Annotations: 6KMA

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	OxoGdeHyase_C	e6kmaA1	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: OxoGdeHyase_C	ECOD (1.6)
A	E1_dh	e6kmaA2	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: E1_dh	ECOD (1.6)
A	Transket_pyr	e6kmaA3	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: Transket_pyr	ECOD (1.6)
B	OxoGdeHyase_C	e6kmaB2	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: OxoGdeHyase_C	ECOD (1.6)
B	E1_dh	e6kmaB3	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: E1_dh	ECOD (1.6)
B	Transket_pyr	e6kmaB1	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: Transket_pyr	ECOD (1.6)
C	OxoGdeHyase_C	e6kmaC3	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: OxoGdeHyase_C	ECOD (1.6)
C	E1_dh	e6kmaC2	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: E1_dh	ECOD (1.6)
C	Transket_pyr	e6kmaC1	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: Transket_pyr	ECOD (1.6)
D	OxoGdeHyase_C	e6kmaD3	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: OxoGdeHyase_C	ECOD (1.6)
D	E1_dh	e6kmaD1	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: E1_dh	ECOD (1.6)
D	Transket_pyr	e6kmaD2	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: Transket_pyr	ECOD (1.6)

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	PF16870	2-oxoglutarate dehydrogenase C-terminal (OxoGdeHyase_C)	2-oxoglutarate dehydrogenase C-terminal	-	Family
A, B, C, D	PF00676	Dehydrogenase E1 component (E1_dh)	Dehydrogenase E1 component	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component	oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxoglutarate dehydrogenase (succinyl-transferring) activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding vitamin binding thiamine pyrophosphate binding organic cyclic compound binding anion binding oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxoglutarate dehydrogenase (succinyl-transferring) activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding vitamin binding thiamine pyrophosphate binding organic cyclic compound binding anion binding quaternary ammonium group binding heterocyclic compound binding sulfur compound binding	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex oxoglutarate dehydrogenase complex catalytic complex oxidoreductase complex tricarboxylic acid cycle heteromeric enzyme complex alpha-ketoacid dehydrogenase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR042179	Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR029061	Thiamin diphosphate-binding fold	Homologous Superfamily
A, B, C, D	IPR032106	2-oxoglutarate dehydrogenase E1 component, N-terminal domain	Domain
A, B, C, D	IPR005475	Transketolase-like, pyrimidine-binding domain	Domain
A, B, C, D	IPR011603	2-oxoglutarate dehydrogenase E1 component	Family
A, B, C, D	IPR031717	2-oxoglutarate dehydrogenase E1 component/KDG, C-terminal	Domain
A, B, C, D	IPR001017	Dehydrogenase, E1 component	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.