bifunctional folylpolyglutamate synthase (FGPS)/dihydrofolate synthase (DHFS) functions in two distinct reactions of the de novo folate biosynthetic pathway, catalyzing the addition of a glutamate residue to dihydropteroate to form dihydrofolate and the successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
1-422
1.01e-144
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
:
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 418.74 E-value: 1.01e-144
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
1-422
1.01e-144
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 418.74 E-value: 1.01e-144
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
22-416
7.09e-101
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 305.75 E-value: 7.09e-101
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
291-344
6.58e-09
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 52.73 E-value: 6.58e-09
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
1-422
1.01e-144
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 418.74 E-value: 1.01e-144
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
22-416
7.09e-101
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 305.75 E-value: 7.09e-101
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
291-344
6.58e-09
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 52.73 E-value: 6.58e-09
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
33-399
1.78e-04
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273435 [Multi-domain] Cd Length: 464 Bit Score: 43.46 E-value: 1.78e-04
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 40.86 E-value: 1.42e-03
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 40.45 E-value: 1.92e-03
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
14-65
4.61e-03
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 39.28 E-value: 4.61e-03
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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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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