histidine ammonia-lyase; This enzyme deaminates histidine to urocanic acid, the first step in ...
114-625
0e+00
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: 848.22 E-value: 0e+00
N-terminal of Par3 and HAL proteins; This domain is about 150 amino acids in length found ...
15-87
4.06e-04
N-terminal of Par3 and HAL proteins; This domain is about 150 amino acids in length found associated with pfam00595 in eukaryotes. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament.
The actual alignment was detected with superfamily member pfam12053:
Pssm-ID: 463446 Cd Length: 82 Bit Score: 39.62 E-value: 4.06e-04
histidine ammonia-lyase; This enzyme deaminates histidine to urocanic acid, the first step in ...
114-625
0e+00
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: 848.22 E-value: 0e+00
Aromatic amino acid lyase; This family includes proteins with phenylalanine ammonia-lyase, EC: ...
121-585
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: 697.63 E-value: 0e+00
Phenylalanine ammonia-lyase (PAL) and histidine ammonia-lyase (HAL); PAL and HAL are members ...
121-567
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: 694.26 E-value: 0e+00
N-terminal of Par3 and HAL proteins; This domain is about 150 amino acids in length found ...
15-87
4.06e-04
N-terminal of Par3 and HAL proteins; This domain is about 150 amino acids in length found associated with pfam00595 in eukaryotes. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament.
Pssm-ID: 463446 Cd Length: 82 Bit Score: 39.62 E-value: 4.06e-04
histidine ammonia-lyase; This enzyme deaminates histidine to urocanic acid, the first step in ...
114-625
0e+00
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: 848.22 E-value: 0e+00
Aromatic amino acid lyase; This family includes proteins with phenylalanine ammonia-lyase, EC: ...
121-585
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: 697.63 E-value: 0e+00
Phenylalanine ammonia-lyase (PAL) and histidine ammonia-lyase (HAL); PAL and HAL are members ...
121-567
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: 694.26 E-value: 0e+00
phenylalanine ammonia-lyase; Members of this subfamily of MIO prosthetic group enzymes are ...
99-571
2.89e-65
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: 227.76 E-value: 2.89e-65
phenylalanine aminomutase (L-beta-phenylalanine forming); Members of this family are the ...
112-647
7.16e-43
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: 164.50 E-value: 7.16e-43
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
288-553
1.11e-32
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze 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. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 125.80 E-value: 1.11e-32
N-terminal of Par3 and HAL proteins; This domain is about 150 amino acids in length found ...
15-87
4.06e-04
N-terminal of Par3 and HAL proteins; This domain is about 150 amino acids in length found associated with pfam00595 in eukaryotes. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament.
Pssm-ID: 463446 Cd Length: 82 Bit Score: 39.62 E-value: 4.06e-04
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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