prephenate dehydrogenase [Bacillus cereus]
Protein Classification
prephenate dehydrogenase( domain architecture ID 11482296)
prephenate dehydrogenase catalyzes the conversion of prephenate and NAD(+) to 4-hydroxyphenylpyruvate, CO(2) and NADH
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK06545 | PRK06545 | prephenate dehydrogenase; Validated |
3-362 | 4.59e-163 | ||||||
prephenate dehydrogenase; Validated : Pssm-ID: 235824 [Multi-domain] Cd Length: 359 Bit Score: 460.53 E-value: 4.59e-163
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| PRK06545 | PRK06545 | prephenate dehydrogenase; Validated |
3-362 | 4.59e-163 | ||||||
prephenate dehydrogenase; Validated Pssm-ID: 235824 [Multi-domain] Cd Length: 359 Bit Score: 460.53 E-value: 4.59e-163
|
||||||||||
| TyrA | COG0287 | Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
3-280 | 7.16e-115 | ||||||
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 334.79 E-value: 7.16e-115
|
||||||||||
| PDH_N | pfam02153 | Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ... |
17-172 | 1.55e-40 | ||||||
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face. Pssm-ID: 460467 [Multi-domain] Cd Length: 154 Bit Score: 140.21 E-value: 1.55e-40
|
||||||||||
| ACT_PDH-BS | cd04909 | C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH); ... |
294-362 | 4.01e-25 | ||||||
C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH); The C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback-inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153181 Cd Length: 69 Bit Score: 96.53 E-value: 4.01e-25
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| PRK06545 | PRK06545 | prephenate dehydrogenase; Validated |
3-362 | 4.59e-163 | ||||||
prephenate dehydrogenase; Validated Pssm-ID: 235824 [Multi-domain] Cd Length: 359 Bit Score: 460.53 E-value: 4.59e-163
|
||||||||||
| TyrA | COG0287 | Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
3-280 | 7.16e-115 | ||||||
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 334.79 E-value: 7.16e-115
|
||||||||||
| PRK14806 | PRK14806 | bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
3-281 | 1.77e-66 | ||||||
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 223.33 E-value: 1.77e-66
|
||||||||||
| PRK08507 | PRK08507 | prephenate dehydrogenase; Validated |
4-283 | 3.37e-56 | ||||||
prephenate dehydrogenase; Validated Pssm-ID: 181452 [Multi-domain] Cd Length: 275 Bit Score: 184.71 E-value: 3.37e-56
|
||||||||||
| PRK07502 | PRK07502 | prephenate/arogenate dehydrogenase family protein; |
3-273 | 4.29e-55 | ||||||
prephenate/arogenate dehydrogenase family protein; Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 182.86 E-value: 4.29e-55
|
||||||||||
| PRK07417 | PRK07417 | prephenate/arogenate dehydrogenase; |
4-280 | 2.06e-49 | ||||||
prephenate/arogenate dehydrogenase; Pssm-ID: 180970 [Multi-domain] Cd Length: 279 Bit Score: 167.38 E-value: 2.06e-49
|
||||||||||
| PDH_N | pfam02153 | Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ... |
17-172 | 1.55e-40 | ||||||
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face. Pssm-ID: 460467 [Multi-domain] Cd Length: 154 Bit Score: 140.21 E-value: 1.55e-40
|
||||||||||
| PRK11861 | PRK11861 | bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
65-293 | 1.79e-34 | ||||||
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 134.06 E-value: 1.79e-34
|
||||||||||
| PDH_C | pfam20463 | Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate ... |
176-274 | 3.48e-25 | ||||||
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate dehydrogenases EC:1.3.1.12 (PDHs) involved in tyrosine biosynthesis. This is the C-terminal, helical dimerization domain of PDHs. Pssm-ID: 466612 [Multi-domain] Cd Length: 102 Bit Score: 97.84 E-value: 3.48e-25
|
||||||||||
| ACT_PDH-BS | cd04909 | C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH); ... |
294-362 | 4.01e-25 | ||||||
C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH); The C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback-inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153181 Cd Length: 69 Bit Score: 96.53 E-value: 4.01e-25
|
||||||||||
| PRK08655 | PRK08655 | prephenate dehydrogenase; Provisional |
3-278 | 1.15e-15 | ||||||
prephenate dehydrogenase; Provisional Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 77.72 E-value: 1.15e-15
|
||||||||||
| ACT_PDH-BS-like | cd04889 | C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) ... |
297-355 | 2.59e-12 | ||||||
C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate; Included in this CD is the C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Also included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153161 Cd Length: 56 Bit Score: 60.98 E-value: 2.59e-12
|
||||||||||
| ACT | cd02116 | ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
297-355 | 1.26e-04 | ||||||
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times. Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 39.58 E-value: 1.26e-04
|
||||||||||
| ACT | pfam01842 | ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
295-347 | 4.98e-04 | ||||||
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 38.06 E-value: 4.98e-04
|
||||||||||
| PRK06349 | PRK06349 | homoserine dehydrogenase; Provisional |
276-322 | 4.72e-03 | ||||||
homoserine dehydrogenase; Provisional Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 38.90 E-value: 4.72e-03
|
||||||||||
| ACT_RelA-SpoT | cd04876 | ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ... |
297-334 | 6.88e-03 | ||||||
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153148 [Multi-domain] Cd Length: 71 Bit Score: 34.73 E-value: 6.88e-03
|
||||||||||
| ACT_HSDH-Hom | cd04881 | ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ... |
299-322 | 8.96e-03 | ||||||
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153153 [Multi-domain] Cd Length: 79 Bit Score: 34.80 E-value: 8.96e-03
|
||||||||||
| Blast search parameters | ||||
|
