Q92195 · PALY_AGABI
- ProteinPhenylalanine ammonia-lyase
- GenepalA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids142 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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).
Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids (By similarity).
Catalytic activity
- L-phenylalanine = (E)-cinnamate + NH4+
Pathway
Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | phenylalanine ammonia-lyase activity | |
Biological Process | cinnamic acid biosynthetic process | |
Biological Process | L-phenylalanine catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhenylalanine ammonia-lyase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Agaricaceae > Agaricus
Accessions
- Primary accessionQ92195
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215429 | 1-142 | Phenylalanine ammonia-lyase | |||
Sequence: ETGRIHHGGNFQAMAVTNAMEKTRLALHHIGKIIFAQSTELINPATNRGLPPSLAASDPSLNYHVKGVDIATAAYAAELGYLASPVSTHIQSAEMHNQAVNSMALVSARATINSIDVLSMLVATYLYNLCQALDLRALQAEF |
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 statusFragment
- Length142
- Mass (Da)15,200
- Last updated1997-02-01 v1
- Checksum93F82EAAD1E4C7F9
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: E | ||||||
Non-terminal residue | 142 | |||||
Sequence: F |