Chorismate mutase I [Klebsiella pneumoniae]
Protein Classification
bifunctional chorismate mutase/prephenate dehydratase( domain architecture ID 11484831)
bifunctional chorismate mutase/prephenate dehydratase catalyzes the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| pheA | PRK10622 | bifunctional chorismate mutase/prephenate dehydratase; Provisional |
1-386 | 0e+00 | ||||||
bifunctional chorismate mutase/prephenate dehydratase; Provisional : Pssm-ID: 182594 [Multi-domain] Cd Length: 386 Bit Score: 819.36 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| pheA | PRK10622 | bifunctional chorismate mutase/prephenate dehydratase; Provisional |
1-386 | 0e+00 | ||||||
bifunctional chorismate mutase/prephenate dehydratase; Provisional Pssm-ID: 182594 [Multi-domain] Cd Length: 386 Bit Score: 819.36 E-value: 0e+00
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| PheA2 | COG0077 | Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ... |
103-380 | 3.99e-128 | ||||||
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: 369.04 E-value: 3.99e-128
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| PBP2_Ct-PDT_like | cd13631 | Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ... |
103-287 | 1.18e-88 | ||||||
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, subgroup 2; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270349 [Multi-domain] Cd Length: 182 Bit Score: 265.43 E-value: 1.18e-88
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| PDT | pfam00800 | Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ... |
106-286 | 1.29e-80 | ||||||
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein catalyzes the decarboxylation of prephenate to phenylpyruvate. Pssm-ID: 425875 [Multi-domain] Cd Length: 181 Bit Score: 244.76 E-value: 1.29e-80
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| CM_P_1 | TIGR01797 | chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ... |
7-89 | 1.30e-39 | ||||||
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the chorismate mutase domain of the gamma and beta proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. [Amino acid biosynthesis, Aromatic amino acid family] Pssm-ID: 130856 [Multi-domain] Cd Length: 83 Bit Score: 135.71 E-value: 1.30e-39
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| CM_2 | smart00830 | Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ... |
11-89 | 2.38e-21 | ||||||
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.. Pssm-ID: 214841 [Multi-domain] Cd Length: 79 Bit Score: 86.86 E-value: 2.38e-21
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| Name | Accession | Description | Interval | E-value | ||||||
| pheA | PRK10622 | bifunctional chorismate mutase/prephenate dehydratase; Provisional |
1-386 | 0e+00 | ||||||
bifunctional chorismate mutase/prephenate dehydratase; Provisional Pssm-ID: 182594 [Multi-domain] Cd Length: 386 Bit Score: 819.36 E-value: 0e+00
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| PheA2 | COG0077 | Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ... |
103-380 | 3.99e-128 | ||||||
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: 369.04 E-value: 3.99e-128
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| PBP2_Ct-PDT_like | cd13631 | Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ... |
103-287 | 1.18e-88 | ||||||
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, subgroup 2; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270349 [Multi-domain] Cd Length: 182 Bit Score: 265.43 E-value: 1.18e-88
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| PDT | pfam00800 | Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ... |
106-286 | 1.29e-80 | ||||||
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein catalyzes the decarboxylation of prephenate to phenylpyruvate. Pssm-ID: 425875 [Multi-domain] Cd Length: 181 Bit Score: 244.76 E-value: 1.29e-80
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| PRK11898 | PRK11898 | prephenate dehydratase; Provisional |
103-377 | 1.70e-70 | ||||||
prephenate dehydratase; Provisional Pssm-ID: 237013 [Multi-domain] Cd Length: 283 Bit Score: 222.78 E-value: 1.70e-70
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| PBP2_PDT_like | cd13532 | Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic ... |
105-286 | 3.26e-70 | ||||||
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270250 [Multi-domain] Cd Length: 184 Bit Score: 218.17 E-value: 3.26e-70
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| PBP2_PDT_1 | cd13630 | Catalytic domain of prephenate dehydratase and similar proteins, subgroup 1; the type 2 ... |
105-287 | 6.24e-63 | ||||||
Catalytic domain of prephenate dehydratase and similar proteins, subgroup 1; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270348 [Multi-domain] Cd Length: 180 Bit Score: 199.60 E-value: 6.24e-63
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| PLN02317 | PLN02317 | arogenate dehydratase |
100-376 | 1.24e-61 | ||||||
arogenate dehydratase Pssm-ID: 215181 [Multi-domain] Cd Length: 382 Bit Score: 203.04 E-value: 1.24e-61
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| PBP2_Sa-PDT_like | cd13633 | Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, ... |
105-286 | 8.20e-58 | ||||||
Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, subgroup 4; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270351 [Multi-domain] Cd Length: 184 Bit Score: 186.56 E-value: 8.20e-58
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| PRK11899 | PRK11899 | prephenate dehydratase; Provisional |
105-377 | 1.38e-57 | ||||||
