Annotations: 1MBB

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1mbba1	Alpha and beta proteins (a+b)	FAD-binding/transporter-associated domain-like	FAD-binding/transporter-associated domain-like	Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase (MurB), N-terminal domain	Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase (MurB), N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1mbba2	Alpha and beta proteins (a+b)	Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain	Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain	Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain	Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain	(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	FAD-binding/transporter-associated domain-like	8036705	3000913	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase MurB C-terminal domain	8036714	3000935	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	FAD_binding_4	e1mbbA1	A: a+b complex topology	X: FAD-binding domain-like	H: FAD-binding domain (From Topology)	T: FAD-binding domain	F: FAD_binding_4	ECOD (1.6)
A	MurB_C	e1mbbA2	A: a+b complex topology	X: Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain (From Topology)	H: Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain (From Topology)	T: Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain	F: MurB_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.78.10	Alpha Beta	Alpha-Beta Complex	Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase	domain 1	CATH (4.3.0)
A	3.30.43.10	Alpha Beta	2-Layer Sandwich	Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase	domain 2	CATH (4.3.0)
A	3.30.465.10	Alpha Beta	2-Layer Sandwich	Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01565	FAD binding domain (FAD_binding_4)	FAD binding domain	This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, call ...	This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [1]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan [2].	Domain
A	PF02873	UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain (MurB_C)	UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain	Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE	UDP-N-acetylmuramate dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors catalytic activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding UDP-N-acetylmuramate dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors catalytic activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	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 cycle cell division 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 cycle cell division cellular component organization cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization cellular biosynthetic process glycosaminoglycan metabolic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process cellular component biogenesis organic substance metabolic process peptidoglycan metabolic process organic substance biosynthetic process glycosaminoglycan biosynthetic process carbohydrate derivative biosynthetic process peptidoglycan-based cell wall biogenesis organonitrogen compound metabolic process cellular metabolic process macromolecule biosynthetic process peptidoglycan biosynthetic process cell wall biogenesis biosynthetic process cell wall macromolecule biosynthetic process aminoglycan metabolic process aminoglycan biosynthetic process metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016167	FAD-binding, type PCMH, subdomain 1	Homologous Superfamily
A	IPR006094	FAD linked oxidase, N-terminal	Domain
A	IPR003170	UDP-N-acetylenolpyruvoylglucosamine reductase	Family
A	IPR016166	FAD-binding domain, PCMH-type	Domain
A	IPR036635	UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain superfamily	Homologous Superfamily
A	IPR036318	FAD-binding, type PCMH-like superfamily	Homologous Superfamily
A	IPR016169	FAD-binding, type PCMH, subdomain 2	Homologous Superfamily
A	IPR011601	UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A	UDP-N-acetylenolpyruvylglucosamine reductase (MurB) M-CSA #353	UDP-N-acetylenolpyruvylglucosamine reductase (MurB) reduces both E and Z isomers of enolbutyryl-UDP-GlcBAc analogs of the C3 enolpyruvate substate to UDP-methyl-N-acetylmuramic acid in the presence of NADPH. The overall product of this metabolic pathway, petidoglycan, is a biopolymer unique to Gram-positive and Gram-negative bacteria for which is essential for maintaining osmotic cell wall integrity. The absence of a homologue in eukaryotic cells makes MurB an attractive target for small molecule inhibitors with the potential to have broad antibacterial activity. The ability of MurB to catalyse the stereo-selective reduction of both E and Z isomers of the substrate is thought to result from the active site architecture restricting free rotation around the C2-C3 bond, and slowing the rate relative to reprotonation. Structural data show the functional groups thought to be involved in the hydride transfer to C3 and protonation at C2 of the enol-ether substrate are arranged anti relative to the enol-double bond. From this information, the stereochemical outcome was predicted to yield a 2R,3R-dideuterio product. This product was later identified using chemical synthetic analysis and comparative NMR.	Defined by 3 residues: ARG:A-159SER:A-229GLU:A-325 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.1.1.158 (PDB Primary Data) Search M-CSA Motif + EC 1.1.1.158

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.