id: P52209
gene_symbol: PGD
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: 6-phosphogluconate dehydrogenase (decarboxylating; EC 1.1.1.44) is the third
  enzyme and the second NADPH-producing step of the oxidative branch of the pentose phosphate
  pathway. It catalyses the oxidative decarboxylation of 6-phospho-D-gluconate to
  D-ribulose-5-phosphate and CO2, reducing NADP+ to NADPH. The enzyme is a cytosolic
  homodimer with a shared NADP-binding site between subunits. Its product ribulose-5-phosphate
  feeds the non-oxidative branch of the pathway, ultimately supplying ribose-5-phosphate for
  nucleotide biosynthesis, while the NADPH it generates supports reductive biosynthesis and
  cellular antioxidant defence.
alternative_products:
- name: '1'
  id: P52209-1
- name: '2'
  id: P52209-2
  sequence_note: VSP_055767
existing_annotations:
- term:
    id: GO:0004616
    label: phosphogluconate dehydrogenase (decarboxylating) activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Phylogenetic (PAN-GO) inference of the diagnostic catalytic activity of PGD,
      the third oxidative-PPP enzyme (EC 1.1.1.44). This is the core molecular function and
      is directly supported by biochemical and structural work on the human enzyme.
    action: ACCEPT
    reason: Correct core molecular function, confirmed by direct experimental evidence on
      human PGD and by the UniProt catalytic-activity record.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "Catalyzes the oxidative decarboxylation of 6-phosphogluconate"
    - reference_id: PMID:3965621
      supporting_text: "6-Phosphogluconate dehydrogenase has been purified from human brain"
- term:
    id: GO:0009051
    label: pentose-phosphate shunt, oxidative branch
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetic inference that PGD acts in the oxidative branch of the pentose
      phosphate pathway. PGD is the terminal (third) enzyme of this branch, generating
      ribulose-5-phosphate + CO2 + NADPH.
    action: ACCEPT
    reason: Correct core biological process; PGD is definitionally an oxidative-PPP enzyme.
    supported_by:
    - reference_id: PMID:31586547
      supporting_text: "The third enzyme in the pathway, 6PGD, converts 6PG to\nribulose-5-phosphate (Ru-5-P) and produces NADPH."
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Phylogenetic inference of cytosolic localization, consistent with UniProt
      subcellular location (Cytoplasm) and with the enzyme's role in cytosolic glucose
      metabolism.
    action: ACCEPT
    reason: PGD is a soluble cytosolic enzyme; localization is correct and represents where
      it functions.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Cytoplasm"
- term:
    id: GO:0050661
    label: NADP binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Phylogenetic inference of NADP binding, a component activity of the enzyme.
      PGD binds NADP+ as cofactor; the crystal structures show an NADP-binding Rossmann
      fold with the dinucleotide shared between dimeric partners.
    action: ACCEPT
    reason: Correct and supported by X-ray structures of human PGD in complex with NADP and
      by UniProt binding-site features. It is a molecular-function component of the
      catalytic activity rather than the diagnostic function itself.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH NADP"
- term:
    id: GO:0004616
    label: phosphogluconate dehydrogenase (decarboxylating) activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Electronic (InterPro/RHEA/EC) assignment of the catalytic activity, mapping
      EC 1.1.1.44 and RHEA:10116 to PGD. Duplicate of the experimentally supported core MF.
    action: ACCEPT
    reason: Correct catalytic activity assignment; consistent with the diagnostic domain
      architecture (6PGD family) and the UniProt EC/RHEA cross-references.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "Reaction=6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2"
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: UniProt keyword/SubCell mapping to cytoplasm. Correct but less specific than
      the cytosol annotations.
    action: ACCEPT
    reason: Consistent with the UniProt subcellular location; cytoplasm is a correct (if
      broader) parent of cytosol.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Cytoplasm"
- term:
    id: GO:0006098
    label: pentose-phosphate shunt
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: Electronic assignment of the pentose phosphate pathway (parent of the oxidative
      branch). Correct but more general than the oxidative-branch term.
    action: ACCEPT
    reason: Accurate parent process; PGD is a PPP enzyme. The more specific oxidative-branch
      term (GO:0009051) captures its precise role.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "PATHWAY: Carbohydrate degradation; pentose phosphate pathway"
- term:
    id: GO:0050661
    label: NADP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Electronic (InterPro IPR006115, 6PGDH_NADP-bd) inference of NADP binding.
