1ONR | pdb_00001onr

STRUCTURE OF TRANSALDOLASE B

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	d1onrb_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Aldolase	Class I aldolase	Transaldolase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1onra_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Aldolase	Class I aldolase	Transaldolase	(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	Aldolase	8043556	3000445	SCOP2B (2022-06-29)
A	SCOP2 Family	Class I aldolase	8031178	4003216	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Aldolase	8043556	3000445	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	TAL_FSA	e1onrB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TAL_FSA	ECOD (1.6)
A	TAL_FSA	e1onrA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TAL_FSA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00923	Transaldolase/Fructose-6-phosphate aldolase (TAL_FSA)	Transaldolase/Fructose-6-phosphate aldolase	Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-p ...	Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family[4]. Their protein structures have been revealed[5].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	TRANSALDOLASE B	transketolase or transaldolase activity transaldolase activity transferase activity catalytic activity	carbohydrate metabolic process primary metabolic process metabolic process cellular process carbohydrate derivative metabolic process glyceraldehyde-3-phosphate metabolic process glucose 6-phosphate metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process pentose-phosphate shunt phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process carbohydrate metabolic process primary metabolic process metabolic process cellular process carbohydrate derivative metabolic process glyceraldehyde-3-phosphate metabolic process glucose 6-phosphate metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process pentose-phosphate shunt phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process generation of precursor metabolites and energy nucleotide metabolic process aldehyde metabolic process purine-containing compound metabolic process NADP metabolic process NADPH regeneration organophosphate metabolic process pentose-phosphate shunt, non-oxidative branch	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B	IPR004730	Transaldolase type 1	Family
A, B	IPR018225	Transaldolase, active site	Active Site
A, B	IPR001585	Transaldolase/Fructose-6-phosphate aldolase	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	transaldolase (type I) M-CSA #148	Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). It is important for the balance of metabolites in the pentose-phosphate pathway, and catalyses the reversible transfer of a three-carbon ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate. This enzyme, together with transketolase, provides a link between the glycolytic and pentose-phosphate pathways.	Defined by 5 residues: ASP:A-16 [auth A-17]GLU:A-95 [auth A-96]LYS:A-131 [auth A-132]THR:A-155 [auth A-156]PHE:A-177 [auth A-178] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.2.1.2 (PDB Primary Data) Search M-CSA Motif + EC 2.2.1.2

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.