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Literature summary for 5.4.99.25 extracted from

  • Fitzek, E.; Joardar, A.; Gupta, R.; Geisler, M.
    Evolution of eukaryal and archaeal pseudouridine synthase Pus10 (2018), J. Mol. Evol., 86, 77-89 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.99.25

Cloned(Commentary)

Cloned (Comment) Organism
gene PUS10, genotyping, phylogenetic analysis Homo sapiens
gene PUS10, genotyping, phylogenetic analysis Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
tRNA uridine55 Homo sapiens
-
 tRNA pseudouridine55
-
 ?
tRNA uridine55 Methanocaldococcus jannaschii
-
 tRNA pseudouridine55
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q3MIT2
-
-
Methanocaldococcus jannaschii Q60346
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tRNA uridine55
-
 Homo sapiens tRNA pseudouridine55
-
 ?
tRNA uridine55
-
 Methanocaldococcus jannaschii tRNA pseudouridine55
-
 ?

Subunits

Subunits Comment Organism
More homology modeling and structural superimposition, overview Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
More cf. tRNA pseudouridine54 synthase, EC 5.4.99 Homo sapiens
More cf. tRNA pseudouridine54 synthase, EC 5.4.99 Methanocaldococcus jannaschii
pseudouridine synthase
-
 Homo sapiens
pseudouridine synthase
-
 Methanocaldococcus jannaschii
pseudouridine synthase Pus10
-
 Homo sapiens
pseudouridine synthase Pus10
-
 Methanocaldococcus jannaschii
PSI synthase
-
 Homo sapiens
PSI synthase
-
 Methanocaldococcus jannaschii
Pus10
-
 Homo sapiens
Pus10
-
 Methanocaldococcus jannaschii

General Information

General Information Comment Organism
evolution in archaea, pseudouridine (Psi) synthase Pus10 modifies uridine (U) to Psi at positions 54 and 55 of tRNA. Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m5U54) and TruB (U55 to Psi55). Many eukaryotes have an apparent redundancy, their genomes contain orthologues of archaeal Pus10 and bacterial TrmA and TruB. Eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes. Pus10 is found in earlier evolutionary branches of fungi (such as chytrid Batrachochytrium) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). Examination of 116 archaeal and eukaryotic Pus10 protein sequences reveals that Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. Functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages. The enzyme is a member of the pseudouridine synthase superfamily with a similar three-dimensional structure and a conserved catalytic Asp. In the catalytic region, five amino acids (Asp275, Tyr339, Ile412, Lys413, Leu440 in Methanocalcoccus jannaschii) are conserved throughout all pseudouridine synthase families Homo sapiens
evolution in archaea, pseudouridine (Psi) synthase Pus10 modifies uridine (U) to Psi at positions 54 and 55 of tRNA. Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m5U54) and TruB (U55 to Psi55). Many eukaryotes have an apparent redundancy, their genomes contain orthologues of archaeal Pus10 and bacterial TrmA and TruB. Eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes. Pus10 is found in earlier evolutionary branches of fungi (such as chytrid Batrachochytrium) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). Examination of 116 archaeal and eukaryotic Pus10 protein sequences reveals that Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. Functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages. The enzyme is a member of the pseudouridine synthase superfamily with a similar three-dimensional structure and a conserved catalytic Asp. In the catalytic region, five amino acids (Asp275, Tyr339, Ile412, Lys413, Leu440 in Methanocalcoccus jannaschii) are conserved throughout all pseudouridine synthase families Methanocaldococcus jannaschii
additional information homology modeling and structural superimposition using the crystal structure of Homo sapiens enzyme Pus10, PDB ID 2V9K, as a template, overview Methanocaldococcus jannaschii
additional information the human enzyme crystal structure, PDB ID 2V9K, is modelled onto the structure of Methanocalcoccus jannaschii Homo sapiens
physiological function human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand Homo sapiens