| Title | Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution. To be published | | Site | JCSG | | PDB Id | | 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
Name:L-Aspartate
Formula:C4H6NO4
KEGG:
C00049
+
nad
Name:Nicotinamide adenine dinucleotide
Formula:C21H26N7O14P2
KEGG:
C00003
-->
h
Name:H+
Formula:H
KEGG:
C00080
+
iasp
Name:Iminoaspartate
Formula:C4H3NO4
KEGG:
C05840
+
nadh
Name:Nicotinamide adenine dinucleotide - reduced
Formula:C21H27N7O14P2
KEGG:
C00004
Classification: |
| Ligand Information | | Ligands | | | Metals | | | |
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