Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BQRPTase_Ne2b7nB1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Nicotinate/Quinolinate PRTase N-terminal domain-likeF: QRPTase_NECOD (1.6)
BQRPTase_Ce2b7nB2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: QRPTase_CECOD (1.6)
CQRPTase_Ne2b7nC1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Nicotinate/Quinolinate PRTase N-terminal domain-likeF: QRPTase_NECOD (1.6)
CQRPTase_Ce2b7nC2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: QRPTase_CECOD (1.6)
AQRPTase_Ne2b7nA2 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Nicotinate/Quinolinate PRTase N-terminal domain-likeF: QRPTase_NECOD (1.6)
AQRPTase_Ce2b7nA1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: QRPTase_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B3.90.1170.20 Alpha Beta Alpha-Beta Complex Aldehyde Oxidoreductase domain 3CATH (4.3.0)
B3.20.20.70 Alpha Beta Alpha-Beta Barrel TIM Barrel Aldolase class ICATH (4.3.0)
C3.90.1170.20 Alpha Beta Alpha-Beta Complex Aldehyde Oxidoreductase domain 3CATH (4.3.0)
C3.20.20.70 Alpha Beta Alpha-Beta Barrel TIM Barrel Aldolase class ICATH (4.3.0)
A3.90.1170.20 Alpha Beta Alpha-Beta Complex Aldehyde Oxidoreductase domain 3CATH (4.3.0)
A3.20.20.70 Alpha Beta Alpha-Beta Barrel TIM Barrel Aldolase class ICATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C
PF02749Quinolinate phosphoribosyl transferase, N-terminal domain (QRPTase_N)Quinolinate phosphoribosyl transferase, N-terminal domainQuinolinate 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
PF01729Quinolinate phosphoribosyl transferase, C-terminal domain (QRPTase_C)Quinolinate phosphoribosyl transferase, C-terminal domainQuinolinate 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

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C
Probable nicotinate-nucleotide pyrophosphorylase