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{
"metadata": {
"accession": "IPR013221",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0005524",
"name": "ATP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0016881",
"name": "acid-amino acid ligase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0009058",
"name": "biosynthetic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF08245": "Mur ligase middle domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR013221",
"name": "Mur ligase, central",
"type": "Domain",
"children": []
},
"name": {
"name": "Mur ligase, central",
"short": "Mur_ligase_cen"
},
"description": [
{
"text": "<p>This entry represents the central domain from all four stage 2 Mur enzymes: UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanine-D-glutamate ligase (MurD), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). 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) [[cite:PUB00008020]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria is comprised of a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages:</p>\n\n<ul>\n<li>(1) formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc).</li>\n<li>(2) addition of a short polypeptide chain to the UDPMurNAc.</li>\n<li>(3) addition of a second GlcNAc to the disaccharide-pentapeptide building block and transport of this unit through the cytoplasmic membrane and incorporation into the growing peptidoglycan layer.</li>\n</ul>\n\n<p>Stage two involves four key Mur ligase enzymes: MurC ([ec:6.3.2.8]) [[cite:PUB00035788]], MurD ([ec:6.3.2.9]) [[cite:PUB00035789]], MurE ([ec:6.3.2.13]) [[cite:PUB00035790]] and MurF ([ec:6.3.2.10]) [[cite:PUB00035791]]. These four Mur ligases are responsible for the successive additions of L-alanine, D-glutamate, meso-diaminopimelate or L-lysine, and D-alanyl-D-alanine to UDP-N-acetylmuramic acid [[cite:PUB00101154]]. All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each composed of three domains: an N-terminal Rossmann-fold domain responsible for binding the UDPMurNAc substrate; a central domain (similar to ATP-binding domains of several ATPases and GTPases); and a C-terminal domain (similar to dihydrofolate reductase fold) that binds the incoming amino acid [[cite:PUB00101154]]. Residues found in the three domains (the Asp50, Lys130 (GKT motif), and Glu174 residues, MurC numbering) are involved in the catalytic process [[cite:PUB00101154]]. The conserved sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family, including folylpolyglutamate synthetase, cyanophycin synthetase and the capB enzyme from Bacillales [[cite:PUB00035792]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00035788": {
"PMID": 17139082,
"ISBN": null,
"volume": "62",
"issue": "Pt 12",
"year": 2006,
"title": "Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC).",
"URL": null,
"raw_pages": "1466-74",
"medline_journal": "Acta Crystallogr D Biol Crystallogr",
"ISO_journal": "Acta Crystallogr. D Biol. Crystallogr.",
"authors": [
"Deva T",
"Baker EN",
"Squire CJ",
"Smith CA."
],
"DOI_URL": "http://dx.doi.org/10.1107/S0907444906038376"
},
"PUB00035789": {
"PMID": 17427948,
"ISBN": null,
"volume": "68",
"issue": "1",
"year": 2007,
"title": "Targeted molecular dynamics simulation studies of binding and conformational changes in E. coli MurD.",
"URL": null,
"raw_pages": "243-54",
"medline_journal": "Proteins",
"ISO_journal": "Proteins",
"authors": [
"Perdih A",
"Kotnik M",
"Hodoscek M",
"Solmajer T."
],
"DOI_URL": "http://dx.doi.org/10.1002/prot.21374"
},
"PUB00035790": {
"PMID": 16595662,
"ISBN": null,
"volume": "281",
"issue": "23",
"year": 2006,
"title": "The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity.",
"URL": null,
"raw_pages": "15680-6",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Boniface A",
"Bouhss A",
"Mengin-Lecreulx D",
"Blanot D."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M506311200"
},
"PUB00035791": {
"PMID": 16322581,
"ISBN": null,
"volume": "14",
"issue": "12",
"year": 2005,
"title": "Structure of MurF from Streptococcus pneumoniae co-crystallized with a small molecule inhibitor exhibits interdomain closure.",
"URL": null,
"raw_pages": "3039-47",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci.",
"authors": [
"Longenecker KL",
"Stamper GF",
"Hajduk PJ",
"Fry EH",
"Jakob CG",
"Harlan JE",
"Edalji R",
"Bartley DM",
"Walter KA",
"Solomon LR",
"Holzman TF",
"Gu YG",
"Lerner CG",
"Beutel BA",
"Stoll VS."
],
"DOI_URL": "http://dx.doi.org/10.1110/ps.051604805"
},
"PUB00035792": {
"PMID": 16934839,
"ISBN": null,
"volume": "362",
"issue": "4",
"year": 2006,
"title": "Structure, function and dynamics in the mur family of bacterial cell wall ligases.",
"URL": null,
"raw_pages": "640-55",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Smith CA."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.jmb.2006.07.066"
},
"PUB00008020": {
"PMID": 9652408,
"ISBN": null,
"volume": "254",
"issue": "1",
"year": 1998,
"title": "Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin).",
"URL": null,
"raw_pages": "154-9",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Ziegler K",
"Diener A",
"Herpin C",
"Richter R",
"Deutzmann R",
"Lockau W."
],
"DOI_URL": "http://dx.doi.org/10.1046/j.1432-1327.1998.2540154.x"
},
"PUB00101154": {
"PMID": 18974047,
"ISBN": null,
"volume": "283",
"issue": "52",
"year": 2008,
"title": "The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum.",
"URL": null,
"raw_pages": "36553-63",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Fiuza M",
"Canova MJ",
"Patin D",
"Letek M",
"Zanella-Cleon I",
"Becchi M",
"Mateos LM",
"Mengin-Lecreulx D",
"Molle V",
"Gil JA."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036565",
"name": "Mur-like, catalytic domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 370,
"interactions": 0,
"matches": 164263,
"pathways": 0,
"proteins": 163580,
"proteomes": 18754,
"sets": 0,
"structural_models": {
"alphafold": 126332,
"bfvd": 0
},
"structures": 148,
"taxa": 33912
},
"entry_annotations": {
"alignment:seed": 54,
"alignment:full": 56813
},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "6.3.2",
"url": "https://enzyme.expasy.org/EC/6.3.2"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "8ewa",
"name": "Crystal Structure of UDP-N-acetylmuramate-L-alanine ligase (UDP-N-acetylmuramoyl-L-alanine synthetase, MurC) Pseudomonas aeruginosa in complex with ligand AZ-13644923"
}
}
}
