Current biological judgments belong in the review YAML. The source archive retains the 17 original QuickGO contexts, source and sequence provenance, historical row joins, and literal ancestral assertions. The inherited archive preserves the complete earlier review and journal. The source archive deliberately does not repeat current annotation reviews, reference assessments or core functions.
Genuine native acquisition is complete. All 17 original contexts were reconciled with the actual 16-column export and native parser, preserving the inherited review order and restoring nine missing donor fields. The normal source inventory contains 29 files: 11 unchanged files from the base commit and 18 missing-only acquisitions. It includes the additionally qualified UniProt pathway dependency R-HSA-3282872. The four added publication titles and the core excerpt were checked against the native caches. The review's 18 manually assessed references are a narrower set than this acquisition inventory; cache availability does not expand the original reading scope stated below.
PMID:30626647 / PMC6347702 provides the principal direct mechanism. Selected Results, Discussion and construct Methods establish human G6PC3-mediated 1,5-anhydroglucitol 6-phosphate hydrolysis, a catalytic H167A control, and metabolite accumulation in deficient human cells. Human HEK293T membrane preparations were used, not purified protein. Human HAP1 cells, mouse neutrophil models, rat microsomal transport assays and patient neutrophils are separate experimental systems; the human G6PC3 patient sample was one individual. G6PC3 performs the hydrolysis and SLC37A4 supplies transport. Neutrophil consequences do not establish a separate apoptosis-regulator activity. The exact seven-word core excerpt comes from the Results concluding paragraph on joint dephosphorylation; its original XML and passage offsets are recorded in the source archive. Native-cache verification and precise locators are recorded in the source archive.
PMID:39548727 / PMC11788743 reports additional sugar-phosphate hydrolysis using recombinant human GFP-G6PC3 in HEK-cell lysates with empty-vector background. Rat microsomal transport and HL-60 differentiation are distinct experiments. The Table 1 and Discussion assignments of fructose-6-phosphate versus mannose-6-phosphate Km values disagree; those numbers do not support a physiological substrate ranking here. Selected main-text passages were read, not every figure image or supplementary assay.
PMID:14718531(https://pubmed.ncbi.nlm.nih.gov/14718531/) was read as an authentic complete abstract. It identifies G6Pase-beta's covalent His167 intermediate and luminal catalytic residues in a nine-transmembrane ER protein. The abstract does not specify construct species; human attribution comes from the current human GOA and target identity. Original Methods were not recovered. PMID:25492228 / PMC4794745 was read in selected original Methods and Results, including human wild-type and variant expression in COS-1 cells, supplied glucose-6-phosphate, mock controls and protein measurements. These experiments establish catalytic capability and variant effects without identifying the dominant physiological substrate.
Glucose-6-phosphate hydrolysis is represented as a second core molecular activity because direct human biochemical and mutant-control experiments corroborate the conserved catalytic assignment. This does not equate biochemical capability with physiological dominance. The 2019 study explicitly favors a different physiological substrate after comparing human recombinant proteins and rat tissue microsomes (Fig. 1 and the Results substrate-spectrum section); it also measures transport-dependent G6P hydrolysis in rat muscle microsomes. The 2025 study demonstrates G6P accessibility using rat liver microsomes and leaves the physiological significance of additional substrate reactions unresolved in its Conclusions. These experiments do not quantify human G6PC3-dependent flux or justify adding a gluconeogenesis core. The specific 1,5AG6P detoxification core and its proposed molecular-function term remain unchanged.
The single authored cellular-detoxification assertion is recorded separately from the 17 incoming annotations. Its rationale and both core molecular activities remain in the review YAML. The accepted participation, same-role comparator and typed-ontology checks distinguish direct detoxifying hydrolysis from indirect neutrophil consequences; narrower metabolite-repair terminology remains a question because a useful role for the dephosphorylated product is unresolved.
PMID:15661744(https://pubmed.ncbi.nlm.nih.gov/15661744/) provides authentic abstract support for a mouse astrocyte G6PC3/G6PT glucose-production system. PMID:4303362(https://pubmed.ncbi.nlm.nih.gov/4303362/) concerns developing rat kidney metabolism; its abstract does not resolve the molecular phosphatase isoenzyme. Both complete original Methods remain unrecovered. These source limits are distinct from the independently established human catalytic activity.
The actual PTHR12591 tree and alignment place the exact 346-residue human Q9BUM1 sequence at AN106/PTN002488969. All four incoming IBA contexts descend from AN0/PTN000971890 (Eumetazoa). Their literal IBD lines, donor order and target/donor ancestry are retained. Target self-donors represent experimental grounding and are not circular transfer. No family label is used to infer substrate priority.
The official normal reaction R-HSA-3262512 explicitly identifies the G6PC3 ER membrane catalyst and its Gluconeogenesis parent. R-HSA-3282876 models defective variants and links the normal reaction; its title is not a negation of wild-type activity. The retained R-HSA-70263 summary names Gluconeogenesis. Its fresh direct web request returned 404, while the official child reaction independently resolves target membership. Pathway membership alone does not quantify net human tissue flux.
PMID:19946888(https://pubmed.ncbi.nlm.nih.gov/19946888/) was read as an authentic abstract of YTS membrane proteomics. Its G6PC3-specific peptide table was not independently recovered. The GO_REF method records document phylogenetic, ortholog, location and combined electronic provenance; the individual HPA target images were not independently inspected. Detailed manual assessments are maintained in the YAML references rather than reproduced here.
PMID:12370122(https://pubmed.ncbi.nlm.nih.gov/12370122/) supports broad human UGRP/G6PC3 expression by RNA blot. Its early negative glucose-6-phosphate assay remains explicitly distinguished from later direct catalytic results. PMID:19118303 / PMC2778311 provides human segregation, recombinant wild-type/R253H experiments and patient-cell reconstitution supporting disease causation. Selected Methods and Results were read, including the variable cardiac, urogenital and venous features. PMID:22050868(https://pubmed.ncbi.nlm.nih.gov/22050868/) extends the clinical spectrum in a selected syndromic-neutropenia cohort; its complete abstract was read, not the full Methods. These sources support the expression and disease summary without assigning separate developmental or apoptosis-regulator functions.
The core now names the specific 1,5-anhydro-D-glucitol-6-phosphate phosphatase reaction through the proposed-term mechanism, with phosphatase activity as its proposed parent. This avoids inventing a GO identifier or allowing a broad substrate class to obscure the physiological reaction. The existing glucose-6-phosphatase capabilities and all other annotation judgments are unchanged. The broader sugar-phosphatase terms describe real substrate-class capabilities; they are not rejected as chemically impossible for polyols.
The inherited archive keeps all 23 quotation associations with their original review locations. Thirteen match the retained source bytes and ten do not; these are historical associations, not 13 independent experiments. Matching a substring does not by itself establish target-specific support. In particular, the global YTS proteome count does not verify a G6PC3 peptide, and the older glucose-production interpretation does not establish physiological substrate priority. Three focused excerpts now support the experimental catalytic rows and cellular-detoxification assertion, alongside the original core excerpt. Each is independently checked against the unchanged native source; the complete historical text remains unchanged.
The official sequence is Q9BUM1, 346 residues, identical to the inherited record. No alternative product is declared in the retained UniProt record; this does not establish the absence of every unrecorded biological product. The source archive preserves the sequence and exact original fields, including all null values. The source archive records the actual 17-row bijection. The separate authored cellular-detoxification assertion follows the original 17 rows; it is not represented as a native GOA row.