      Duplicate of the IBA NADP-binding annotation.
    action: ACCEPT
    reason: Correct cofactor-binding activity, supported by the NADP-binding domain and
      crystal structures of the human enzyme.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "IPR006115; 6PGDH_NADP-bd"
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: is_active_in
  review:
    summary: Ensembl orthology-based transfer of cytosolic localization. Duplicate of the
      IBA/TAS cytosol annotations.
    action: ACCEPT
    reason: Correct cytosolic localization, consistent across evidence lines.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Cytoplasm"
- term:
    id: GO:0006739
    label: NADP+ metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Ensembl orthology transfer reflecting that PGD reduces NADP+ to NADPH during
      catalysis. A general process term consistent with the enzyme's cofactor chemistry.
    action: ACCEPT
    reason: The reaction consumes NADP+ and produces NADPH, so PGD participates in
      NADP+/NADPH metabolism. Broad but not wrong.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "with concomitant reduction of NADP"
- term:
    id: GO:0006740
    label: NADPH regeneration
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Ensembl orthology transfer capturing PGD's role in NADPH production, the second
      NADPH-generating step of the oxidative PPP.
    action: ACCEPT
    reason: PGD generates NADPH, a principal metabolic output of the oxidative PPP,
      supporting reductive biosynthesis and redox homeostasis.
    supported_by:
    - reference_id: PMID:31586547
      supporting_text: "The third enzyme in the pathway, 6PGD, converts 6PG to\nribulose-5-phosphate (Ru-5-P) and produces NADPH."
- term:
    id: GO:0009051
    label: pentose-phosphate shunt, oxidative branch
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: Electronic assignment of oxidative-branch PPP involvement. Duplicate of the IBA
      oxidative-branch annotation and the core process of the gene.
    action: ACCEPT
    reason: Correct core biological process for PGD.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step"
- term:
    id: GO:0019521
    label: D-gluconate metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: UniProt keyword (Gluconate utilization) / Ensembl transfer. PGD's substrate is
      6-phospho-D-gluconate, a phosphorylated gluconate derivative, so this term is a
      keyword-driven generalization of the substrate.
    action: KEEP_AS_NON_CORE
    reason: Not wrong (the substrate is a gluconate phosphate), but "D-gluconate metabolic
      process" is a keyword-derived generalization; the precise role is captured by the
      oxidative-PPP process terms. Retained as non-core.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "Gluconate utilization"
- term:
    id: GO:0030246
    label: carbohydrate binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: Ensembl orthology-transferred generic binding term. This is an uninformative
      reflection of the enzyme binding its phosphosugar substrate rather than a distinct
      lectin-like carbohydrate-binding function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Generic substrate binding is already subsumed by the catalytic activity
      (GO:0004616). Carbohydrate binding implies a lectin-type function that PGD does not
      have; it is an over-annotation of ordinary substrate engagement.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "Reaction=6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2"
- term:
    id: GO:0031406
    label: carboxylic acid binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: Ensembl orthology-transferred generic binding term reflecting that the substrate
      6-phospho-D-gluconate is a carboxylic acid. Not an informative independent molecular
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Redundant with, and less informative than, the catalytic activity; ordinary
      substrate binding should not be annotated as a standalone molecular function.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "Reaction=6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2"
- term:
    id: GO:0004616
    label: phosphogluconate dehydrogenase (decarboxylating) activity
  evidence_type: IDA
  original_reference_id: PMID:23153533
  qualifier: enables
  review:
    summary: Direct assay of recombinant human 6PGD, which converts 6-phosphogluconate to
      ribulose 5-phosphate in the presence of NADP+; the study also determined 6PGD/substrate
      binding and crystallized the human enzyme.
