Summary: Quinolinate phosphoribosyl transferase, N-terminal domain
Quinolinate phosphoribosyl transferase, N-terminal domain Provide feedback
Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:184.108.40.206 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.
Eads JC, Ozturk D, Wexler TB, Grubmeyer C, Sacchettini JC; , Structure 1997;5:47-58.: A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase. PUBMED:9016724 EPMC:9016724
Bhatia R, Calvo KC; , Arch Biochem Biophys 1996;325:270-278.: The sequencing expression, purification, and steady-state kinetic analysis of quinolinate phosphoribosyl transferase from Escherichia coli. PUBMED:8561507 EPMC:8561507
Internal database links
|Similarity to PfamA using HHSearch:||Biotin_lipoyl_2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR022412Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC 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 [PUBMED:9016724, PUBMED:8561507]. Unlike INTERPRO, this domain also includes the molybdenum transport system protein ModD.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||transferase activity, transferring pentosyl groups (GO:0016763)|
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This superfamily contains proteins with a hybrid motif . This motif is embedded in structurally diverse proteins.
The clan contains the following 17 members:Apocytochr_F_C Biotin_lipoyl Biotin_lipoyl_2 Complex1_51K DUF2118 DUF2254 GCV_H HlyD HlyD_2 HlyD_3 NQRA OEP Peptidase_M23 PTS_EIIA_1 PYNP_C QRPTase_N RnfC_N
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Curation and family details
|Seed source:||Pfam-B_2063 (release 4.1)|
|Author:||Bashton M, Bateman A, Griffiths-Jones SR|
|Number in seed:||161|
|Number in full:||3866|
|Average length of the domain:||88.60 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||30.01 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the QRPTase_N domain has been found. There are 80 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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