Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
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Combined evidence from InterPro, RHEA, EC number, UniRule, and UniPathway supports thiamine-phosphate kinase activity and thiamine diphosphate biosynthetic process annotations.
Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.
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MJ0028 (thiL) was identified as part of the complete M. jannaschii genome sequence. Only 38% of predicted proteins could be assigned a putative function with high confidence.
"A total of 1738 predicted protein-coding genes were identified; however, only a minority of these (38 percent) could be assigned a putative cellular role with high confidence."
Structural studies of thiamin monophosphate kinase in complex with substrates and products.
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Crystal structures of A. aeolicus ThiL with AMP-PCP/TMP (substrates) and ADP/TPP (products) established the direct in-line phosphoryl transfer mechanism, distinguishing ThiL from other PurM superfamily members that use phosphorylated enzyme intermediates.
"The results suggest that AaThiL utilizes a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate."
Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.
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High-resolution structures of A. baumannii ThiL confirm the in-line attack mechanism and reveal plasticity in active-site metal identity, though magnesium is preferred for the transferred phosphate groups.
"The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site."
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ThiL is essential for A. baumannii growth and is a potential antimicrobial target.
"the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate"
thiK and thiL loci of Escherichia coli.
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Original identification and naming of the thiL gene in E. coli, encoding thiamine monophosphate kinase activity. Mutants lacking ThiL respond only to thiamine pyrophosphate, not thiamine monophosphate.
"the latter lacks thiamine monophosphate kinase activity"
ThiN as a versatile domain of transcriptional repressors and catalytic enzymes of thiamine biosynthesis.
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Archaeal thiamine biosynthesis is regulated by a transcriptional repressor ThiR (not a riboswitch), and uses a chimeric pathway with eukaryote-like Thi4 and bacterium-like ThiC components.
"thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch"
From suicide enzyme to catalyst -- the iron-dependent sulfide transfer in Methanococcus jannaschii thiamin thiazole biosynthesis.
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The M. jannaschii Thi4 ortholog uses exogenous sulfide and is catalytic (multiple turnover), unlike the yeast Thi4p which is a suicide enzyme. This establishes the upstream thiazole synthesis pathway feeding into ThiL.
"the Thi4 ortholog from Methanococcus jannaschii uses exogenous sulfide and is catalytic"
Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms.
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Comparative genomics analysis reveals that archaea, eubacteria, and eukaryota have different pathways for HMP and thiazole biosynthesis, but the terminal ThiL step (TMP to TPP) is broadly conserved.
"eubacteria, archaea, and eukaryota have different pathways for the HMP and hydroxyethylthiazole biosynthesis"