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dihydropteroate synthase, partial [Thiocystis violacea]
dihydropteroate synthase( domain architecture ID 11416730)
dihydropteroate synthase catalyzes the formation of 7,8-dihydropteroate from para-aminobenzoic acid and 6-hydroxymethyl-7,8-dihydropterin-pyrophosphate, a key step in the folate biosynthetic pathway
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
FolP | COG0294 | Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ... |
9-146 | 1.34e-72 | |||
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis : Pssm-ID: 440063 Cd Length: 274 Bit Score: 218.38 E-value: 1.34e-72
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Name | Accession | Description | Interval | E-value | |||
FolP | COG0294 | Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ... |
9-146 | 1.34e-72 | |||
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis Pssm-ID: 440063 Cd Length: 274 Bit Score: 218.38 E-value: 1.34e-72
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DHPS | cd00739 | DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ... |
19-146 | 7.73e-56 | |||
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Pssm-ID: 238380 Cd Length: 257 Bit Score: 175.10 E-value: 7.73e-56
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DHPS | TIGR01496 | dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ... |
20-146 | 1.03e-53 | |||
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid] Pssm-ID: 273657 Cd Length: 257 Bit Score: 169.75 E-value: 1.03e-53
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folP | PRK11613 | dihydropteroate synthase; Provisional |
14-146 | 5.12e-50 | |||
dihydropteroate synthase; Provisional Pssm-ID: 183230 Cd Length: 282 Bit Score: 161.07 E-value: 5.12e-50
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Pterin_bind | pfam00809 | Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
22-146 | 2.73e-49 | |||
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin. Pssm-ID: 395651 [Multi-domain] Cd Length: 243 Bit Score: 158.22 E-value: 2.73e-49
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Name | Accession | Description | Interval | E-value | |||
FolP | COG0294 | Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ... |
9-146 | 1.34e-72 | |||
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis Pssm-ID: 440063 Cd Length: 274 Bit Score: 218.38 E-value: 1.34e-72
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DHPS | cd00739 | DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ... |
19-146 | 7.73e-56 | |||
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Pssm-ID: 238380 Cd Length: 257 Bit Score: 175.10 E-value: 7.73e-56
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DHPS | TIGR01496 | dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ... |
20-146 | 1.03e-53 | |||
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid] Pssm-ID: 273657 Cd Length: 257 Bit Score: 169.75 E-value: 1.03e-53
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Pterin_binding | cd00423 | Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
19-146 | 6.63e-51 | |||
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH. Pssm-ID: 238242 [Multi-domain] Cd Length: 258 Bit Score: 162.44 E-value: 6.63e-51
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folP | PRK11613 | dihydropteroate synthase; Provisional |
14-146 | 5.12e-50 | |||
dihydropteroate synthase; Provisional Pssm-ID: 183230 Cd Length: 282 Bit Score: 161.07 E-value: 5.12e-50
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Pterin_bind | pfam00809 | Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ... |
22-146 | 2.73e-49 | |||
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin. Pssm-ID: 395651 [Multi-domain] Cd Length: 243 Bit Score: 158.22 E-value: 2.73e-49
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PRK13753 | PRK13753 | dihydropteroate synthase; Provisional |
18-134 | 4.45e-13 | |||
dihydropteroate synthase; Provisional Pssm-ID: 184303 Cd Length: 279 Bit Score: 64.34 E-value: 4.45e-13
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DHDPS | cd00950 | Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
27-115 | 8.29e-06 | |||
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways. Pssm-ID: 188637 [Multi-domain] Cd Length: 284 Bit Score: 44.02 E-value: 8.29e-06
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MetH2 | COG1410 | Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
40-120 | 4.84e-05 | |||
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis Pssm-ID: 441020 [Multi-domain] Cd Length: 1141 Bit Score: 41.86 E-value: 4.84e-05
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DHDPS-like | cd00408 | Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
21-115 | 1.63e-04 | |||
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family. Pssm-ID: 188630 [Multi-domain] Cd Length: 281 Bit Score: 40.22 E-value: 1.63e-04
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Met_dep_hydrolase_A | cd01299 | Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
42-117 | 8.39e-03 | |||
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown. Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 35.35 E-value: 8.39e-03
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