Annotations: 4Y4M

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Thi4/GidA-like	8085330	3000051	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thi4/GidA-like	8085330	3000051	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thi4/GidA-like	8085330	3000051	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thi4/GidA-like	8085330	3000051	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Thi4/GidA-like	8085330	3000051	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Thi4/GidA-like	8085330	3000051	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thi4/GidA-like	8085330	3000051	SCOP2B (2022-06-29)
C	SCOP2 Family	Thi4-like	8085329	4000050	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Thi4/GidA-like	8085330	3000051	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	FAD_binding_3_1st	e4y4mB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
D	FAD_binding_3_1st	e4y4mD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
E	FAD_binding_3_1st	e4y4mE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
F	FAD_binding_3_1st	e4y4mF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
G	FAD_binding_3_1st	e4y4mG1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
H	FAD_binding_3_1st	e4y4mH1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
A	FAD_binding_3_1st	e4y4mA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
C	FAD_binding_3_1st	e4y4mC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
D	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
E	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
F	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
G	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
H	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
C	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	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, G, H	PF01946	Thi4 family (Thi4)	Thi4 family	-	Family

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, G, H	Putative ribose 1,5-bisphosphate isomerase	cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding pentosyltransferase activity glycosyltransferase activity transferase activity catalytic activity	oxazole or thiazole biosynthetic process sulfur compound biosynthetic process biosynthetic process thiazole biosynthetic process oxazole or thiazole metabolic process sulfur compound metabolic process metabolic process cellular process thiazole metabolic process pyrimidine-containing compound metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process thiamine-containing compound metabolic process vitamin biosynthetic process oxazole or thiazole biosynthetic process sulfur compound biosynthetic process biosynthetic process thiazole biosynthetic process oxazole or thiazole metabolic process sulfur compound metabolic process metabolic process cellular process thiazole metabolic process pyrimidine-containing compound metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process thiamine-containing compound metabolic process vitamin biosynthetic process vitamin metabolic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process thiamine diphosphate metabolic process small molecule metabolic process pyrimidine-containing compound biosynthetic process water-soluble vitamin metabolic process phosphorus metabolic process thiamine diphosphate biosynthetic process thiamine-containing compound biosynthetic process organic hydroxy compound metabolic process alcohol metabolic process thiamine metabolic process thiamine biosynthetic process primary alcohol biosynthetic process organic hydroxy compound biosynthetic process alcohol biosynthetic process primary alcohol metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR022828	Thiazole biosynthetic enzyme, prokaryotic	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002922	Thiazole biosynthetic enzyme Thi4 family	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.