Literature summary for 6.2.1.73 extracted from

Zhang, C.; Kong, L.; Liu, Q.; Lei, X.; Zhu, T.; Yin, J.; Lin, B.; Deng, Z.; You, D.
In vitro characterization of echinomycin biosynthesis formation and hydroxylation of L-tryptophanyl-S-enzyme and oxidation of (2S,3S) beta-hydroxytryptophan (2013), PLoS ONE, 8, e56772 .

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Organism

Organism	UniProt	Comment	Textmining
Streptomyces griseovariabilis subsp. bandungensis	G9JKM4	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phospholipoprotein	cytalytic activity of Qui18 requires phosphopantetheinylating its peptidyl carrier domain	Streptomyces griseovariabilis subsp. bandungensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(L-tryptophyl)adenylate + holo-[L-tryptophyl-carrier protein Qui18]	-	Streptomyces griseovariabilis subsp. bandungensis	AMP + L-tryptophyl-[L-tryptophyl-carrier protein Qui18]	-	?
ATP + L-tryptophan + holo-[L-tryptophyl-carrier protein Qui18]	-	Streptomyces griseovariabilis subsp. bandungensis	AMP + diphosphate + -L-tryptophyl-[L-tryptophyl-carrier protein Qui18]	-	?
ATP + tryptophan	-	Streptomyces griseovariabilis subsp. bandungensis	diphosphate + (L-tryptophyl)adenylate	-	?
additional information	no substrates: D-tryptophan or L-phenylalanine	Streptomyces griseovariabilis subsp. bandungensis	?	-	-

Subunits

Subunits	Comment	Organism
?	x * 64496, mass spectrometry, Qui18 without phosphopantetheinylation	Streptomyces griseovariabilis subsp. bandungensis

Synonyms

Synonyms	Comment	Organism
Qui18	-	Streptomyces griseovariabilis subsp. bandungensis

General Information

General Information	Comment	Organism
physiological function	during biosynthesis of echinomycin, the beginning precursor, L-tryptophan is loaded onto non-ribosomal peptide synthase protein Qui18, which contains both adenylation and PCP domains. The adenylation domain activates L-tryptophan by adenylation and subsequently catalyzes the formation of a thioester bond between the carbonyl group of adenylated tryptophan and the thiol group of phosphopantetheine on PCP domain and thereby loading tryptophan onto the PCP domain of Qui18 to form tryptophanyl-S-Qui18. Enzyme Qui18 interacts with MbtH-like protein Qui5. Two subunits of Qui5 and two subunits of Qui18 form a hetero-tetramer	Streptomyces griseovariabilis subsp. bandungensis

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Release 2023.1 (January 2023)