id: Q2U1U6
gene_symbol: Q2U1U6
taxon:
  id: NCBITaxon:510516
  label: Aspergillus oryzae
status: COMPLETE
description: >-
  The 134-residue protein has a partial polysaccharide-lyase-like fold assignment. Neither polysaccharide
  catabolism nor O-glycosyl hydrolase activity is established for this short sequence.
source_documents:
  - genes/ASPOR/Q2U1U6/Q2U1U6-uniprot.txt
  - genes/ASPOR/Q2U1U6/Q2U1U6-goa.tsv
  - genes/ASPOR/Q2U1U6/Q2U1U6-hypotheses/prediction-glycoside-hydrolase/openscientist.md
predictions:
  - source_method: ProtNLM2
    source_version: UniProt 2024_06 pilot
    predicted_term:
      id: GO:0000272
      label: polysaccharide catabolic process
    predicted_term_type: GO_BP
    review:
      assessment: UNC
      confidence_score: 1
      summary: >-
        The sole InterPro assignment is the chondroitin-lyase-like structural superfamily IPR008929 in
        a 134-residue sequence. A partial fold assignment does not establish a complete catalytic enzyme
        or its physiological substrate. Polysaccharide catabolism is plausible for some proteins with
        this fold, but the inspected sources contain neither a diagnostic complete enzyme architecture
        nor a target assay. The term is absent from the cached annotations and remains uncertain.
      supported_by:
        - reference_id: file:ASPOR/Q2U1U6/Q2U1U6-uniprot.txt
          supporting_text: >-
            ID   Q2U1U6_ASPOR            Unreviewed;       134 AA. ... DR   InterPro; IPR008929; Chondroitin_lyas.
            ... DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
        - reference_id: file:ASPOR/Q2U1U6/Q2U1U6-hypotheses/prediction-glycoside-hydrolase/openscientist.md
          supporting_text: >-
            No positive evidence for catalysis of any kind.
  - source_method: ProtNLM2
    source_version: UniProt 2024_06 pilot
    predicted_term:
      id: GO:0004553
      label: hydrolase activity, hydrolyzing O-glycosyl compounds
    predicted_term_type: GO_MF
    review:
      assessment: NPI
      confidence_score: 0
      error_type: DOMAIN_ARCHITECTURE_MISMATCH
      summary: >-
        IPR008929 identifies a partial chondroitin/alginate-lyase-like fold in a 134-residue protein,
        not an experimentally demonstrated O-glycosyl hydrolase. The focused report found that the
        only mechanistic lead is a lyase superfamily assignment, not a glycoside hydrolase family, and
        that the match is too short to establish even a complete lyase enzyme. The GO:0004553 molecular-function
        prediction is therefore an off-class transfer from a fragmentary lyase-like fold to a hydrolytic
        activity; the inspected evidence supports leaving molecular function uncharacterized rather than
        adding a lyase replacement.
      supported_by:
        - reference_id: file:ASPOR/Q2U1U6/Q2U1U6-uniprot.txt
          supporting_text: >-
            ID   Q2U1U6_ASPOR            Unreviewed;       134 AA. ... DR   InterPro; IPR008929; Chondroitin_lyas.
            ... DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
        - reference_id: file:ASPOR/Q2U1U6/Q2U1U6-hypotheses/prediction-glycoside-hydrolase/openscientist.md
          supporting_text: >-
            Predicting a **hydrolase** from a **lyase** fold is a category error.
references:
  - id: file:ASPOR/Q2U1U6/Q2U1U6-uniprot.txt
    title: Q2U1U6-uniprot.txt
  - id: file:ASPOR/Q2U1U6/Q2U1U6-hypotheses/prediction-glycoside-hydrolase/openscientist.md
    title: openscientist.md