5JYX

Crystal structure of the covalent thioimide intermediate of the archaeosine synthase QueF-Like

External Resource: Annotation

Domain Annotation: ECOD Classification
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	QueF	e5jyxA1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
B	QueF	e5jyxB1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
C	QueF	e5jyxC1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
D	QueF	e5jyxD1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
E	QueF	e5jyxE1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
F	QueF	e5jyxF1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
G	QueF	e5jyxG1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
H	QueF	e5jyxH1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
I	QueF	e5jyxI1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
J	QueF	e5jyxJ1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
K	QueF	e5jyxK1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
L	QueF	e5jyxL1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
M	QueF	e5jyxM1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
N	QueF	e5jyxN1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)
O	QueF	e5jyxO1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: QueF	ECOD (1.6)

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, I, J, K, L, M, N, O	PF14489	QueF-like protein (QueF)	QueF-like protein	This protein is involved in the biosynthesis of queuosine. In some proteins this domain appears to be fused to Pfam:PF06508.	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, G, H, I, J, K, L, M, N, O	Archeaosine synthase QueF-Like	oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors preQ1 synthase activity oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors catalytic activity transferase activity	carbohydrate derivative biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process carbohydrate derivative metabolic process primary metabolic process ribonucleoside biosynthetic process nucleoside biosynthetic process nucleobase-containing compound biosynthetic process queuosine metabolic process nucleoside metabolic process nucleobase-containing small molecule biosynthetic process nucleobase-containing compound metabolic process queuosine biosynthetic process biosynthetic process carbohydrate derivative biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process carbohydrate derivative metabolic process primary metabolic process ribonucleoside biosynthetic process nucleoside biosynthetic process nucleobase-containing compound biosynthetic process queuosine metabolic process nucleoside metabolic process nucleobase-containing small molecule biosynthetic process nucleobase-containing compound metabolic process queuosine biosynthetic process biosynthetic process nucleobase-containing small molecule metabolic process small molecule metabolic process metabolic process cellular process ribonucleoside metabolic process RNA metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process RNA biosynthetic process nucleic acid biosynthetic process tRNA processing macromolecule metabolic process RNA processing	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O	IPR029500	NADPH-dependent 7-cyano-7-deazaguanine reductase QueF	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O	IPR050084	NADPH-dependent 7-cyano-7-deazaguanine reductase	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O	IPR043133	GTP cyclohydrolase I, C-terminal/NADPH-dependent 7-cyano-7-deazaguanine reductase	Homologous Superfamily

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.