1UAG

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1uaga1	Alpha and beta proteins (a/b)	MurCD N-terminal domain	MurCD N-terminal domain	MurCD N-terminal domain	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase MurD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1uaga2	Alpha and beta proteins (a/b)	MurD-like peptide ligases, peptide-binding domain	MurD-like peptide ligases, peptide-binding domain	MurCDEF C-terminal domain	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase MurD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1uaga3	Alpha and beta proteins (a/b)	Ribokinase-like	MurD-like peptide ligases, catalytic domain	MurCDEF	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase MurD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	MurCD N-terminal domain	8058462	3000082	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	MurD catalytic domain-like	8058463	3000107	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	MurD peptide-binding domain-like	8091456	3001290	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	NAD_binding_8_1	e1uagA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: MurCD/PglD N-terminal domain-like	F: NAD_binding_8_1	ECOD (1.6)
A	Mur_ligase_M	e1uagA2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: Mur_ligase_M	ECOD (1.6)
A	Mur_ligase_C	e1uagA3	A: a/b three-layered sandwiches	X: MurD-like peptide ligases, peptide-binding domain (From Topology)	H: MurD-like peptide ligases, peptide-binding domain (From Topology)	T: MurD-like peptide ligases, peptide-binding domain	F: Mur_ligase_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.40.1190.10	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Mur-like, catalytic domain	CATH (4.3.0)
A	3.90.190.20	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08245	Mur ligase middle domain (Mur_ligase_M)	Mur ligase middle domain	-	Domain
A	PF02875	Mur ligase, glutamate ligase domain (Mur_ligase_C)	Mur ligase, glutamate ligase domain	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 ...	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].	Domain
A	PF21799	Mur ligase MurD-like, N-terminal domain (MurD-like_N)	Mur ligase MurD-like, N-terminal domain	This domain is found at the N-terminal end of Mur ligases predominantly from proteobacteria, including UDP-N -acetylmuramoylalanine--D-glutamate ligase from Escherichia coli (MurD). Proteins in this family play a crucial role in the intracellular ste ...	This domain is found at the N-terminal end of Mur ligases predominantly from proteobacteria, including UDP-N -acetylmuramoylalanine--D-glutamate ligase from Escherichia coli (MurD). Proteins in this family play a crucial role in the intracellular steps leading to the synthesis of bacterial peptidoglycan. MurD shows a three-domain topology, with the N-terminal (this entry) responsible for binding the UDP-precursor. This domain shows a Rossmann fold [1-6].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	UDP-N-ACETYLMURAMOYL-L-ALANINE/:D-GLUTAMATE LIGASE	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding identical protein binding protein binding acid-amino acid ligase activity catalytic activity UDP-N-acetylmuramoylalanine-D-glutamate ligase activity ligase activity, forming carbon-nitrogen bonds ligase activity	developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis cellular process cell division cellular component organization developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis cellular process cell division cellular component organization cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization carbohydrate derivative biosynthetic process peptidoglycan-based cell wall biogenesis cellular biosynthetic process glycosaminoglycan metabolic process cellular metabolic process carbohydrate derivative metabolic process macromolecule biosynthetic process cellular component biogenesis peptidoglycan biosynthetic process cell wall biogenesis biosynthetic process cell wall macromolecule biosynthetic process aminoglycan metabolic process peptidoglycan metabolic process aminoglycan biosynthetic process metabolic process glycosaminoglycan biosynthetic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR004101	Mur ligase, C-terminal	Domain
A	IPR036565	Mur-like, catalytic domain superfamily	Homologous Superfamily
A	IPR005762	UDP-N-acetylmuramoylalanine-D-glutamate ligase MurD	Family
A	IPR036615	Mur ligase, C-terminal domain superfamily	Homologous Superfamily
A	IPR013221	Mur ligase, central	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase M-CSA #317	UDP-N-acetylmuramoylalanine-D-glutamate ligase catalyses the formation of the peptide bond between UDP-N-acetylmuramoyl-L-alanine and D-glutamate in peptidoglycan biosynthesis. Peptidoglycan is formed as linear repeating disaccharide chains interconnected by a short peptide moiety. It is found in bacterial cell walls and hence peptidoglycan biosynthetic enzymes are possible targets for antibacterial drugs.	Defined by 3 residues: LYS:A-115ASN:A-138HIS:A-183 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 6.3.2.9 (PDB Primary Data) Search M-CSA Motif + EC 6.3.2.9

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.