8CI0

Maize Transketolase in complex with TPP and hydrolyzed (+)-Cornexistin

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth AAA]	SCOP2B Superfamily	TK C-terminal domain-like	8042481	3000424	SCOP2B (2022-06-29)
A [auth AAA]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8042478	3001790	SCOP2B (2022-06-29)
A [auth AAA]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8042480	3001790	SCOP2B (2022-06-29)
B [auth BBB]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8042480	3001790	SCOP2B (2022-06-29)
B [auth BBB]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8042478	3001790	SCOP2B (2022-06-29)
B [auth BBB]	SCOP2B Superfamily	TK C-terminal domain-like	8042481	3000424	SCOP2B (2022-06-29)
C [auth CCC]	SCOP2B Superfamily	TK C-terminal domain-like	8042481	3000424	SCOP2B (2022-06-29)
C [auth CCC]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8042480	3001790	SCOP2B (2022-06-29)
C [auth CCC]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8042478	3001790	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 [auth AAA]	F_UNCLASSIFIED	e8ci0AAA1	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: F_UNCLASSIFIED	ECOD (1.6)
A [auth AAA]	F_UNCLASSIFIED	e8ci0AAA2	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: F_UNCLASSIFIED	ECOD (1.6)
B [auth BBB]	F_UNCLASSIFIED	e8ci0BBB3	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: F_UNCLASSIFIED	ECOD (1.6)
B [auth BBB]	F_UNCLASSIFIED	e8ci0BBB1	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: F_UNCLASSIFIED	ECOD (1.6)
C [auth CCC]	F_UNCLASSIFIED	e8ci0CCC3	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: F_UNCLASSIFIED	ECOD (1.6)
C [auth CCC]	F_UNCLASSIFIED	e8ci0CCC2	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: F_UNCLASSIFIED	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth AAA], B [auth BBB], C [auth CCC]	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 [auth AAA], B [auth BBB], C [auth CCC]	PF00456	Transketolase, thiamine diphosphate binding domain (Transketolase_N)	Transketolase, thiamine diphosphate binding domain	This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit Swiss:P37941 EC:1.2.4.4. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common ...	This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit Swiss:P37941 EC:1.2.4.4. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.	Domain
A [auth AAA], B [auth BBB], C [auth CCC]	PF22613	Transketolase-like TK C-terminal domain (Transketolase_C_1)	Transketolase-like TK C-terminal domain	This entry represents the C-terminal domain found in transketolase and transketolase-like enzymes [1-5], such as pyruvate dehydrogenase E1 component (OPD1) [4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth AAA], B [auth BBB], C [auth CCC]	Transketolase, chloroplastic	cation binding transition metal ion binding ion binding binding metal ion binding cobalt ion binding small molecule binding calcium ion binding transketolase activity transketolase or transaldolase activity transferase activity catalytic activity manganese ion binding	carbohydrate derivative 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 cellular metabolic process carbohydrate derivative 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 cellular metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process NADPH regeneration organophosphate metabolic process metabolic process cellular process carbohydrate metabolic process photosynthesis carbohydrate biosynthetic process photosynthesis, dark reaction biosynthetic process reductive pentose-phosphate cycle carbon fixation	chloroplast thylakoid membrane membrane-bounded organelle plastid membrane intracellular anatomical structure plastid organelle outer membrane plastid thylakoid membrane plastid thylakoid intracellular organelle organelle envelope bounding membrane of organelle thylakoid plastid envelope chloroplast chloroplast thylakoid membrane membrane-bounded organelle plastid membrane intracellular anatomical structure plastid organelle outer membrane plastid thylakoid membrane plastid thylakoid intracellular organelle organelle envelope bounding membrane of organelle thylakoid plastid envelope chloroplast non-membrane-bounded organelle membrane cellular anatomical entity intracellular membrane-bounded organelle thylakoid membrane organelle chloroplast thylakoid intracellular non-membrane-bounded organelle outer membrane cytoplasm photosynthetic membrane organelle membrane cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth AAA], B [auth BBB], C [auth CCC]	IPR033247	Transketolase family	Family
A [auth AAA], B [auth BBB], C [auth CCC]	IPR005474	Transketolase, N-terminal	Domain
A [auth AAA], B [auth BBB], C [auth CCC]	IPR029061	Thiamin diphosphate-binding fold	Homologous Superfamily
A [auth AAA], B [auth BBB], C [auth CCC]	IPR009014	Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II	Homologous Superfamily
A [auth AAA], B [auth BBB], C [auth CCC]	IPR049557	Transketolase conserved site	Conserved Site
A [auth AAA], B [auth BBB], C [auth CCC]	IPR005478	Transketolase, bacterial-like	Family
A [auth AAA], B [auth BBB], C [auth CCC]	IPR005475	Transketolase-like, pyrimidine-binding domain	Domain

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.