Literature summary for 2.8.1.B3 extracted from

Bender, R.
The danger of annotation by analogy: Most thiI genes play no role in thiamine biosynthesis (2011), J. Bacteriol., 193, 4574-4575.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Escherichia coli	three domains of ThiI are essential for the thiolation of tRNA: a THUMP domain that binds tRNA, an AANH domain that activates the uridine residue by adenylylation, and a rhodanese domain that transfers sulfur to the activated uridine residue. Only the rhodanese domain of the ThiI protein is required for a key thiolation reaction in the synthesis of thiamine, while the other two domains (THUMP and AANH) are dispensable	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	three domains of ThiI are essential for the thiolation of tRNA: a THUMP domain that binds tRNA, an AANH domain that activates the uridine residue by adenylylation, and a rhodanese domain that transfers sulfur to the activated uridine residue. Only the rhodanese domain of the ThiI protein is required for a key thiolation reaction in the synthesis of thiamine, while the other two domains (THUMP and AANH) are dispensable	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
ThiI	-	Escherichia coli

General Information

General Information	Comment	Organism
malfunction	thiI mutants are auxotrophic for thiamine, specifically for the thiazole component of this essential vitamin	Escherichia coli

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Release 2023.1 (January 2023)