A0A8K0V2S5 · A0A8K0V2S5_9ENTR
- ProteinBifunctional chorismate mutase/prephenate dehydratase
- GenepheA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids385 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
function
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic activity
- H+ + prephenate = 3-phenylpyruvate + CO2 + H2O
Pathway
Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10 | substrate | ||||
Sequence: R | ||||||
Binding site | 27 | substrate | ||||
Sequence: R | ||||||
Binding site | 38 | substrate | ||||
Sequence: K | ||||||
Binding site | 47 | substrate | ||||
Sequence: D | ||||||
Binding site | 51 | substrate | ||||
Sequence: E | ||||||
Binding site | 83 | substrate | ||||
Sequence: S | ||||||
Binding site | 87 | substrate | ||||
Sequence: Q | ||||||
Site | 277 | Essential for prephenate dehydratase activity | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | chorismate mutase activity | |
Molecular Function | prephenate dehydratase activity | |
Biological Process | chorismate metabolic process | |
Biological Process | L-phenylalanine biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional chorismate mutase/prephenate dehydratase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Tenebrionibacter/Tenebrionicola group > Tenebrionibacter
Accessions
- Primary accessionA0A8K0V2S5
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-91 | Chorismate mutase | ||||
Sequence: MSDNPLLALRDKISALDEKLLALLAERRQLAVDVGTAKLATHRPVRDIDRERDLLEHLVRIGQKHHLDGHYITRLFQLIIEDSVLTQQALL | ||||||
Domain | 104-284 | Prephenate dehydratase | ||||
Sequence: RIAFLGPKGSYSHLAARRYAARHFEHFIESGCARFEEIFRQVETGQADYAIVPAENTSSGSINDVYDLLQHTSLSIVSELTLPIDHCVMVATTTTLEKIKTVYSHPQPFQQCSQFVNRWPQWKIEYCESTSAAMEKVAQSGSSDAAALGSEAGGALYGLQVLERNLANQTQNITRFLVLAR | ||||||
Domain | 298-375 | ACT | ||||
Sequence: TLLFATGQQSGALVEALLVMRNHNLIMTKLESRPIHGNPWEEMFYLDIQANLESADMRQALRELGEITRSMKVLGCYP |
Family and domain databases
Sequence
- Sequence statusComplete
- Length385
- Mass (Da)42,895
- Last updated2022-08-03 v1
- Checksum9E1F1BCC6A1CF743
Keywords
- Technical term