phenylalanine ammonia-lyase catalyzes the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton, i.e., the conversion of L-phenylalanine to trans-cinnamate and ammonia
phenylalanine ammonia-lyase; Members of this subfamily of MIO prosthetic group enzymes are ...
23-704
0e+00
phenylalanine ammonia-lyase; Members of this subfamily of MIO prosthetic group enzymes are phenylalanine ammonia-lyases. They are found, so far, in plants and fungi. From phenylalanine, this enzyme yields cinnaminic acid, a precursor of many important plant compounds. This protein shows extensive homology to histidine ammonia-lyase, the first enzyme of a histidine degradation pathway. Note that members of this family from plant species that synthesize taxol are actually phenylalanine aminomutase, and are covered by exception model TIGR04473.
Pssm-ID: 130293 [Multi-domain] Cd Length: 680 Bit Score: 1218.11 E-value: 0e+00
Aromatic amino acid lyase; This family includes proteins with phenylalanine ammonia-lyase, EC: ...
61-544
0e+00
Aromatic amino acid lyase; This family includes proteins with phenylalanine ammonia-lyase, EC:4.3.1.24, histidine ammonia-lyase, EC:4.3.1.3, and tyrosine aminomutase, EC:5.4.3.6, activities.
Pssm-ID: 459718 Cd Length: 464 Bit Score: 588.24 E-value: 0e+00
Phenylalanine ammonia-lyase (PAL) and histidine ammonia-lyase (HAL); PAL and HAL are members ...
59-525
0e+00
Phenylalanine ammonia-lyase (PAL) and histidine ammonia-lyase (HAL); PAL and HAL are members of the Lyase class I_like superfamily of enzymes that, catalyze similar beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. PAL, present in plants and fungi, catalyzes the conversion of L-phenylalanine to E-cinnamic acid. HAL, found in several bacteria and animals, catalyzes the conversion of L-histidine to E-urocanic acid. Both PAL and HAL contain the cofactor 3, 5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) which is formed by autocatalytic excision/cyclization of the internal tripeptide, Ala-Ser-Gly. PAL is being explored as enzyme substitution therapy for Phenylketonuria (PKU), a disorder which involves an inability to metabolize phenylalanine. HAL failure in humans results in the disease histidinemia.
Pssm-ID: 176460 [Multi-domain] Cd Length: 444 Bit Score: 568.68 E-value: 0e+00
phenylalanine ammonia-lyase; Members of this subfamily of MIO prosthetic group enzymes are ...
23-704
0e+00
phenylalanine ammonia-lyase; Members of this subfamily of MIO prosthetic group enzymes are phenylalanine ammonia-lyases. They are found, so far, in plants and fungi. From phenylalanine, this enzyme yields cinnaminic acid, a precursor of many important plant compounds. This protein shows extensive homology to histidine ammonia-lyase, the first enzyme of a histidine degradation pathway. Note that members of this family from plant species that synthesize taxol are actually phenylalanine aminomutase, and are covered by exception model TIGR04473.
Pssm-ID: 130293 [Multi-domain] Cd Length: 680 Bit Score: 1218.11 E-value: 0e+00
phenylalanine aminomutase (L-beta-phenylalanine forming); Members of this family are the ...
39-711
0e+00
phenylalanine aminomutase (L-beta-phenylalanine forming); Members of this family are the phenylalanine aminomutase known from taxol biosynthesis. This enzyme has the MIO prosthetic group (4-methylideneimidazole-5-one), derived from an Ala-Ser-Gly motif. Other MIO enzymes include Phe, Tyr, and His ammonia-lyases. This model serves as an exception to overrule assignments by equivalog model TIGR01226 for phenylalanine ammonia-lyase.
Pssm-ID: 275266 Cd Length: 687 Bit Score: 588.61 E-value: 0e+00
Aromatic amino acid lyase; This family includes proteins with phenylalanine ammonia-lyase, EC: ...
61-544
0e+00
Aromatic amino acid lyase; This family includes proteins with phenylalanine ammonia-lyase, EC:4.3.1.24, histidine ammonia-lyase, EC:4.3.1.3, and tyrosine aminomutase, EC:5.4.3.6, activities.
Pssm-ID: 459718 Cd Length: 464 Bit Score: 588.24 E-value: 0e+00
Phenylalanine ammonia-lyase (PAL) and histidine ammonia-lyase (HAL); PAL and HAL are members ...
59-525
0e+00
Phenylalanine ammonia-lyase (PAL) and histidine ammonia-lyase (HAL); PAL and HAL are members of the Lyase class I_like superfamily of enzymes that, catalyze similar beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. PAL, present in plants and fungi, catalyzes the conversion of L-phenylalanine to E-cinnamic acid. HAL, found in several bacteria and animals, catalyzes the conversion of L-histidine to E-urocanic acid. Both PAL and HAL contain the cofactor 3, 5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) which is formed by autocatalytic excision/cyclization of the internal tripeptide, Ala-Ser-Gly. PAL is being explored as enzyme substitution therapy for Phenylketonuria (PKU), a disorder which involves an inability to metabolize phenylalanine. HAL failure in humans results in the disease histidinemia.
Pssm-ID: 176460 [Multi-domain] Cd Length: 444 Bit Score: 568.68 E-value: 0e+00
histidine ammonia-lyase; This enzyme deaminates histidine to urocanic acid, the first step in ...
54-528
8.01e-89
histidine ammonia-lyase; This enzyme deaminates histidine to urocanic acid, the first step in histidine degradation. It is closely related to phenylalanine ammonia-lyase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200086 Cd Length: 506 Bit Score: 287.37 E-value: 8.01e-89
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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