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Links from Protein

Items: 14

1.

Mur ligase family protein

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
2.

glutamate ligase domain-containing protein

This entry contains a number of related ligase enzymes which have EC numbers 6.3.2.* which 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 [1,3,4]. This entry also includes folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate and cyanophycin synthetase that catalyses the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin) [2]. [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. [2]. 9652408. Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). Ziegler K, Diener A, Herpin C, Richter R, Deutzmann R, Lockau W;. Eur J Biochem. 1998;254:154-159. [3]. 25130693. The biology of Mur ligases as an antibacterial target. Ko. TRUNCATED at 1650 bytes (from Pfam)

GO Terms:
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
acid-amino acid ligase activity (GO:0016881)
Date:
2024-10-16
Family Accession:
NF014874.5
Method:
HMM
3.

Mur 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:
2024-10-16
Family Accession:
NF013396.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
regulation of cell shape (GO:0008360)
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
ligase activity (GO:0016874)
Biological Process:
cell division (GO:0051301)
Date:
2021-07-22
Family Accession:
NF001126.0
Method:
HMM
11.

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
regulation of cell shape (GO:0008360)
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
acid-amino acid ligase activity (GO:0016881)
Biological Process:
cell division (GO:0051301)
Date:
2021-07-28
Family Accession:
NF001124.0
Method:
HMM
12.

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

Gene:
murE
GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
regulation of cell shape (GO:0008360)
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
acid-amino acid ligase activity (GO:0016881)
Biological Process:
cell division (GO:0051301)
Date:
2021-08-24
Family Accession:
NF001123.0
Method:
HMM
13.

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan

Date:
2023-03-08
Family Accession:
11478177
Method:
Sparcle
14.

UDP-N-acetylmuramyl-tripeptide synthetase

This model is equivalog because it does not distinguish lysine-adding (EC 6.3.2.7) from diaminopimelate-adding forms of MurE (EC 6.3.2.13).

Gene:
murE
GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
regulation of cell shape (GO:0008360)
Molecular Function:
acid-amino acid ligase activity (GO:0016881)
Biological Process:
cell division (GO:0051301)
Date:
2024-05-30
Family Accession:
TIGR01085.1
Method:
HMM
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