| Title | Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 A resolution. Proteins 55 768-771 2004 | | Site | JCSG | | PDB Id | | Target Id | 283502 | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1308,TM1645 | Molecular Weight | 30179.27 Da. | | Residues | 273 | Isoelectric Point | 5.08 | | Sequence | mekildllmsfvkedegkldlasfplrnttagahlllktenvvasgievsrmflekmgllskfnvedge ylegtgvigeiegntykllvaertllnvlsvmfsvatttrrfaeklkhakiaatrkilpglgvlqkiav vhgggdphrldlsgcvmikdnhlkmygsaeravqevrkiipfttkievevenledalraveagadivml dnlspeevkdisrrikdinpnvivevsggiteenvslydfetvdvisssrltlqevfvdlsleiqr | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 2 | | Resolution (Å) | 2.50 | Rfree | 0.27225 | | Matthews' coefficent | 3.57 | Rfactor | 0.21295 | | Waters | 113 | Solvent Content | 65.25 |
| Pathway | | Reactions found in Metabolic Reconstruction for TM1645 | Name: nicotinate-nucleotide diphosphorylase (carboxylating) Metabolic Subsystem: NAD Metabolism Reaction: :
h
Name:H+
Formula:H
KEGG:
C00080
+
prpp
Name:5-Phospho-alpha-D-ribose 1-diphosphate
Formula:C5H8O14P3
KEGG:
C00119
+
quln
Name:Quinolinate
Formula:C7H3NO4
KEGG:
C03722
-->
co2
Name:CO2
Formula:CO2
KEGG:
C00011
+
nicrnt
Name:Nicotinate D-ribonucleotide
Formula:C11H12NO9P
KEGG:
C01185
+
ppi
Name:Diphosphate
Formula:HO7P2
KEGG:
C00013
Classification: EC:2.4.2.19 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The TM1645 gene from Thermotoga maritima encodes the NP_229445 protein, a type II quinolic acid phosphoribosyltransferase (QAPRTase, NadC, EC:2.4.2.19, PubMed:15103640), which is an essential enzyme in the NAD+ biosynthetic pathway. This enzyme catalyzes the transfer of a phosphoribosyl moiety from 5-phosphoribosyl-1-pyrophosphate (PRPP) to quinolinic acid (QA), yielding nicotinic acid mononucleotide (NAMN), pyrophosphate and CO2, the last resulting from decarboxylation at position 2 of the quinolinate ring.
The active enzyme exists as a dimer, where each monomer has two domains with different fold. The N-terminal domain (PF02749) has alpha/beta-Hammerhead fold (SCOP sunid:54664) and belongs to the family of quinolinic acid phosphoribosyltransferase N-terminal domain (SCOP sunid: 54676). The C-terminal domain (PF01729) has a TIM beta/alpha-barrel fold (SCOP sunid:51350) and belongs to a superfamily with characteristic incomplete beta/alpha barrel with parallel beta-sheet of 7 strands (Quinolinic acid phosphoribosyltransferase C-terminal domain; SCOP sunid:51690). DALI top hits are with other pyrophosphorylases like PDB:2jbm (Z=30), PDB:2b7n (Z=28), PDB:3l0g (Z=28), PDB:1x1o (Z=28).
Ligand Summary
References