    action: ACCEPT
    reason: Experimental (IDA) confirmation of the core catalytic activity of human PGD.
    supported_by:
    - reference_id: PMID:23153533
      supporting_text: "6-phosphogluconate dehydrogenase (6PGD), an enzyme that also produces NADPH while converting 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP+"
- term:
    id: GO:0004616
    label: phosphogluconate dehydrogenase (decarboxylating) activity
  evidence_type: IDA
  original_reference_id: PMID:3965621
  qualifier: enables
  review:
    summary: Enzyme purified from human brain with defined kinetic mechanism using NADP+ and
      6-phosphogluconate as substrates, releasing CO2, ribulose 5-phosphate and NADPH.
    action: ACCEPT
    reason: Direct experimental (IDA) confirmation of the catalytic activity on the human
      enzyme.
    supported_by:
    - reference_id: PMID:3965621
      supporting_text: "6-Phosphogluconate dehydrogenase has been purified from human brain"
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-71299
  qualifier: located_in
  review:
    summary: Reactome traceable assertion placing PGD's decarboxylation reaction in the
      cytosol. Consistent with all other localization evidence.
    action: ACCEPT
    reason: Correct cytosolic localization from a curated pathway source.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Cytoplasm"
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9761846
  qualifier: located_in
  review:
    summary: Reactome traceable assertion (NFE2L2-dependent PGD gene expression context)
      placing PGD in the cytosol. Duplicate cytosol localization.
    action: ACCEPT
    reason: Correct cytosolic localization from a curated pathway source.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Cytoplasm"
- term:
    id: GO:0009051
    label: pentose-phosphate shunt, oxidative branch
  evidence_type: IMP
  original_reference_id: PMID:31586547
  qualifier: acts_upstream_of_or_within
  review:
    summary: Knockdown of 6PGD reduces oxidative-PPP flux, NADPH/NADP+ ratio and its product
      ribulose-5-phosphate, establishing PGD's functional involvement in the oxidative branch
      of the PPP.
    action: ACCEPT
    reason: Experimental (IMP) support that PGD activity is required for oxidative-PPP output;
      consistent with its identity as the third oxiPPP enzyme.
    supported_by:
    - reference_id: PMID:31586547
      supporting_text: "knockdown of 6PGD resulted in increased\nphosphorylation levels of AMPK and ACC1 in cancer cells"
    - reference_id: PMID:31586547
      supporting_text: "The third enzyme in the pathway, 6PGD, converts 6PG to\nribulose-5-phosphate (Ru-5-P) and produces NADPH."
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:23533145
  qualifier: located_in
  review:
    summary: High-throughput mass-spectrometry detection of PGD in exosomes isolated from
      expressed prostatic secretions in urine (a shotgun proteome of about 900 proteins).
      PGD is an abundant cytosolic enzyme commonly recovered as a passenger in vesicle
      proteomes.
    action: MARK_AS_OVER_ANNOTATED
    reason: Proteomic detection in an exosome preparation does not indicate that extracellular
      exosome is a functional location of this cytosolic housekeeping enzyme; it reflects
      co-purification of an abundant protein. Not core; not removed because the protein was
      genuinely detected.
    supported_by:
    - reference_id: PMID:23533145
      supporting_text: "In pooled EPS-urine exosome samples, ~900 proteins were detected."
