Literature summary for 2.7.1.225 extracted from

Verstraete, M.M.; Perez-Borrajero, C.; Brown, K.L.; Heinrichs, D.E.; Murphy, M.E.P.
SbnI is a free serine kinase that generates O-phospho-L-serine for staphyloferrin B biosynthesis in Staphylococcus aureus (2018), J. Biol. Chem., 293, 6147-6160 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.5 A resolution. SbnI consists of two domains, and elevated B-factors in domain II are consistent with an open-close reaction mechanism	Staphylococcus aureus

Protein Variants

Protein Variants	Comment	Organism
D58A	active site variant, no catalytic activity	Staphylococcus aureus
E20A	active site variant, no catalytic activity	Staphylococcus aureus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
61000	-	dynamic light scattering	Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-serine	Staphylococcus aureus	-	ADP + O-phospho-L-serine	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	Q2G1M5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-serine	-	Staphylococcus aureus	ADP + O-phospho-L-serine	-	?
additional information	no phosphate acceptors: L-Threonine, x022-oxoglutarate, L-2,3-diaminopropionate, His-Ser dipeptide	Staphylococcus aureus	?	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 30000, calculated from sequence	Staphylococcus aureus

Synonyms

Synonyms	Comment	Organism
SbnI	-	Staphylococcus aureus

General Information

General Information	Comment	Organism
physiological function	enzyme is involved in synthesis of staphyloferrin B, an iron-chelating siderophore in Staphylococcus aureus	Staphylococcus aureus

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Release 2023.1 (January 2023)