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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Mycoplasma genitalium and UniProt Accession P47449

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.16 protein-serine/threonine phosphatase
IUBMB Comments
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
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This record set is specific for:
Mycoplasma genitalium
UNIPROT: P47449
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The taxonomic range for the selected organisms is: Mycoplasma genitalium
The enzyme appears in selected viruses and cellular organisms
Synonyms
calcineurin, protein phosphatase, pac-1, dusp1, dusp6, serine/threonine phosphatase, pp2ac, ppm1d, phosphoprotein phosphatase, laforin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
serine/threonine protein phosphatase
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3-hydroxy 3-methylglutaryl CoenzymeA reductase phosphatase
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-
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Aspergillus awamori acid protein phosphatase
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-
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BCKDH phosphatase
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-
-
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branched-chain alpha-keto acid dehydrogenase phosphatase
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-
-
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calcineurin
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-
-
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Calcineurin A1
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-
-
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Calcineurin A2
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-
-
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CaM-kinase phosphatase
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-
-
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CaMKPase
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-
-
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casein phosphatase
-
-
-
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DRES10
-
-
-
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Fibroblast growth factor inducible protein 13
-
-
-
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FIN13
-
-
-
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Flap wing protein
-
-
-
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HMG-CoA reductase phosphatase
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-
-
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Magnesium-dependent calcium inhibitable phosphatase
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-
-
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MCPP
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-
-
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Microtubule star protein
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-
-
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phosphatase 2A
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-
-
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phosphatase 2B
-
-
-
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phosphatase C-II
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-
-
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Phosphatase esp1
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-
-
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phosphatase H-II
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-
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phosphatase I
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-
-
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phosphatase IB
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-
-
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phosphatase II
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-
-
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phosphatase III
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-
-
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phosphatase IV
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-
-
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phosphatase SP
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-
-
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phosphoprotein phosphatase
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-
-
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phosphopyruvate dehydrogenase phosphatase
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-
-
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phosphospectrin phosphatase
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-
-
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PK-Pase
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-
-
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polycation modulated (PCM-) phosphatase
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-
-
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PP-1A
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-
-
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PP-1B
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-
-
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PP-1G
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-
-
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PP2A-alpha
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-
-
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PP2A-beta
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-
-
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PP2C
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-
-
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PP2C-alpha
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-
-
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PP2C-beta
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-
-
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PP2C-delta
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-
-
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PP2C-gamma
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-
-
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Pp4
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-
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PP5
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-
-
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PP6
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-
-
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PPEF
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-
-
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PPN
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-
-
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PPT
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-
-
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protein D phosphatase
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-
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protein phosphatase
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Protein phosphatase 1A
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-
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Protein phosphatase 1B
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-
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Protein phosphatase 1C
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Protein phosphatase magnesium-dependent 1 delta
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-
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Protein phosphatase magnesium-dependent 1 gamma
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-
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Protein phosphatase with EF calcium-binding domain
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PSPase
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-
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Retinal degeneration C protein
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-
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Suppressor protein SDS21
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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SYSTEMATIC NAME
IUBMB Comments
protein-serine/threonine-phosphate phosphohydrolase
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
CAS REGISTRY NUMBER
COMMENTARY hide
9025-75-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
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
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
Hanks-type STKs and STPs play an essential role in the regulation of various cellular processes, by reversibly phosphorylating many protein targets, among them several regulatory proteins of other signaling cascades. High complexity of bacterial regulatory network, in which the crosstalk between STK/STP signaling enzymes, components of bacterial two-component systems (TCSs), and the translational machinery occurs. Physiological processes regulated by bacterial Hanks-type STKs and STPs in different bacteria, overview
physiological function
reversible phosphorylation is a key mechanism that enables bacteria to sense and respond to changing environmental conditions. Alternative regulatory pathways controlled by Hanks-type serine/threonine kinases (STKs) and serine/threonine phosphatases (STPs) play an essential role in regulation of many different processes in bacteria, such as growth and cell division, cell wall biosynthesis, sporulation, biofilm formation, stress response, metabolic and developmental processes, as well as interactions (either pathogenic or symbiotic) with higher host organisms. The corresponding kinase to enzyme MG_207 is kinase MG_109. Enzyme MG_207 is a PPM phosphatase involved in cell signaling and virulence
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Janczarek, M.; Vinardell, J.M.; Lipa, P.; Karas, M.
Hanks-type Serine/threonine protein kinases and phosphatases in bacteria roles in signaling and adaptation to various environments
Int. J. Mol. Sci.
19
2872-2901
2018
Streptococcus pneumoniae, Enterococcus faecium, Streptococcus mutans, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 (P37979), Pseudomonas aeruginosa (A0A072ZI21), Pseudomonas aeruginosa (Q9I757), Bacillus anthracis (A0A0F7RDQ4), Mycoplasma pneumoniae (A0A0H3DJW0), Bacillus subtilis (O34779), Bacillus subtilis (P37475), Mycoplasma genitalium (P47449), Escherichia coli (P55798), Mycobacterium tuberculosis (P9WHW5), Myxococcus xanthus (Q1D1H4), Rhizobium leguminosarum bv. viciae (Q1MCQ2), Mycoplasmopsis synoviae (Q4A6S8), Streptococcus pyogenes serotype M6 (Q5XAP6), Streptococcus agalactiae (Q8VQA1), Listeria monocytogenes serotype 1/2a (Q8Y678), Nostoc sp. PCC 7120 = FACHB-418 (Q8YW58), Staphylococcus aureus (Q9RL81), Pseudomonas aeruginosa ATCC 15692 (Q9I757), Bacillus subtilis 168 (O34779), Bacillus subtilis 168 (P37475), Mycoplasma pneumoniae FH (A0A0H3DJW0), Myxococcus xanthus DK 1622 (Q1D1H4), Mycoplasma genitalium NCTC 10195 (P47449), Mycoplasma pneumoniae NBRC 14401 (A0A0H3DJW0), Pseudomonas aeruginosa 1C (Q9I757), Synechocystis sp. PCC 6803 Kasuza (P37979), Mycoplasma genitalium ATCC 33530 (P47449), Mycoplasma pneumoniae ATCC 15531 (A0A0H3DJW0), Pseudomonas aeruginosa PRS 101 (Q9I757), Mycoplasma pneumoniae DSM 22911 (A0A0H3DJW0), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y678), Pseudomonas aeruginosa DSM 22644 (Q9I757), Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576 (Q8YW58), Pseudomonas aeruginosa CIP 104116 (Q9I757), Pseudomonas aeruginosa LMG 12228 (Q9I757), Mycobacterium tuberculosis H37Rv (P9WHW5), Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82 (Q8YW58), Streptococcus pyogenes serotype M6 ATCC BAA-946 (Q5XAP6), Mycoplasmopsis synoviae 53 (Q4A6S8), Mycoplasma genitalium G-37 (P47449), Listeria monocytogenes serotype 1/2a EGD-e (Q8Y678), Pseudomonas aeruginosa JCM 14847 (Q9I757), Mycoplasma pneumoniae NCTC 10119 (A0A0H3DJW0)
Manually annotated by BRENDA team