id: Pfam:PF01958
pfam_id: PF01958
name: Aspartate dehydrogenase, C-terminal
short_name: Asp_DH_C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01958
counters:
  proteins: 3184
  matches: 3195
  proteomes: 2698
  taxa: 5585
  structures: 3
  alphafold_models: 2258
  domain_architectures: 31
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR002811
description: This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a
  unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found
  to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta
  domain [[cite:PUB00014412]]. Enzymatic characterisation of TM1643 revealed that it possesses NAD or
  NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity [[cite:PUB00014412]].
  Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases,
  including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH [[cite:PUB00014412]].
  It has been proposed that in Thermotoga maritima, TM1643 catalyses the first reaction of de novo biosynthesis
  of NAD from aspartate, and it produces iminoaspartate required for this pathway.