prephenate dehydratase; Provisional Pssm-ID: 237014 [Multi-domain] Cd Length: 279 Bit Score: 189.32 E-value: 1.38e-57
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| CM_P_1 | TIGR01797 | chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ... |
7-89 | 1.30e-39 | ||||||
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the chorismate mutase domain of the gamma and beta proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. [Amino acid biosynthesis, Aromatic amino acid family] Pssm-ID: 130856 [Multi-domain] Cd Length: 83 Bit Score: 135.71 E-value: 1.30e-39
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| PheA | COG1605 | Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ... |
1-180 | 1.38e-38 | ||||||
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 441213 [Multi-domain] Cd Length: 166 Bit Score: 136.05 E-value: 1.38e-38
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| ACT_CM-PDT | cd04905 | C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ... |
297-376 | 3.97e-32 | ||||||
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: 116.06 E-value: 3.97e-32
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| PBP2_Aa-PDT_like | cd13632 | Catalytic domain of prephenate dehydratase from Arthrobacter aurescens and similar proteins, ... |
103-285 | 2.97e-29 | ||||||
Catalytic domain of prephenate dehydratase from Arthrobacter aurescens and similar proteins, subgroup 3; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270350 [Multi-domain] Cd Length: 183 Bit Score: 111.87 E-value: 2.97e-29
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| CM_2 | pfam01817 | Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ... |
11-89 | 4.35e-23 | ||||||
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine. Pssm-ID: 460345 [Multi-domain] Cd Length: 79 Bit Score: 91.79 E-value: 4.35e-23
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| ACT_AAAH-PDT-like | cd04880 | ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ... |
299-373 | 8.36e-23 | ||||||
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: 91.02 E-value: 8.36e-23
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| CM_2 | smart00830 | Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ... |
11-89 | 2.38e-21 | ||||||
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.. Pssm-ID: 214841 [Multi-domain] Cd Length: 79 Bit Score: 86.86 E-value: 2.38e-21
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| PRK06285 | PRK06285 | chorismate mutase; Provisional |
3-92 | 5.56e-12 | ||||||
chorismate mutase; Provisional Pssm-ID: 180509 [Multi-domain] Cd Length: 96 Bit Score: 61.59 E-value: 5.56e-12
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| PRK09269 | PRK09269 | chorismate mutase; Provisional |
15-94 | 9.81e-08 | ||||||
chorismate mutase; Provisional Pssm-ID: 236441 Cd Length: 193 Bit Score: 51.91 E-value: 9.81e-08
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| tyrA | PRK11199 | bifunctional chorismate mutase/prephenate dehydrogenase; Provisional |
1-122 | 3.07e-07 | ||||||
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional Pssm-ID: 183035 [Multi-domain] Cd Length: 374 Bit Score: 51.80 E-value: 3.07e-07
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| PRK12595 | PRK12595 | bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed |
7-96 | 5.49e-06 | ||||||
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed Pssm-ID: 183614 [Multi-domain] Cd Length: 360 Bit Score: 48.05 E-value: 5.49e-06
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| PRK07248 | PRK07248 | chorismate mutase; |
10-58 | 2.73e-05 | ||||||
chorismate mutase; Pssm-ID: 168880 [Multi-domain] Cd Length: 87 Bit Score: 42.36 E-value: 2.73e-05
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| PRK09239 | PRK09239 | chorismate mutase; Provisional |
7-85 | 6.42e-05 | ||||||
chorismate mutase; Provisional Pssm-ID: 181719 [Multi-domain] Cd Length: 104 Bit Score: 41.55 E-value: 6.42e-05
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| Phe4hydrox_tetr | TIGR01268 | phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ... |
296-345 | 7.60e-04 | ||||||
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form of phenylalanine-4-hydroxylase, as found in metazoans. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. It is closely related to metazoan tyrosine 3-monooxygenase and tryptophan 5-monoxygenase, and more distantly to monomeric phenylalanine-4-hydroxylases of some Gram-negative bacteria. The member of this family from Drosophila has been described as having both phenylalanine-4-hydroxylase and tryptophan 5-monoxygenase activity (. However, a Drosophila member of the tryptophan 5-monoxygenase clade has subsequently been discovered. Pssm-ID: 130335 [Multi-domain] Cd Length: 436 Bit Score: 41.36 E-value: 7.60e-04
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| PRK06443 | PRK06443 | chorismate mutase; Validated |
10-52 | 1.08e-03 | ||||||
chorismate mutase; Validated Pssm-ID: 235801 Cd Length: 177 Bit Score: 39.50 E-value: 1.08e-03
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| PRK06034 | PRK06034 | hypothetical protein; Provisional |
7-58 | 1.79e-03 | ||||||
hypothetical protein; Provisional Pssm-ID: 235680 [Multi-domain] Cd Length: 279 Bit Score: 39.69 E-value: 1.79e-03
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| PRK07857 | PRK07857 | chorismate mutase; |
9-58 | 3.93e-03 | ||||||
chorismate mutase; Pssm-ID: 236117 Cd Length: 106 Bit Score: 36.59 E-value: 3.93e-03
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| Blast search parameters | ||||
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