Q6GZ04 · PAM_TAXCA

  • Protein
    Phenylalanine aminomutase (L-beta-phenylalanine forming)
  • Gene
    pam
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.057 mML-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.

TypeIDPosition(s)Description
Active site80Proton donor/acceptor
Binding site231(E)-cinnamate (UniProtKB | ChEBI)
Binding site319(E)-cinnamate (UniProtKB | ChEBI)
Binding site325(E)-cinnamate (UniProtKB | ChEBI)
Binding site355(E)-cinnamate (UniProtKB | ChEBI)
Binding site427(E)-cinnamate (UniProtKB | ChEBI)
Binding site455(E)-cinnamate (UniProtKB | ChEBI)
Binding site458(E)-cinnamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionintramolecular aminotransferase activity
Molecular Functionphenylalanine ammonia-lyase activity
Biological Processalkaloid biosynthetic process
Biological Processcinnamic acid biosynthetic process
Biological ProcessL-phenylalanine catabolic process
Biological ProcessL-phenylalanine metabolic process
Biological Processpaclitaxel biosynthetic process
Biological Processprotein homotetramerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phenylalanine aminomutase (L-beta-phenylalanine forming)
  • EC number
  • Alternative names
    • Phenylalanine ammonia-lyase (EC:4.3.1.24
      ) . EC:4.3.1.24 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      pam

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Pinopsida > Pinidae > Conifers II > Cupressales > Taxaceae > Taxus

Accessions

  • Primary accession
    Q6GZ04

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis80Abolishes enzyme activity.
Mutagenesis104Decreases enzyme activity.

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004299691-698Phenylalanine aminomutase (L-beta-phenylalanine forming)
Cross-link175↔1775-imidazolinone (Ala-Gly)
Modified residue1762,3-didehydroalanine (Ser)

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.

Family & Domains

Sequence similarities

Belongs to the PAL/histidase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    698
  • Mass (Da)
    76,532
  • Last updated
    2004-07-19 v1
  • Checksum
    BE106526C9AA891C
MGFAVESRSHVKDILGLINTFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAEQCRARVETCSSWVQRKAEDGADIYGVTTGFGACSSRRTNQLSELQESLIRCLLAGVFTKGCASSVDELPATATRSAMLLRLNSFTYGCSGIRWEVMEALEKLLNSNVSPKVPLRGSVSASGDLIPLAYIAGLLIGKPSVVARIGDDVEVPAPEALSRVGLRPFKLQAKEGLALVNGTSFATALASTVMYDANVLLLLVETLCGMFCEVIFGREEFAHPLIHKVKPHPGQIESAELLEWLLRSSPFQDLSREYYSIDKLKKPKQDRYALRSSPQWLAPLVQTIRDATTTVETEVNSANDNPIIDHANDRALHGANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGPDLSVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALISARKTEEALDILKLMIASHLTAMCQAVDLRQLEEALVKVVENVVSTLADECGLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLEQSCFGSILALHKKDGIETDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKKGHKTADNNDALVRIQGSRFLPFYRFVREELDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFLGQPNGCANGVESFQSVWNKSA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY582743
EMBL· GenBank· DDBJ
AAT47186.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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