id: Pfam:PF07005
pfam_id: PF07005
name: Sugar-binding N-terminal domain
short_name: SBD_N
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF07005
counters:
  proteins: 9455
  matches: 9503
  proteomes: 6051
  taxa: 9808
  structures: 7
  alphafold_models: 5748
  domain_architectures: 93
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:IPR010737
description: This is the N-terminal domain found in proteins in a range of Proteobacteria as well as the
  Gram-positive Oceanobacillus iheyensis. Structural analysis of the whole protein indicates the N- and
  C-termini act together to produce a surface into which a threonate-ADP complex is bound, demonstrating
  that a sugar binding site is on the N-terminal domain, and a nucleotide binding site is in the C-terminal
  domain [[cite:PUB00085179]]. There is a critical motif, DDXTG, at approximately residues 22-25. Proteins
  containing this domain have been predicted as kinases. Some members are associated with PdxA2 by physical
  clustering and gene fusion with PdxA2. Some members that are fused with PdxA2 have been shown to be
  involved in L-4-hydroxythreonine (4HT) phosphorylation, part of the alternative pathway to make PLP
  (pyridoxal 5'-phosphate) out of a toxic metabolite, 4HT. However, 4HT phosphorylation might not be the
  main function of this group of proteins. Moreover, some members that are not associated with pdxA2,
  and even one that is associated with pdxA2, have lost 4HT kinase activity [[cite:PUB00083215]]. Functional
  analysis demonstrate that family members include D-Threonate kinases (DtnK), D-Erythronate kinases (DenK)
  and 3-Oxo-tetronate kinases (OtnK) [[cite:PUB00085179]].