Q92195 · PALY_AGABI

Function

function

Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and a free ammonium ion (By similarity).
Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids (By similarity).

Catalytic activity

Pathway

Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1.

Features

Showing features for binding site.

1142102030405060708090100110120130140
TypeIDPosition(s)Description
Binding site66(E)-cinnamate (UniProtKB | ChEBI)
Binding site94(E)-cinnamate (UniProtKB | ChEBI)
Binding site97(E)-cinnamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionphenylalanine ammonia-lyase activity
Biological Processcinnamic acid biosynthetic process
Biological ProcessL-phenylalanine catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phenylalanine ammonia-lyase
  • EC number

Gene names

    • Name
      palA

Organism names

  • Taxonomic identifier
  • Strain
    • Horst U1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Agaricaceae > Agaricus

Accessions

  • Primary accession
    Q92195

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002154291-142Phenylalanine ammonia-lyase

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

Family & Domains

Sequence similarities

Belongs to the PAL/histidase family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    142
  • Mass (Da)
    15,200
  • Last updated
    1997-02-01 v1
  • Checksum
    93F82EAAD1E4C7F9
ETGRIHHGGNFQAMAVTNAMEKTRLALHHIGKIIFAQSTELINPATNRGLPPSLAASDPSLNYHVKGVDIATAAYAAELGYLASPVSTHIQSAEMHNQAVNSMALVSARATINSIDVLSMLVATYLYNLCQALDLRALQAEF

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue142

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z82018
EMBL· GenBank· DDBJ
CAB04783.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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