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: HDA
  original_reference_id: PMID:21630459
  qualifier: located_in
  review:
    summary: High-throughput detection of PGD among 403 proteins in a purified human sperm
      nucleus proteome. PGD is a soluble cytosolic enzyme with no established nuclear
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Large-scale proteomic identification in a nuclear fraction does not establish a
      biological nuclear localization for this abundant cytosolic enzyme; likely
      co-purification. Retained (not removed) as a genuine detection but flagged as
      over-annotation.
    supported_by:
    - reference_id: PMID:21630459
      supporting_text: "different proteins have been identified from the isolated sperm nuclei"
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:19056867
  qualifier: located_in
  review:
    summary: High-throughput MS detection of PGD in a 1132-protein human urinary exosome
      proteome. Consistent with recovery of an abundant cytosolic enzyme in vesicle preps.
    action: MARK_AS_OVER_ANNOTATED
    reason: Proteomic co-purification, not a functional extracellular-exosome localization
      for this cytosolic enzyme.
    supported_by:
    - reference_id: PMID:19056867
      supporting_text: "analysis identified 1132 proteins unambiguously"
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:20458337
  qualifier: located_in
  review:
    summary: High-throughput MS detection of PGD in a 539-protein B-cell-derived exosome
      proteome. Abundant cytosolic enzyme recovered as an exosomal passenger.
    action: MARK_AS_OVER_ANNOTATED
    reason: Proteomic co-purification, not a functional extracellular-exosome localization.
    supported_by:
    - reference_id: PMID:20458337
      supporting_text: "identified 539 proteins, including known and not"
- term:
    id: GO:0004616
    label: phosphogluconate dehydrogenase (decarboxylating) activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: Sequence-similarity (ISS) transfer of the catalytic activity from an ortholog
      (UniProtKB P00349). Duplicate of the experimentally supported core MF.
    action: ACCEPT
    reason: Correct catalytic activity, redundantly supported by direct experimental evidence
      on the human enzyme.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "Belongs to the 6-phosphogluconate dehydrogenase family"
- term:
    id: GO:0006098
    label: pentose-phosphate shunt
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: Sequence-similarity transfer of PPP involvement. Correct but more general than
      the oxidative-branch term.
    action: ACCEPT
    reason: Accurate parent process; captured more specifically by GO:0009051.
    supported_by:
    - reference_id: file:human/PGD/PGD-uniprot.txt
      supporting_text: "PATHWAY: Carbohydrate degradation; pentose phosphate pathway"
- term:
    id: GO:0009051
    label: pentose-phosphate shunt, oxidative branch
  evidence_type: IDA
  original_reference_id: PMID:3858849
  qualifier: involved_in
  review:
    summary: This IDA on the oxidative-PPP branch cites Beutler et al. 1985, whose abstract
      concerns hereditary deficiency of 6-phosphogluconolactonase (PGLS, EC 3.1.1.31), the
      second oxidative-PPP enzyme, and its interaction with G6PD deficiency, rather than PGD
      itself. The cached record is abstract-only.
    action: UNDECIDED
    reason: PGD's involvement in the oxidative branch of the PPP is well established by other
      annotations, but this specific reference (abstract-only) is about a different oxiPPP
      enzyme (PGLS/6-phosphogluconolactonase), so its support for a PGD annotation cannot be
      verified from the available text. Per policy, not removing an experimental annotation
      whose full text is unavailable; flagged as undecided pending the full text.
    supported_by:
    - reference_id: PMID:3858849
      supporting_text: "Partial deficiency of 6-phosphogluconolactonase (EC 3.1.1.31) of the \nerythrocytes was discovered as an autosomal dominant disorder."
core_functions:
- description: Catalyses the oxidative decarboxylation of 6-phospho-D-gluconate to
    D-ribulose-5-phosphate + CO2 with reduction of NADP+ to NADPH, the third (terminal) and
    second NADPH-producing step of the oxidative pentose phosphate pathway, acting as a
    cytosolic homodimer.
