Protein Family Models for Protein (Select 1005571660) - Protein Family Models

Select item 4173281.

This HMM hits multiple proteins of peptidoglycan (murein) biosynthesis, such as MurC, MurD, MurE, and MurF of Escherichia coli.

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Biological Process:: biosynthetic process (GO:0009058)

Molecular Function:: acid-amino acid ligase activity (GO:0016881)

Date:: 2024-08-14

Family Accession:: NF019850.5
Method:: HMM

Select item 4136942.

glutamate ligase domain-containing protein

This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC (Swiss:P17952), MurD (Swiss:P14900), MurE (Swiss:P22188), MurF (Swiss:P11880), Mpl (Swiss:P37773) and FolC (Swiss:P08192). MurC, MurD, Mure and MurF catalyse 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 synthesised 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. [1]. 9218784. Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate. ligase from Escherichia coli.. Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van. Heijenoort J, Dideberg O;. EMBO J 1997;16:3416-3425. (from Pfam)

GO Terms:

Biological Process:: biosynthetic process (GO:0009058)

Molecular Function:: acid-amino acid ligase activity (GO:0016881)

Date:: 2024-08-14

Family Accession:: NF014874.5
Method:: HMM

Select item 3947243.

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Family Accession:

Select item 3904304.

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Family Accession:

Select item 3535785.

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Family Accession:

Select item 3489556.

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Family Accession:

Select item 1419967.

bifunctional protein FolC

This HMM 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.

Gene:: folC

GO Terms:

Molecular Function:: tetrahydrofolylpolyglutamate synthase activity (GO:0004326)

Molecular Function:: ATP binding (GO:0005524)

Cellular Component:: cytoplasm (GO:0005737)

Biological Process:: folic acid-containing compound metabolic process (GO:0006760)

Molecular Function:: dihydrofolate synthase activity (GO:0008841)

Biological Process:: tetrahydrofolate biosynthetic process (GO:0046654)

Date:: 2024-05-30

Family Accession:: TIGR01499.1
Method:: HMM

Select item 911328.

bifunctional folylpolyglutamate synthase/dihydrofolate synthase

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

Date:: 2024-07-05

Family Accession:: 11416298
Method:: Sparcle

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