4NJK

Crystal Structure of QueE from Burkholderia multivorans in complex with AdoMet, 7-carboxy-7-deazaguanine, and Mg2+

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Fer4_14	e4njkA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Fer4_14	ECOD (1.6)
B	Fer4_14	e4njkB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Fer4_14	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
B	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	7-carboxy-7-deazaguanine synthase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding metal cluster binding lyase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding metal cluster binding lyase activity catalytic activity carbon-nitrogen lyase activity S-adenosyl-L-methionine binding sulfur compound binding	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	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR007197	Radical SAM	Domain
A, B	IPR024924	7-carboxy-7-deazaguanine synthase-like	Family
A, B	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B	IPR030977	7-carboxy-7-deazaguanine synthase, Cx14CxxC-type	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	7-carboxy-7-deazaguanine synthase M-CSA #943	This enzyme is involved in the pathway of 7-cyano-7-deazaquanine (preQ0) biosynthesis and catalyses the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7- carboxy-7-deazaguanine (CDG). Although this step is common to the biosynthetic pathways of all 7-deazapurine-containing compounds the radical SAM enzyme QueE itself is quite variable. This entry represents a variant form in which the three-Cys motif that binds the signature 4Fe-4S cluster takes the form Cx14CxxC, as in Burkholderia multivorans ATCC 17616. The 3D structure of this form has been solved and the mechanism of other QueE proteins is thought to be broadly similar to the one proposed here.	Defined by 8 residues: PHE:A-45 [auth A-25]CYS:A-51 [auth A-31]CYS:A-66 [auth A-46]CYS:A-69 [auth A-49]ASP:A-70 [auth A-50]THR:A-71 [auth A-51]GLU:A-136 [auth A-116]HIS:A-224 [auth A-204] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.3.99.3 (PDB Primary Data) Search M-CSA Motif + EC 4.3.99.3

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.