MULTISPECIES: hypothetical protein [Cutibacterium]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PheA2 super family | cl33760 | Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ... |
1-48 | 3.59e-13 | ||
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis The actual alignment was detected with superfamily member COG0077: Pssm-ID: 439847 [Multi-domain] Cd Length: 274 Bit Score: 61.27 E-value: 3.59e-13
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| Name | Accession | Description | Interval | E-value | ||
| PheA2 | COG0077 | Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ... |
1-48 | 3.59e-13 | ||
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 439847 [Multi-domain] Cd Length: 274 Bit Score: 61.27 E-value: 3.59e-13
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| ACT_CM-PDT | cd04905 | C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ... |
1-48 | 3.02e-12 | ||
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme; The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153177 [Multi-domain] Cd Length: 80 Bit Score: 55.58 E-value: 3.02e-12
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| PRK11898 | PRK11898 | prephenate dehydratase; Provisional |
1-40 | 5.92e-09 | ||
prephenate dehydratase; Provisional Pssm-ID: 237013 [Multi-domain] Cd Length: 283 Bit Score: 49.82 E-value: 5.92e-09
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| Name | Accession | Description | Interval | E-value | ||
| PheA2 | COG0077 | Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ... |
1-48 | 3.59e-13 | ||
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 439847 [Multi-domain] Cd Length: 274 Bit Score: 61.27 E-value: 3.59e-13
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| ACT_CM-PDT | cd04905 | C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ... |
1-48 | 3.02e-12 | ||
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme; The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153177 [Multi-domain] Cd Length: 80 Bit Score: 55.58 E-value: 3.02e-12
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| ACT_AAAH-PDT-like | cd04880 | ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ... |
1-48 | 6.13e-10 | ||
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes appear to be regulated, in part, by the phosphorylation of serine residues N-terminal of the ACT domain. Also included in this CD are the C-terminal ACT domains of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme found in plants, fungi, bacteria, and archaea. The P-protein of Escherichia coli (CM-PDT) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153152 [Multi-domain] Cd Length: 75 Bit Score: 49.42 E-value: 6.13e-10
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| PRK11898 | PRK11898 | prephenate dehydratase; Provisional |
1-40 | 5.92e-09 | ||
prephenate dehydratase; Provisional Pssm-ID: 237013 [Multi-domain] Cd Length: 283 Bit Score: 49.82 E-value: 5.92e-09
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| Blast search parameters | ||||
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