4HCY

Structure of a eukaryotic thiaminase-I bound to the thiamin analogue 3-deazathiamin

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF08625	e4hcyA1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: EUF08625	ECOD (1.6)
A	PBP2_Thiaminase_I	e4hcyA2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: PBP2_Thiaminase_I	ECOD (1.6)
B	EUF08625	e4hcyB2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: EUF08625	ECOD (1.6)
B	PBP2_Thiaminase_I	e4hcyB1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: PBP2_Thiaminase_I	ECOD (1.6)
D	EUF08625	e4hcyD1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: EUF08625	ECOD (1.6)
D	PBP2_Thiaminase_I	e4hcyD2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: PBP2_Thiaminase_I	ECOD (1.6)
E	EUF08625	e4hcyE1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: EUF08625	ECOD (1.6)
E	PBP2_Thiaminase_I	e4hcyE2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: PBP2_Thiaminase_I	ECOD (1.6)
F	EUF08625	e4hcyF1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: EUF08625	ECOD (1.6)
F	PBP2_Thiaminase_I	e4hcyF2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: PBP2_Thiaminase_I	ECOD (1.6)
C	EUF08625	e4hcyC1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: EUF08625	ECOD (1.6)
C	PBP2_Thiaminase_I	e4hcyC2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: PBP2_Thiaminase_I	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
A	3.40.190.220	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B	3.40.190.220	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D	3.40.190.220	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
E	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
E	3.40.190.220	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
F	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
F	3.40.190.220	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.40.190.220	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF22156	Thiaminase I-like, N-terminal domain (Thiaminase_I-like_N)	Thiaminase I-like, N-terminal domain	This domain is found at the the N-terminal end of Thiaminase I from the amoeba Naegleria gruberi (Swiss:D2V4Z5) and similar eukaryotic sequences. This enzyme catalyse the elimination of the thiazole ring moiety from thiamin through substitution of th ...	This domain is found at the the N-terminal end of Thiaminase I from the amoeba Naegleria gruberi (Swiss:D2V4Z5) and similar eukaryotic sequences. This enzyme catalyse the elimination of the thiazole ring moiety from thiamin through substitution of the methylene group. This domain has thiaminase I activity by itself. It consists of a seven-stranded beta-sheet surrounded by eight alpha-helices [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	thiaminase-I	transketolase activity transketolase or transaldolase activity transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process carbohydrate derivative metabolic process primary 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 nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process carbohydrate derivative metabolic process primary 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 metabolic process cellular process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR033247	Transketolase family	Family
A, B, C, D, E A, B, C, D, E, F	IPR005474	Transketolase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR029061	Thiamin diphosphate-binding fold	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR009014	Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR049557	Transketolase conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR005478	Transketolase, bacterial-like	Family
A, B, C, D, E A, B, C, D, E, F	IPR054407	Thiaminase I-like, N-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR005475	Transketolase-like, pyrimidine-binding domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR020826	Transketolase binding site	Binding Site

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.