Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1w27a_ All alpha proteins L-aspartase-like L-aspartase-like HAL/PAL-like Phenylalanine ammonia-lyase, PAL PARSLEY (Petroselinum crispum ) [TaxId: 4043 ], SCOPe (2.08)
Bd1w27b_ All alpha proteins L-aspartase-like L-aspartase-like HAL/PAL-like Phenylalanine ammonia-lyase, PAL PARSLEY (Petroselinum crispum ) [TaxId: 4043 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyHAL/PAL-like 8030850 4001447 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyL-aspartase-like 8043229 3001572 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyL-aspartase-like 8043229 3001572 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ALyase_aromatic_Ne1w27A3 A: alpha arraysX: L-aspartase N-terminal domain-like (From Topology)H: L-aspartase N-terminal domain-like (From Topology)T: L-aspartase N-terminal domain-likeF: Lyase_aromatic_NECOD (1.6)
APLN02457e1w27A2 A: alpha arraysX: L-aspartase C-terminal domain-like (From Homology)H: L-aspartase C-terminal domain-likeT: L-aspartase C-terminal domain-likeF: PLN02457ECOD (1.6)
ALyase_aromatic_Ce1w27A1 A: alpha arraysX: L-aspartase middle domain-likeH: L-aspartase middle domain-like (From Topology)T: L-aspartase middle domain-likeF: Lyase_aromatic_CECOD (1.6)
BLyase_aromatic_Ne1w27B3 A: alpha arraysX: L-aspartase N-terminal domain-like (From Topology)H: L-aspartase N-terminal domain-like (From Topology)T: L-aspartase N-terminal domain-likeF: Lyase_aromatic_NECOD (1.6)
BPLN02457e1w27B2 A: alpha arraysX: L-aspartase C-terminal domain-like (From Homology)H: L-aspartase C-terminal domain-likeT: L-aspartase C-terminal domain-likeF: PLN02457ECOD (1.6)
BLyase_aromatic_Ce1w27B1 A: alpha arraysX: L-aspartase middle domain-likeH: L-aspartase middle domain-like (From Topology)T: L-aspartase middle domain-likeF: Lyase_aromatic_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.10.275.10 Mainly Alpha Orthogonal Bundle Fumarase C Chain B, domain 1CATH (4.3.0)
A1.20.200.10 Mainly Alpha Up-down Bundle Fumarase C Chain A, domain 2CATH (4.3.0)
A1.10.274.20 Mainly Alpha Orthogonal Bundle Enzyme I Chain A, domain 2CATH (4.3.0)
B1.10.275.10 Mainly Alpha Orthogonal Bundle Fumarase C Chain B, domain 1CATH (4.3.0)
B1.20.200.10 Mainly Alpha Up-down Bundle Fumarase C Chain A, domain 2CATH (4.3.0)
B1.10.274.20 Mainly Alpha Orthogonal Bundle Enzyme I Chain A, domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00221Aromatic amino acid lyase (Lyase_aromatic)Aromatic amino acid lyase- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
PHENYLALANINE AMMONIA-LYASE 1

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
phenylalanine ammonia-lyase  M-CSA #708

Phenylalanine ammonia-lyase (PAL) is a plant enzyme which catalyses the non-oxidative elimination of ammonia from L-Phe to give trans-cinnamate. Trans-cinnamate is the precursor of numerous phenylpropanoid compounds and plays an important role in plant development and plant stress response. PAL may become a useful palliative for phenylketonuria as it has been shown to be able to convert excess Phe (toxic) in the blood into harmless compounds. It follows the same catalytic mechanism as tyrosine ammonia-lyase (TAL) for the deamination of L-tyrosine to (E)-4-coumarate.

Defined by 3 residues: TYR:A-110ASP:A-349 [auth A-351]GLY:A-398 [auth A-400]
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Explore in 3DM-CSA Motif Definition
Extent of motif is too large to support Structure Motif searching.
EC: 4.3.1.5 (PDB Primary Data)
EC: 4.3.1.24 (UniProt)