Information on EC 5.4.99.12 - tRNA pseudouridine38-40 synthase:
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Specific data for protein or organism
This record set is specific for: Agaricus bisporus
UniProt-Accession: P31115
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The enzyme appears in selected viruses and cellular organisms

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EC NUMBERCOMMENTARY
5.4.99.12-

RECOMMENDED NAMEGeneOntology No.
tRNA pseudouridine38-40 synthaseGO:0009982

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
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REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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PATHWAYKEGG LinkMetaCyc Link
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SYSTEMATIC NAMEIUBMB Comments
tRNA-uridine38-40 uracil mutaseThe uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine. TruA specifically modifies uridines at positions 38, 39, and/or 40 in the anticodon stem loop of tRNAs with highly divergent sequences and structures [1].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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CAS REGISTRY NUMBERCOMMENTARY
430429-15-5-
61506-89-6-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
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GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
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NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
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COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
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METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
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INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
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ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
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KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
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TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
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kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
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Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
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IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
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pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
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pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
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pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
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LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
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PDBSCOPCATHORGANISM
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MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
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SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
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POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
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Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
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pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
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TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
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GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
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ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
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OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
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STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
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Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
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Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
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EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
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ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
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APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
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REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE

LINKS TO OTHER DATABASES (specific for EC-Number 5.4.99.12)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)