2I14

Crystal structure of nicotinate-nucleotide pyrophosphorylase from Pyrococcus furiosus

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	d2i14a1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Nicotinate/Quinolinate PRTase C-terminal domain-like	NadC C-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
A	d2i14a2	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	Nicotinate/Quinolinate PRTase N-terminal domain-like	NadC N-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
B	d2i14b1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Nicotinate/Quinolinate PRTase C-terminal domain-like	NadC C-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
B	d2i14b2	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	Nicotinate/Quinolinate PRTase N-terminal domain-like	NadC N-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
C	d2i14c1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Nicotinate/Quinolinate PRTase C-terminal domain-like	NadC C-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
C	d2i14c2	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	Nicotinate/Quinolinate PRTase N-terminal domain-like	NadC N-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
D	d2i14d1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Nicotinate/Quinolinate PRTase C-terminal domain-like	NadC C-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
D	d2i14d2	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	Nicotinate/Quinolinate PRTase N-terminal domain-like	NadC N-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
E	d2i14e1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Nicotinate/Quinolinate PRTase C-terminal domain-like	NadC C-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
E	d2i14e2	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	Nicotinate/Quinolinate PRTase N-terminal domain-like	NadC N-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
F	d2i14f1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Nicotinate/Quinolinate PRTase C-terminal domain-like	NadC C-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
F	d2i14f2	Alpha and beta proteins (a+b)	alpha/beta-Hammerhead	Nicotinate/Quinolinate PRTase N-terminal domain-like	NadC N-terminal domain-like	Nicotinate-nucleotide pyrophosphorylase PF1904	(Pyrococcus furiosus ) [TaxId: 2261 ],	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	8030180	4003327	SCOP2 (2022-06-29)
A	SCOP2 Family	NadC N-terminal domain-like	8030183	4001131	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nicotinate/Quinolinate PRTase C-terminal domain-like	8042559	3000603	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nicotinate/Quinolinate PRTase N-terminal domain-like	8042562	3000867	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase C-terminal domain-like	8042559	3000603	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase N-terminal domain-like	8042562	3000867	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase N-terminal domain-like	8042562	3000867	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase C-terminal domain-like	8042559	3000603	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase C-terminal domain-like	8042559	3000603	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase N-terminal domain-like	8042562	3000867	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase C-terminal domain-like	8042559	3000603	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase N-terminal domain-like	8042562	3000867	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase C-terminal domain-like	8042559	3000603	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Nicotinate/Quinolinate PRTase N-terminal domain-like	8042562	3000867	SCOP2B (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	PF02749	e2i14A4	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: PF02749	ECOD (1.6)
A	PF01729	e2i14A3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01729	ECOD (1.6)
A	PF17956	e2i14A2	A: few secondary structure elements	X: Rubredoxin-like	H: Zinc-binding domain in CopZ (From Topology)	T: Zinc-binding domain in CopZ	F: PF17956	ECOD (1.6)
B	PF02749	e2i14B4	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: PF02749	ECOD (1.6)
B	PF01729	e2i14B3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01729	ECOD (1.6)
B	PF17956	e2i14B2	A: few secondary structure elements	X: Rubredoxin-like	H: Zinc-binding domain in CopZ (From Topology)	T: Zinc-binding domain in CopZ	F: PF17956	ECOD (1.6)
C	PF02749	e2i14C4	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: PF02749	ECOD (1.6)
C	PF01729	e2i14C3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01729	ECOD (1.6)
C	PF17956	e2i14C2	A: few secondary structure elements	X: Rubredoxin-like	H: Zinc-binding domain in CopZ (From Topology)	T: Zinc-binding domain in CopZ	F: PF17956	ECOD (1.6)
D	PF02749	e2i14D4	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: PF02749	ECOD (1.6)
D	PF01729	e2i14D3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01729	ECOD (1.6)
D	PF17956	e2i14D2	A: few secondary structure elements	X: Rubredoxin-like	H: Zinc-binding domain in CopZ (From Topology)	T: Zinc-binding domain in CopZ	F: PF17956	ECOD (1.6)
E	PF02749	e2i14E4	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: PF02749	ECOD (1.6)
E	PF01729	e2i14E3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01729	ECOD (1.6)
E	PF17956	e2i14E2	A: few secondary structure elements	X: Rubredoxin-like	H: Zinc-binding domain in CopZ (From Topology)	T: Zinc-binding domain in CopZ	F: PF17956	ECOD (1.6)
F	PF02749	e2i14F4	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: PF02749	ECOD (1.6)
F	PF01729	e2i14F3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01729	ECOD (1.6)
F	PF17956	e2i14F2	A: few secondary structure elements	X: Rubredoxin-like	H: Zinc-binding domain in CopZ (From Topology)	T: Zinc-binding domain in CopZ	F: PF17956	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)
B	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
B	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
C	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
C	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
D	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
D	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
E	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
E	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
F	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
F	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, B, C, D, E A, B, C, D, E, F	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
A, B, C, D, E A, B, C, D, E, F	PF17956	Nicotinate phosphoribosyltransferase C-terminal domain (NAPRTase_C)	Nicotinate phosphoribosyltransferase C-terminal domain	This domain is found at the C-terminus of some Nicotinate phosphoribosyltransferase enzymes. The function of this domain is uncertain.	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	Nicotinate-nucleotide pyrophosphorylase	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 binding metal ion binding small molecule binding	nucleotide biosynthetic process organonitrogen compound biosynthetic process NAD metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process organic substance biosynthetic process pyridine-containing compound metabolic process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleotide biosynthetic process organonitrogen compound biosynthetic process NAD metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process organic substance biosynthetic 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 organonitrogen compound 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 organic cyclic compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound 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, B, C, D, E A, B, C, D, E, F	IPR007229	Nicotinate phosphoribosyltransferase family	Family
A, B, C, D, E A, B, C, D, E, F	IPR041619	Nicotinate phosphoribosyltransferase C-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR035809	Nicotinate phosphoribosyltransferase, archaeal-type	Family
A, B, C, D, E A, B, C, D, E, F	IPR037128	Quinolinate phosphoribosyl transferase, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR002638	Quinolinate phosphoribosyl transferase, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	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 R01GM133198.