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    Table of contents
    1. 1. Topsan Members
    2. 2. Summary

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    Pfam ID: DUF108 PDB: 1j5p_A
    Solved by: JCSG Priority Score: 3.6
    Member of this family is in PDB.
    Co-occurence with annotated domain(s) (no restrictions on number of architectures).
      # sequence matches: 275 # architectures: 4 # taxonomy ids:204
      Top FFAS hit in PDB: "1j5pA, ASPARTATE DEHYDROGENASE" No significant hits in Pfam.
      Top significant hit (PDB90): "1j5pA, oxidoreductase ; crystal structure of aspartate dehydrogenase (tm1643) from thermotoga maritima at 1.9 a resolution "
    CATH: CATH Domain E-value CATH Node
      1j5pA02 3.40E-25 3.30.360.10
    FUNFAM (eval=0 ): L-aspartate dehydrogenase -like
      Publications(s) found: 154
      Publications(s) meeting filtering criteria: 3
    GeneSilico Metaserver: (Login and password: Jamboree)
    PDBBLAST: PDB: 1j5p_A ECC:
    FFAS: PDB: 1j5p_A ECC:
    PRC: PDB: 1j5p_A ECC:
    SPARKS: PDB: 1j5p_A ECC:
    BLASTP: PDB: 2dc1_A SCOP: predicted d.81.1 ECC:
    HHBLITS: PDB: 1j5p_A ECC:
    COMPASS: PDB: 2dc1_A SCOP: predicted d.81.1 ECC:
    COMA: PDB: 1j5p_A ECC:
    CSBLAST: PDB: 1j5p_A ECC:
    HHSEARCH: PDB: 1j5p_A ECC:

    Topsan Members

    Tag pages as 'PF01958' to appear in this list.

    Name Annotation Author(s)
     The gene TM1643 from Thermotoga maritima encodes an enzyme aspartate dehydrogenase EC: COG:COG0136.  The structure of this enzyme has been previously solved PDB:1H2H [Ref].  TM1643 is found i... anton (3 edits)
    pascual (2 edits)
    kellrott (1 edits)


    Pfam family PFAM:PF01958 {Domain of unknown function DUF108} with 223 members in NR database and additional 111 members in the metagenomic datasets is represented in Archaea, Bacteria, and Eukaryota. The first structural representative solved (PDB Id: TOPSAN:1j5p) was subject to FATCAT structural similarity search that indicated similarity to SCOP (v. 1.73) domain SCOP:d1diha2 classified as Fwde/GAPDH domain-like fold. Based on Ligand one can argue that this family is remotely homologous to previously known structures from 'd1diha2' this fold. Based on fold and evidence of homology, ligands one can hypothesize that this family is oxidoreductases, aspartate dehydrogenases




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