A0A4Y6HUD7 · PALY2_PLEOS
- ProteinPhenylalanine ammonia-lyase 2
- GenePAL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids747 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and a free ammonium ion (PubMed:31655558).
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 active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 124 | Proton donor/acceptor | ||||
Sequence: Y | ||||||
Binding site | 290 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 380 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 386 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 416 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 487 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 515 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 518 | (E)-cinnamate (UniProtKB | ChEBI) | ||||
Sequence: N |
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 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Pleurotineae > Pleurotaceae > Pleurotus
Accessions
- Primary accessionA0A4Y6HUD7
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454792 | 1-747 | Phenylalanine ammonia-lyase 2 | |||
Sequence: MTILSGTTAAPRVNGTTMNGHSKPHTNGVHLNGHAPKATTESPWPQSEEKTLLDKFVEAYYEFESYKSGQTVKVDGKTLSLAGVVAAARHHAKISLDDSASIKDKVVKSRKVIADKVASGASVYGLSTGFGGSADTRTDQPLSLGHALLQHQHVGVLPSSSQPLDVLPLSDPMSATSMPEAWVRAAMLIRMNSLIRGHSGVRWELIEKIAEIFDANITPVVPLRSSISASGDLSPLSYIAGTVVGNPSIRVFDGPAAFGAREMVPSAKALASHGIDPLPLASKEPLGILNGTAFSAAVGALALNEAVHFAMLAQVCTAMGTEALVGTRLSFEPFIHATCRPHPGQIEAARNIYNLLEGTTFASVHHEEVHIAEDQGTLRQDRYPLRTSPQFLGPQLEDILHAYVSVTQECNSTTDNPLIDGETGEIHHGGNFQAMAVTNAMEKTRLALHHIGKLLFAQCTELVNPAMNNGLPPSLAATDPSLNYHTKGIDIATAAYVSELGYLANPVSTHIQSAEMHNQAVNSLALISARATVNSLDVLSLLISSYLYILCQALDLRALQMEFVKGVEEIIREELSLLFASVVSPAELEALTSKVLSAAQTSLDTSGSMDAPARMKKMASTTTIPLFDFLTELTLPDAISSGIAMVSIPSFRSHLASRATALLDQLRRDYLSGQRGAAPASPYLNKTRMVYEFVRLTLGVKMHGSENYARFAKGLGVEDETIGQNISRIHEAIRDGKMQAITVAMFA | ||||||
Cross-link | 229↔231 | 5-imidazolinone (Ala-Gly) | ||||
Sequence: ASG | ||||||
Modified residue | 230 | 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
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Polar residues | ||||
Sequence: MTILSGTTAAPRVNGTTMNGHSKPHT | ||||||
Region | 1-47 | Disordered | ||||
Sequence: MTILSGTTAAPRVNGTTMNGHSKPHTNGVHLNGHAPKATTESPWPQS |
Sequence similarities
Belongs to the PAL/histidase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length747
- Mass (Da)79,946
- Last updated2019-09-18 v1
- Checksum94D295D85EE8A0BB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Polar residues | ||||
Sequence: MTILSGTTAAPRVNGTTMNGHSKPHT |