2O1X

1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Deinococcus radiodurans

External Resource: Annotation

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: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PF02780	e2o1xB1	A: a/b three-layered sandwiches	X: TK C-terminal domain-like (From Topology)	H: TK C-terminal domain-like (From Topology)	T: TK C-terminal domain-like	F: PF02780	ECOD (1.6)
B	PF02779	e2o1xB4	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF02779	ECOD (1.6)
B	PF13292	e2o1xB3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF13292	ECOD (1.6)
C	PF02780	e2o1xC2	A: a/b three-layered sandwiches	X: TK C-terminal domain-like (From Topology)	H: TK C-terminal domain-like (From Topology)	T: TK C-terminal domain-like	F: PF02780	ECOD (1.6)
C	PF02779	e2o1xC4	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF02779	ECOD (1.6)
C	PF13292	e2o1xC3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF13292	ECOD (1.6)
A	PF02780	e2o1xA2	A: a/b three-layered sandwiches	X: TK C-terminal domain-like (From Topology)	H: TK C-terminal domain-like (From Topology)	T: TK C-terminal domain-like	F: PF02780	ECOD (1.6)
A	PF02779	e2o1xA6	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF02779	ECOD (1.6)
A	PF13292	e2o1xA5	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF13292	ECOD (1.6)
D	PF02780	e2o1xD1	A: a/b three-layered sandwiches	X: TK C-terminal domain-like (From Topology)	H: TK C-terminal domain-like (From Topology)	T: TK C-terminal domain-like	F: PF02780	ECOD (1.6)
D	PF02779	e2o1xD4	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF02779	ECOD (1.6)
D	PF13292	e2o1xD3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: PF13292	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (4.3.0)
B	3.40.50.920	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (4.3.0)
C	3.40.50.920	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (4.3.0)
A	3.40.50.920	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (4.3.0)
D	3.40.50.920	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02779	Transketolase, pyrimidine binding domain (Transket_pyr)	Transketolase, pyrimidine binding domain	This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.	Domain
A, B, C, D	PF13292	1-deoxy-D-xylulose-5-phosphate synthase (DXP_synthase_N)	1-deoxy-D-xylulose-5-phosphate synthase	-	Family
A, B, C, D	PF02780	Transketolase, C-terminal domain (Transketolase_C)	Transketolase, C-terminal domain	The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	1-deoxy-D-xylulose-5-phosphate synthase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding transketolase or transaldolase activity 1-deoxy-D-xylulose-5-phosphate synthase activity transferase activity catalytic activity vitamin binding thiamine pyrophosphate binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding transketolase or transaldolase activity 1-deoxy-D-xylulose-5-phosphate synthase activity transferase activity catalytic activity vitamin binding thiamine pyrophosphate binding organic cyclic compound binding anion binding quaternary ammonium group binding heterocyclic compound binding sulfur compound binding	cellular biosynthetic process isopentenyl diphosphate biosynthetic process lipid biosynthetic process carbohydrate derivative metabolic process glyceraldehyde-3-phosphate metabolic process phospholipid metabolic process organic substance metabolic process cellular aldehyde metabolic process organic substance biosynthetic process phosphate-containing compound metabolic process phosphorus metabolic process isoprenoid biosynthetic process isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway cellular metabolic process cellular biosynthetic process isopentenyl diphosphate biosynthetic process lipid biosynthetic process carbohydrate derivative metabolic process glyceraldehyde-3-phosphate metabolic process phospholipid metabolic process organic substance metabolic process cellular aldehyde metabolic process organic substance biosynthetic process phosphate-containing compound metabolic process phosphorus metabolic process isoprenoid biosynthetic process isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway cellular metabolic process primary metabolic process phospholipid biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process cellular lipid metabolic process metabolic process cellular process lipid metabolic process isoprenoid metabolic process isopentenyl diphosphate metabolic process terpenoid biosynthetic process terpenoid metabolic process carbohydrate derivative biosynthetic process 1-deoxy-D-xylulose 5-phosphate biosynthetic process 1-deoxy-D-xylulose 5-phosphate metabolic process organic hydroxy compound metabolic process organonitrogen compound biosynthetic process thiamine-containing compound metabolic process vitamin biosynthetic process alcohol metabolic process thiamine metabolic process thiamine biosynthetic process small molecule metabolic process sulfur compound metabolic process pyrimidine-containing compound biosynthetic process primary alcohol biosynthetic process water-soluble vitamin metabolic process pyrimidine-containing compound metabolic process organonitrogen compound metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process vitamin metabolic process organic cyclic compound metabolic process sulfur compound biosynthetic process organic cyclic compound biosynthetic process organic hydroxy compound biosynthetic process alcohol biosynthetic process thiamine-containing compound biosynthetic process primary alcohol metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR005477	Deoxyxylulose-5-phosphate synthase	Family
A, B, C, D	IPR029061	Thiamin diphosphate-binding fold	Homologous Superfamily
A, B, C, D	IPR009014	Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II	Homologous Superfamily
A, B, C, D	IPR005475	Transketolase-like, pyrimidine-binding domain	Domain
A, B, C, D	IPR033248	Transketolase, C-terminal domain	Domain
A, B, C, D	IPR020826	Transketolase binding site	Binding Site

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

Chains	Enzyme Name	Description	Catalytic Residues
A	1-deoxy-D-xylulose 5-phosphate synthase M-CSA #333	1-Deoxy-D-xylulose-5-phosphate synthase (DXS ) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. DXS is found in bacteria (gene:dxs) and plants (gene:CLA1) which catalyses the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP), a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6). DXS is evolutionary related to TK. This reaction is the first and rate limiting step of the mevalonate-independent pathway for the biosynthesis of isopentyl pyrophosphate, a process undertaken only in fungi, algae and bacteria. DXS differs from related thiamine diphosphate dependent enzymes by virtue of its domain arrangement: the active site is not situated on a chain interface, as seen in related enzymes, but instead resides between two domain faces within the same monomer of a homodimeric complex [PMID:17135236].	Defined by 3 residues: LYS:A-289GLU:A-373ARG:A-401 \| Explore in 3D: M-CSA Motif Definition Extent of motif is too large to support Structure Motif searching. EC: 2.2.1.7 (PDB Primary Data)

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 R01GM133198.