1YTD

Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum, Native Structure

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ytda1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Nicotinate/Quinolinate PRTase C-terminal domain-like	NadC C-terminal domain-like	Nicotinate phosphoribosyltransferase Ta1145	(Thermoplasma acidophilum DSM 1728 ) [TaxId: 273075 ],	SCOPe (2.08)
A	d1ytda2	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	Nicotinate/Quinolinate PRTase N-terminal domain-like	NadC N-terminal domain-like	Nicotinate phosphoribosyltransferase Ta1145	(Thermoplasma acidophilum DSM 1728 ) [TaxId: 273075 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	NadC C-terminal domain-like	8022483	4003327	SCOP2 (2022-06-29)
A	SCOP2 Family	NadC N-terminal domain-like	8022485	4001131	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nicotinate/Quinolinate PRTase C-terminal domain-like	8034863	3000603	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nicotinate/Quinolinate PRTase N-terminal domain-like	8034865	3000867	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)
A	QRPTase_N_1	e1ytdA2	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_1	ECOD (1.6)
A	NAPRTase_1	e1ytdA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: NAPRTase_1	ECOD (1.6)
A	DUF1922_like	e1ytdA3	A: few secondary structure elements	X: Rubredoxin-like	H: Nicotinate phosphoribosyltransferase C-terminal domain-related (From Topology)	T: Nicotinate phosphoribosyltransferase C-terminal domain-related	F: DUF1922_like	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 phosphoribosyltransferase from Thermoplasma acidophilum	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding pentosyltransferase activity glycosyltransferase activity nicotinate-nucleotide diphosphorylase (carboxylating) activity transferase activity catalytic activity nicotinate phosphoribosyltransferase activity ligase activity, forming carbon-nitrogen bonds ligase activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding pentosyltransferase activity glycosyltransferase activity nicotinate-nucleotide diphosphorylase (carboxylating) activity transferase activity catalytic activity nicotinate phosphoribosyltransferase activity ligase activity, forming carbon-nitrogen bonds ligase activity cation binding ion binding metal ion binding	nucleotide biosynthetic process NAD metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound 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 nucleotide biosynthetic process NAD metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound 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 cellular metabolic process pyridine-containing compound biosynthetic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process nicotinamide nucleotide biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process purine nucleotide biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR022412	Quinolinate phosphoribosyl transferase, N-terminal	Domain
A	IPR007229	Nicotinate phosphoribosyltransferase family	Family
A	IPR037128	Quinolinate phosphoribosyl transferase, N-terminal domain superfamily	Homologous Superfamily
A	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A	IPR053190	Nicotinate phosphoribosyltransferase-like	Family
A	IPR035809	Nicotinate phosphoribosyltransferase, archaeal-type	Family
A	IPR002638	Quinolinate phosphoribosyl transferase, C-terminal	Domain
A	IPR036068	Nicotinate phosphoribosyltransferase-like, C-terminal	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.