Literature summary for 2.7.7.9 extracted from

Medeot, D.B.; Romina Rivero, M.; Cendoya, E.; Contreras-Moreira, B.; Rossi, F.A.; Fischer, S.E.; Becker, A.; Jofre, E.
Sinorhizobium meliloti low molecular mass phosphotyrosine phosphatase SMc02309 modifies activity of the UDP-glucose pyrophosphorylase ExoN involved in succinoglycan biosynthesis (2016), Microbiology, 162, 552-563.

Search for more literature for 2.7.7.9

Organism

Organism	UniProt	Comment	Textmining
Sinorhizobium meliloti	-	-	-
Sinorhizobium meliloti 2011	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	UDP-glucose diphosphorylase ExoN is phosphorylated at tyrosine residues and constitutes an endogenous substrate of the phosphotyrosine phosphatase SMc02309 protein. The UDP-glucose diphosphorylase activity is modulated by SMc02309-mediated tyrosine dephosphorylation. A mutation in the SMc02309 gene decreases exopolysaccharide I production and delays nodulation on Medicago sativa roots	Sinorhizobium meliloti

Synonyms

Synonyms	Comment	Organism
ExoN	-	Sinorhizobium meliloti

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)