Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.85 - glucosyl-3-phosphoglycerate phosphatase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WIC6

for references in articles please use BRENDA:EC3.1.3.85
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.85 glucosyl-3-phosphoglycerate phosphatase
IUBMB Comments
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity [1,2].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WIC6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
glucosyl-3-phosphoglycerate phosphatase, mtbgpgp, gpgp protein, rv2419c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucosyl-3-phospho-D-glycerate phosphohydrolase
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity [1,2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the protein is involved in the biosynthesis of methylglucose lipopolysaccharides which regulate the biosynthesis of mycolic acid
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of apo-, vanadate-bound, and phosphate-bound MtbGpgP are refined to 1.95 A, 2.3 A and 1.77 A, respectively. Enzyme consists of a single domain made up of a central beta-sheet flanked by alpha-helices on either side. The active site is located in a positively charged cleft situated above the central beta-sheet
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E84Q
mutant shows only 40% of catalytic activity compared to wild-type
H159A
mutation almost completely abolishes catalytic activity
L209E
mutation results in monomeric GpgP, rendering the enzyme incapable of dephosphorylation. Mutation almost completely abolishes catalytic activity
N17A
mutation almost completely abolishes catalytic activity
Q23A
mutant shows only 20% of catalytic activity compared to wild-type
R10A
mutation almost completely abolishes catalytic activity
R60A
mutation almost completely abolishes catalytic activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zheng, Q.; Jiang, D.; Zhang, W.; Zhang, Q.; Zhao, Q.; Jin, J.; Li, X.; Yang, H.; Bartlam, M.; Shaw, N.; Zhou, W.; Rao, Z.
Mechanism of dephosphorylation of glucosyl-3-phosphoglycerate by a histidine phosphatase
J. Biol. Chem.
289
21242-21251
2014
Mycobacterium tuberculosis (P9WIC6), Mycobacterium tuberculosis
Manually annotated by BRENDA team
Uddin, R.; Zahra, N.; Azam, S.
Identification of glucosyl-3-phosphoglycerate phosphatase as a novel drug target against resistant strain of Mycobacterium tuberculosis (XDR1219) by using comparative metabolic pathway approach
Comput. Biol. Chem.
79
91-102
2019
Mycobacterium tuberculosis (P9WIC7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIC7)
Manually annotated by BRENDA team