OpenScientist blinded function-assignment run on GO:0005576 for THI22
SGD locus record THI22/YPR121W
Gene Ontology annotation through association of InterPro records with GO terms
Use of the ND evidence code for Gene Ontology (GO) terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Genetic redundancy and gene fusion in the genome of the Baker's yeast Saccharomyces cerevisiae: functional characterization of a three-member gene family involved in the thiamine biosynthetic pathway.
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Two of the three family members (THI20/YOL055c and THI21/YPL258c) are isofunctional and encode an HMP-P kinase (EC 2.7.4.7) required for the final steps of thiamine biosynthesis; by implication the third member (THI22/YPR121w) is the one for which this activity was not demonstrated.
"We demonstrate that two members are isofunctional and encode a hydroxymethylpyrimidine phosphate (HMP-P) kinase (EC 2.7.4.7), an activity required for the final steps of thiamine biosynthesis"
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Each of the three genes has two distinct domains that correspond to separate prokaryotic genes, consistent with an ancestral gene fusion; the C-terminal domain is not required for HMP-P kinase activity and its function was unresolved.
"the three genes are each composed of two distinct domains, each corresponding to individual genes in prokaryotes, suggesting gene fusion during evolution. The function of the carboxy-terminal part of the proteins is not yet understood, but it is not required for HMP-P kinase activity"
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All three family genes are co-regulated (induced under thiamine limitation).
"Expression of all three genes is regulated in the same way"
THI22 vs THI20 paralog alignment and catalytic-residue conservation (inline analysis)
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THI22 (Q06490) is ~76% identical to the characterized paralog THI20 (Q08224) and retains THI20's HMP substrate-binding Gln, the ribokinase Gly-rich phosphate-binding motif, and the thiaminase-II catalytic nucleophile Cys and proton-donor Glu, so it is not a residue-dead pseudoenzyme.
"All three THI20 functional residues are conserved in THI22"
THI22 deep research report (falcon / Edison Scientific)