3C2E

Crystal structure at 1.9A of the apo quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
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	QRPTase_N	e3c2eA1	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Nicotinate/Quinolinate PRTase N-terminal domain-like	F: QRPTase_N	ECOD (1.6)
A	QRPTase_C	e3c2eA2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02749	Quinolinate phosphoribosyl transferase, N-terminal domain (QRPTase_N)	Quinolinate phosphoribosyl transferase, N-terminal domain	Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid with 5-phosphoribosyl ...	Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide [1,2]. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The N-terminal domain has an alpha/beta hammerhead fold.	Domain
A	PF01729	Quinolinate phosphoribosyl transferase, C-terminal domain (QRPTase_C)	Quinolinate phosphoribosyl transferase, C-terminal domain	Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid with 5-phosphoribosyl ...	Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide [1,2]. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The C-terminal domain has a 7 beta-stranded TIM barrel-like fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Nicotinate-nucleotide pyrophosphorylase	pentosyltransferase activity glycosyltransferase activity nicotinate-nucleotide diphosphorylase (carboxylating) activity transferase activity catalytic activity	oxoacid metabolic process nucleotide biosynthetic process indole-containing compound metabolic process amino acid metabolic process organic acid metabolic process NAD metabolic process alpha-amino acid metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process 'de novo' NAD biosynthetic process phosphate-containing compound metabolic process indolalkylamine metabolic process oxoacid metabolic process nucleotide biosynthetic process indole-containing compound metabolic process amino acid metabolic process organic acid metabolic process NAD metabolic process alpha-amino acid metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process 'de novo' NAD biosynthetic process phosphate-containing compound metabolic process indolalkylamine metabolic process pyridine-containing compound metabolic process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process NAD biosynthetic process pyridine nucleotide biosynthetic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process cellular metabolic process pyridine-containing compound biosynthetic process carboxylic acid metabolic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process tryptophan metabolic process L-amino acid metabolic process purine-containing compound metabolic process nicotinamide nucleotide biosynthetic process proteinogenic amino acid metabolic process amine metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process 'de novo' NAD biosynthetic process from tryptophan biogenic amine metabolic process purine nucleotide biosynthetic process quinolinate metabolic process catabolic process dicarboxylic acid metabolic process dicarboxylic acid catabolic process organic acid catabolic process cellular catabolic process quinolinate catabolic process carboxylic acid catabolic process small molecule catabolic process pyridine-containing compound catabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR022412	Quinolinate phosphoribosyl transferase, N-terminal	Domain
A	IPR037128	Quinolinate phosphoribosyl transferase, N-terminal domain superfamily	Homologous Superfamily
A	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A	IPR004393	Nicotinate-nucleotide pyrophosphorylase	Family
A	IPR002638	Quinolinate phosphoribosyl transferase, C-terminal	Domain
A	IPR027277	Nicotinate-nucleotide pyrophosphorylase/Putative pyrophosphorylase ModD	Family
A	IPR036068	Nicotinate phosphoribosyltransferase-like, C-terminal	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	nicotinate-nucleotide pyrophosphorylase (carboxylating) (type II) M-CSA #945	This is a type II Quinolinic acid phosphoribosyltransferase (QAPRTase). This protein is required for the de novo biosynthesis of NAD in both prokaryotes and eukaryotes. The enzyme catalyses the reaction between quinolinic acid (QA) and 5-phosphoribosyl-1-pyrophosphate (PRPP), to yield nicotinic acid mononucleotide (NAMN), pyrophosphate and CO₂, the latter resulting from decarboxylation at position 2 of the quinolinate ring. QAPRTase has been grouped with nine other enzymes, (phosphoribosyltransferases, PRTases) that catalyse chemically similar phosphoribosyl transfer reactions using the substrate PRPP. The PRTases are involved in de novo and salvage reactions of nucleotide synthesis, as well as in histidine and tryptophan biosynthesis. Type II enzymes lack the type I PRPP-binding motif and have TIM barrel-like structure [PMID:9016724].	Defined by 1 residue: LYS:A-143 [auth A-144] \| Explore in 3D: M-CSA Motif Definition At least 2 residues must be present to support Structure Motif searching. EC: 2.4.2.19 (PDB Primary Data)

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.