TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
Annotation inferences using phylogenetic trees
The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism.
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Fungal and human UAP1 proteins have directly measured UDP-GlcNAc pyrophosphorylase activity and complement a yeast UAP1 deficiency.
"All the recombinant ScUap1p,
CaUap1p, and HsUap1p possessed UDP-N-acetylglucosamine pyrophosphorylase
activities in vitro."
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The founding UAP1 study establishes the N-acetylglucosamine phosphosugar substrate, distinguishing it from UDP-glucose pyrophosphorylase.
"The yeast Uap1p utilized N-acetylglucosamine-1-phosphate as
the substrate"
A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc.
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Human isoform AGX1, which lacks the 17-residue insert (as does frog uap1.S), is 2-3 times more active with GalNAc-1-P than GlcNAc-1-P, while insert-bearing AGX2 prefers GlcNAc-1-P 8-fold.
"was 2-3 times more active with GalNAc-1-P than with GlcNAc-1-P"
PTHR11952-paint.tsv
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PAINT places an IBD for cytosol (GO:0005829) at the eukaryote-level node PTN000237224, seeded by human UAP1 (Q16222) and Arabidopsis AT5G52560.
"PTHR11952 PTN000237224 GO:0005829 C IBD false AGI_LocusCode:AT5G52560|UniProtKB:Q16222 taxon:2759 20251224"
UniProt record for human UAP1 (Q16222)
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UniProt curates human UAP1 as cytosolic with experimental evidence from PMID:8025165.
"SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8025165}."
uap1.S: exact selected product and human ortholog reference
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The report maps conserved aligned positions between frog uap1.S and human UAP1, but its feature table did not recover the ligand labels for the mapped binding-site rows.
"Reference feature mapping (sequence coverage does not establish retained function):"
uap1.S re-review: Q6DCZ6 vs human UAP1 Q16222
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Q6DCZ6 aligns to human UAP1 over 505 residues with 75.6% identity, conserves all 15 ligand-labelled UDP-HexNAc contact positions, and lacks the human 454-470 segment that is absent from isoform AGX1.
"| 454-470 | in isoform AGX1 | 0 |"
UniProt record identifying the UDP-glucose pyrophosphorylase donor
Frozen exact-input ProtNLM output and UniProt sequence for Q6DCZ6
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.
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Human UAP1 structures establish nucleotide-sugar contacts and isoform-dependent architecture; conservation is mapped explicitly to frog Uap1.S.
"we
have solved the crystal structures of AGX1 and AGX2 in complexes with UDPGlcNAc"
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The active site accommodates both GlcNAc and GalNAc without structural rearrangement, consistent with dual N-acetylhexosamine use.
"The protein accommodates either the GlcNAc or GalNAc moieties without any significant structural rearrangement."
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The insert-lacking AGX1 isoform is mostly dimeric in solution whereas insert-bearing AGX2 is monomeric.
"the majority of AGX1 is dimeric whereas AGX2 is exclusively monomeric"