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The Open Protein Structure Annotation Network
PDB Keyword
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1j5p

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution. To be published
    Site JCSG
    PDB Id 1j5p Target Id 283500
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1307,TM1643 Molecular Weight 26638.52 Da.
    Residues 241 Isoelectric Point 7.75
    Sequence mtvliigmgnigkklvelgnfekiyaydriskdipgvvrldefqvpsdvstvvecaspeavkeyslqil knpvnyiiistsafadevfrerffselknsparvffpsgaiggldvlssikdfvknvrietikppkslg ldlkgktvvfegsveeasklfprninvastiglivgfekvkvtivadpamdhnihivrissaignyefk ienipspenpktsmltvysilrtlrnleskiifg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.90 Rfree 0.26
    Matthews' coefficent 2.29 Rfactor 0.224
    Waters 82 Solvent Content 45.90

    Pathway

    Reactions found in Metabolic Reconstruction for TM1643

    Name: L-aspartate oxidase
    Metabolic Subsystem: NAD Metabolism
    Reaction: : asp-L + nad --> h + iasp + nadh
    Classification:
     

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

     The gene TM1643 from Thermotoga maritima encodes an enzyme aspartate dehydrogenase EC:1.4.1.21 COG:COG0136.  The structure of this enzyme has been previously solved PDB:1H2H [Ref].  TM1643 is found in an operon with two other genes that encode enzymes involved in the biosynthesis of NAD.  The structure, 1j5p, contains a N-terminal Rossmann fold domain with a bound NAD(+) cofactor and a C-terminal alpha+beta DUF108 (SCOP). The active site of the enzyme is located at the interface between the two domains.  The enzyme is highly specific for aspartate and does not oxidize the similar amino acids glutamate and asparagine.  Other bacteria use oxidation of glutamate and asparagine as the first steps of de novo NAD biosynthesis.  In contrast, Thermotoga maritima uses NAD as a cofactor in the first step towards the synthesis of NAD ( PSI-SGKB).

    Ligand Summary



    References

    Reviews

    References

     

    1. Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, and Tong L Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J Biol Chem. 2003 Mar 7; 278(10):8804-8 PubMed HubMed doi:10.1074/jbc.M211892200 pmid:12496312.

       


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