5AYY

CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	QRPTase_N	e5ayyA1	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	e5ayyA2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
B	QRPTase_N	e5ayyB1	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)
B	QRPTase_C	e5ayyB2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
C	QRPTase_N	e5ayyC1	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)
C	QRPTase_C	e5ayyC2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
D	QRPTase_N	e5ayyD1	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)
D	QRPTase_C	e5ayyD2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
E	QRPTase_N	e5ayyE2	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)
E	QRPTase_C	e5ayyE1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
F	QRPTase_N	e5ayyF2	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)
F	QRPTase_C	e5ayyF1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
G	QRPTase_N	e5ayyG1	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)
G	QRPTase_C	e5ayyG2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
H	QRPTase_N	e5ayyH2	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)
H	QRPTase_C	e5ayyH1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: QRPTase_C	ECOD (1.6)
I	QRPTase_N	e5ayyI2	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)
I	QRPTase_C	e5ayyI1	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)
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)
G	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
G	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
H	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
H	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
I	3.90.1170.20	Alpha Beta	Alpha-Beta Complex	Aldehyde Oxidoreductase	domain 3	CATH (4.3.0)
I	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, G, H, I	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, B, C, D, E A, B, C, D, E, F, G, H, I	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, B, C, D, E A, B, C, D, E, F, G, H, I	Nicotinate-nucleotide pyrophosphorylase [carboxylating]	pentosyltransferase activity glycosyltransferase activity nicotinate-nucleotide diphosphorylase (carboxylating) activity transferase activity catalytic activity identical protein binding protein binding binding	quinolinate metabolic process catabolic process oxoacid metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process dicarboxylic acid catabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process quinolinate catabolic process carboxylic acid catabolic process pyridine-containing compound metabolic process small molecule metabolic process metabolic process quinolinate metabolic process catabolic process oxoacid metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process dicarboxylic acid catabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process quinolinate catabolic process carboxylic acid catabolic process pyridine-containing compound metabolic process small molecule metabolic process metabolic process cellular process small molecule catabolic process pyridine-containing compound catabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process primary metabolic process nucleotide metabolic process NAD metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleotide biosynthetic process purine-containing compound biosynthetic process NAD biosynthetic process pyridine nucleotide biosynthetic process pyridine-containing compound biosynthetic process nucleobase-containing compound biosynthetic process nicotinamide nucleotide biosynthetic process biosynthetic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process purine nucleotide biosynthetic process	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol protein-containing complex extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex

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	IPR022412	Quinolinate phosphoribosyl transferase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR037128	Quinolinate phosphoribosyl transferase, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR004393	Nicotinate-nucleotide pyrophosphorylase	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR002638	Quinolinate phosphoribosyl transferase, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR027277	Nicotinate-nucleotide pyrophosphorylase/Putative pyrophosphorylase ModD	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR036068	Nicotinate phosphoribosyltransferase-like, C-terminal	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H, I	Pharos: Q15274	breast cancer interstitial cystitis malignant glioma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia subependymal giant cell astrocytoma ductal breast carcinoma in situ invasive ductal breast carcinoma malignant pancreatic neoplasm pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma transitional cell carcinoma glioblastoma malignant ependymoma ovarian cancer breast cancer interstitial cystitis malignant glioma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia subependymal giant cell astrocytoma ductal breast carcinoma in situ invasive ductal breast carcinoma malignant pancreatic neoplasm pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma transitional cell carcinoma glioblastoma malignant ependymoma ovarian cancer pancreatic intraductal papillary-mucinous neoplasm Sjogren syndrome

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.