  molecular_function:
    id: GO:0004616
    label: phosphogluconate dehydrogenase (decarboxylating) activity
  directly_involved_in:
  - id: GO:0009051
    label: pentose-phosphate shunt, oxidative branch
  - id: GO:0006740
    label: NADPH regeneration
  locations:
  - id: GO:0005829
    label: cytosol
  substrates:
  - id: CHEBI:58759
    label: 6-phospho-D-gluconate
  supported_by:
  - reference_id: file:human/PGD/PGD-uniprot.txt
    supporting_text: "Catalyzes the oxidative decarboxylation of 6-phosphogluconate"
  - reference_id: PMID:23153533
    supporting_text: "6-phosphogluconate dehydrogenase (6PGD), an enzyme that also produces NADPH while converting 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP+"
  - reference_id: PMID:31586547
    supporting_text: "The third enzyme in the pathway, 6PGD, converts 6PG to\nribulose-5-phosphate (Ru-5-P) and produces NADPH."
references:
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
    by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to
    orthologs using Ensembl Compara
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:human/PGD/PGD-uniprot.txt
  title: UniProtKB entry P52209 (6PGD_HUMAN)
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Primary source for the catalytic activity (EC 1.1.1.44, RHEA:10116),
      cytoplasmic localization, homodimeric structure and pathway membership of human PGD.
- id: PMID:19056867
  title: Large-scale proteomics and phosphoproteomics of urinary exosomes.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Large-scale urinary exosome proteome; supports an HDA extracellular-exosome
      detection of PGD (over-annotation for a cytosolic enzyme), not a functional role.
- id: PMID:20458337
  title: MHC class II-associated proteins in B-cell exosomes and potential functional
    implications for exosome biogenesis.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: B-cell exosome proteome; basis for an HDA extracellular-exosome detection
      of PGD (over-annotation), not a biological localization.
- id: PMID:21630459
  title: Proteomic characterization of the human sperm nucleus.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Sperm-nucleus proteome; basis for an HDA nuclear detection of PGD
      (over-annotation for a cytosolic enzyme).
- id: PMID:23153533
  title: Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote
    tumor growth.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Although titled for PGAM1, the study directly assays and crystallizes human
      6PGD and describes its catalytic activity; supports the IDA on GO:0004616.
- id: PMID:23533145
  title: In-depth proteomic analyses of exosomes isolated from expressed prostatic
    secretions in urine.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Prostatic-secretion exosome proteome; basis for an HDA extracellular-exosome
      detection of PGD (over-annotation), not a functional role.
- id: PMID:31586547
  title: γ-6-Phosphogluconolactone, a Byproduct of the Oxidative Pentose Phosphate
    Pathway, Contributes to AMPK Activation through Inhibition of PP2A.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Defines 6PGD as the third oxiPPP enzyme (6PG to ribulose-5-P + NADPH);
      6PGD knockdown reduces oxiPPP flux/NADPH. Supports oxidative-branch involvement and
      NADPH regeneration.
- id: PMID:3858849
  title: '6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency:
    possible interaction with glucose-6-phosphate dehydrogenase deficiency.'
  findings: []
  reference_review:
    relevance: LOW
    correctness: MISCITED
    review_notes: Cited to support the PGD oxidative-branch IDA, but the abstract concerns
      6-phosphogluconolactonase (PGLS, EC 3.1.1.31), the second oxiPPP enzyme, and its
      interaction with G6PD deficiency, not PGD. Abstract-only; associated annotation left
      UNDECIDED rather than removed.
- id: PMID:3965621
  title: 'Human brain 6-phosphogluconate dehydrogenase: purification and kinetic properties.'
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Purification and kinetic characterization of human 6PGD; supports the IDA
      on GO:0004616.
- id: Reactome:R-HSA-71299
  title: PGD decarboxylates 6-phospho-D-gluconate
  findings: []
- id: Reactome:R-HSA-9761846
  title: NFE2L2-dependent PGD gene expression
  findings: []