEVELDRAEAINTSYPSFFDDLESLIHG |
Proteomic databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9S400 | eno Q97QS2 | 2 | EBI-2207276, EBI-2207206 | |
BINARY | Q9S400 | gatC Q97SE5 | 2 | EBI-2207276, EBI-2207053 | |
BINARY | Q9S400 | groES Q97NV3 | 2 | EBI-2207276, EBI-2206949 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length427
- Mass (Da)45,766
- Last updated2001-09-26 v2
- Checksum45CE6F4D0D1C7B70
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 13 | in Ref. 1; AAD45819 | ||||
Sequence: S → I | ||||||
Sequence conflict | 71 | in Ref. 1; AAD45819 | ||||
Sequence: I → V | ||||||
Sequence conflict | 201 | in Ref. 1; AAD45819 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 303 | in Ref. 1; AAD45819 | ||||
Sequence: G → C |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF169483 EMBL· GenBank· DDBJ | AAD45819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE005672 EMBL· GenBank· DDBJ | AAK75469.1 EMBL· GenBank· DDBJ | Genomic DNA |