1I8T | pdb_00001i8t

STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI

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)
B	d1i8tb1	Alpha and beta proteins (a/b)	Nucleotide-binding domain	Nucleotide-binding domain	UDP-galactopyranose mutase, N-terminal domain	UDP-galactopyranose mutase, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1i8tb2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	UDP-galactopyranose mutase	UDP-galactopyranose mutase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1i8ta1	Alpha and beta proteins (a/b)	Nucleotide-binding domain	Nucleotide-binding domain	UDP-galactopyranose mutase, N-terminal domain	UDP-galactopyranose mutase, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1i8ta2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	UDP-galactopyranose mutase	UDP-galactopyranose mutase	(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)
B	SCOP2B Superfamily	Flavoreductase-like	8056249	3000055	SCOP2B (2022-06-29)
A	SCOP2 Family	UDP-galactopyranose mutase-like	8056248	4000125	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Flavoreductase-like	8056249	3000055	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	GLF	e1i8tB2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GLF	ECOD (1.6)
B	Amino_oxidase_1st	e1i8tB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Nucleotide-binding domain	F: Amino_oxidase_1st	ECOD (1.6)
A	GLF	e1i8tA2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GLF	ECOD (1.6)
A	Amino_oxidase_1st	e1i8tA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Nucleotide-binding domain	F: Amino_oxidase_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03275	UDP-galactopyranose mutase (GLF)	UDP-galactopyranose mutase	-	Family
A, B	PF13450	NAD(P)-binding Rossmann-like domain (NAD_binding_8)	NAD(P)-binding Rossmann-like domain		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	UDP-GALACTOPYRANOSE MUTASE	isomerase activity UDP-galactopyranose mutase activity catalytic activity intramolecular transferase activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity flavin adenine dinucleotide binding nucleoside phosphate binding ion binding anion binding nucleotide binding isomerase activity UDP-galactopyranose mutase activity catalytic activity intramolecular transferase activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity flavin adenine dinucleotide binding nucleoside phosphate binding ion binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	lipopolysaccharide biosynthetic process carbohydrate derivative biosynthetic process carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process liposaccharide metabolic process lipid biosynthetic process carbohydrate derivative metabolic process primary metabolic process macromolecule biosynthetic process lipopolysaccharide metabolic process polysaccharide metabolic process biosynthetic process metabolic process lipopolysaccharide biosynthetic process carbohydrate derivative biosynthetic process carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process liposaccharide metabolic process lipid biosynthetic process carbohydrate derivative metabolic process primary metabolic process macromolecule biosynthetic process lipopolysaccharide metabolic process polysaccharide metabolic process biosynthetic process metabolic process cellular process macromolecule metabolic process lipid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR015899	UDP-galactopyranose mutase, C-terminal	Domain
A, B	IPR004379	UDP-galactopyranose mutase	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
B	UDP-galactopyranose mutase M-CSA #368	UDP-galactopyranose mutase catalyses the ring contraction of a non-reducing sugar via a redox-reaction, transforming UDP-D-galactopyranose to UDP-D-galacto-1,4-furanose. This product (UDP-Galf) is the precursor of the D-galactofuranose (Galf) residues found in bacterial and parasitic cell walls, including those of many pathogens such as Mycobacterium tuberculosis and Trypanosoma cruzi. The mutase enzyme is essential for the viability of mycobacteria and is not found in humans, making it a potential therapeutic target. A novel mechanism involving reduced FAD acting as a nucleophile has been proposed.	Defined by 7 residues: ARG:B-170ARG:B-174ARG:B-247ARG:B-278GLU:B-298TYR:B-346ASP:B-348 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.4.99.9 (PDB Primary Data) Search M-CSA Motif + EC 5.4.99.9

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.