Annotations: 3S0C

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3s0ca_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Aldolase	Class I aldolase	automated matches	(Thermoplasma acidophilum DSM 1728 ) [TaxId: 273075 ],	SCOPe (2.08)
B	d3s0cb_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Aldolase	Class I aldolase	automated matches	(Thermoplasma acidophilum DSM 1728 ) [TaxId: 273075 ],	SCOPe (2.08)
D	d3s0cd_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Aldolase	Class I aldolase	automated matches	(Thermoplasma acidophilum DSM 1728 ) [TaxId: 273075 ],	SCOPe (2.08)
E	d3s0ce_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Aldolase	Class I aldolase	automated matches	(Thermoplasma acidophilum DSM 1728 ) [TaxId: 273075 ],	SCOPe (2.08)
C	d3s0cc_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Aldolase	Class I aldolase	automated matches	(Thermoplasma acidophilum DSM 1728 ) [TaxId: 273075 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Aldolase	8083234	3000445	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Aldolase	8083234	3000445	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Aldolase	8083234	3000445	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Aldolase	8083234	3000445	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Aldolase	8083234	3000445	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	TAL_FSA	e3s0cA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TAL_FSA	ECOD (1.6)
B	TAL_FSA	e3s0cB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TAL_FSA	ECOD (1.6)
D	TAL_FSA	e3s0cD1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TAL_FSA	ECOD (1.6)
E	TAL_FSA	e3s0cE1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TAL_FSA	ECOD (1.6)
C	TAL_FSA	e3s0cC1	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)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
B	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
D	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
E	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
C	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, C, D, E	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, C, D, E	Probable transaldolase	transketolase or transaldolase activity transaldolase activity transferase activity catalytic activity lyase activity carbon-carbon lyase activity aldehyde-lyase activity	carbohydrate metabolic process primary metabolic process metabolic process cellular process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process carbohydrate derivative metabolic process generation of precursor metabolites and energy glucose 6-phosphate metabolic process nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration carbohydrate metabolic process primary metabolic process metabolic process cellular process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process carbohydrate derivative metabolic process generation of precursor metabolites and energy glucose 6-phosphate metabolic process nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration purine nucleotide metabolic process organophosphate 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	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR004731	Transaldolase type 3B/Fructose-6-phosphate aldolase	Family
A, B, C, D, E	IPR022999	Transaldolase type 3B, putative	Family
A, B, C, D, E	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B, C, D, E	IPR018225	Transaldolase, active site	Active Site
A, B, C, D, E	IPR033919	Transaldolase/Fructose-6-phosphate aldolase, archaeal/bacterial	Family
A, B, C, D, E	IPR001585	Transaldolase/Fructose-6-phosphate aldolase	Family

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.