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1o4u

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    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 1o4u 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 + prpp + quln --> co2 + nicrnt + ppi
    Classification: EC:2.4.2.19
     

    Ligand Information
    Ligands
    Metals

    Jmol

     

    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

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