Q6GZ04 · PAM_TAXCA
- ProteinPhenylalanine aminomutase (L-beta-phenylalanine forming)
- Genepam
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids698 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Also has low phenylalanine ammonia-lyase activity.
Catalytic activity
- L-phenylalanine = L-beta-phenylalanine
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.057 mM | L-phenylalanine |
kcat is 0.053 sec-1 for L-phenylalanine.
Pathway
Alkaloid biosynthesis; taxol biosynthesis.
Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 80 | Proton donor/acceptor | ||||
Sequence: Y | ||||||
Binding site | 231 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 319 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 325 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 355 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 427 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 455 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 458 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | intramolecular aminotransferase activity | |
Molecular Function | phenylalanine ammonia-lyase activity | |
Biological Process | alkaloid biosynthetic process | |
Biological Process | cinnamic acid biosynthetic process | |
Biological Process | L-phenylalanine catabolic process | |
Biological Process | L-phenylalanine metabolic process | |
Biological Process | paclitaxel biosynthetic process | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhenylalanine aminomutase (L-beta-phenylalanine forming)
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Pinopsida > Pinidae > Conifers II > Cupressales > Taxaceae > Taxus
Accessions
- Primary accessionQ6GZ04
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 80 | Abolishes enzyme activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 104 | Decreases enzyme activity. | ||||
Sequence: L → A |
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000429969 | 1-698 | Phenylalanine aminomutase (L-beta-phenylalanine forming) | |||
Sequence: MGFAVESRSHVKDILGLINTFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAEQCRARVETCSSWVQRKAEDGADIYGVTTGFGACSSRRTNQLSELQESLIRCLLAGVFTKGCASSVDELPATATRSAMLLRLNSFTYGCSGIRWEVMEALEKLLNSNVSPKVPLRGSVSASGDLIPLAYIAGLLIGKPSVVARIGDDVEVPAPEALSRVGLRPFKLQAKEGLALVNGTSFATALASTVMYDANVLLLLVETLCGMFCEVIFGREEFAHPLIHKVKPHPGQIESAELLEWLLRSSPFQDLSREYYSIDKLKKPKQDRYALRSSPQWLAPLVQTIRDATTTVETEVNSANDNPIIDHANDRALHGANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGPDLSVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALISARKTEEALDILKLMIASHLTAMCQAVDLRQLEEALVKVVENVVSTLADECGLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLEQSCFGSILALHKKDGIETDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKKGHKTADNNDALVRIQGSRFLPFYRFVREELDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFLGQPNGCANGVESFQSVWNKSA | ||||||
Cross-link | 175↔177 | 5-imidazolinone (Ala-Gly) | ||||
Sequence: ASG | ||||||
Modified residue | 176 | 2,3-didehydroalanine (Ser) | ||||
Sequence: S |
Post-translational modification
Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length698
- Mass (Da)76,532
- Last updated2004-07-19 v1
- ChecksumBE106526C9AA891C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY582743 EMBL· GenBank· DDBJ | AAT47186.1 EMBL· GenBank· DDBJ | mRNA |