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Information on EC 2.7.4.34 - GDP-polyphosphate phosphotransferase
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EC Tree
2.7.4.34 GDP-polyphosphate phosphotransferaseIUBMB Comments
Polyphosphate kinase 2, characterized from the bacterium Pseudomonas aeruginosa, uses inorganic polyphosphate as a donor to convert GDP to GTP. The enzyme can also act on ADP (cf. EC 2.7.4.1, ATP-polyphosphate phosphotransferase), but with lower activity. The enzyme has only a trivial activity in the opposite direction (synthesizing polyphosphate from GTP). The GTP that is produced is believed to be consumed by EC 2.7.7.13, mannose-1-phosphate guanylyltransferase, for production of alginate during stationary phase.
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The enzyme appears in viruses and cellular organisms
Synonyms
CJJ81176_0632, DR_0132, FTT_1564, K649_10090, Mrub_2488, MSMEG_0891, PA0141, polyphosphate kinase 2, polyphosphate:GDP phosphotransferase, PPK2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CJJ81176_0632
DR_0132
K649_10090
Mrub_2488
MSMEG_0891
PA0141
polyphosphate kinase 2
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-
-
-
polyphosphate:GDP phosphotransferase
PPK2
Rv3232c
PPK2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + (phosphate)n = GDP + (phosphate)n+1
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
GTP:polyphosphate phosphotransferase
Polyphosphate kinase 2, characterized from the bacterium Pseudomonas aeruginosa, uses inorganic polyphosphate as a donor to convert GDP to GTP. The enzyme can also act on ADP (cf. EC 2.7.4.1, ATP-polyphosphate phosphotransferase), but with lower activity. The enzyme has only a trivial activity in the opposite direction (synthesizing polyphosphate from GTP). The GTP that is produced is believed to be consumed by EC 2.7.7.13, mannose-1-phosphate guanylyltransferase, for production of alginate during stationary phase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + (phosphate)n+1
ATP + (phosphate)n
reaction of EC 2.7.4.1
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r
GDP + (phosphate)n+1
GTP + (phosphate)n
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-
-
r
GDP + (phosphate)n+1
GTP + (phosphate)n
enzyme prefers polyphosphates of 25 to 50 in chain length
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-
r
GDP + (phosphate)n+1
GTP + (phosphate)n
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-
-
r
GDP + (phosphate)n+1
GTP + (phosphate)n
short polyphosphyate chains are preferred, enzyme displays processivity
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-
r
GDP + (phosphate)n+1
GTP + (phosphate)n
short polyphosphyate chains are preferred, enzyme displays processivity
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-
r
GTP + (phosphate)n
GDP + (phosphate)n+1
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-
-
r
GTP + (phosphate)n
GDP + (phosphate)n+1
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-
-
r
GTP + (phosphate)n
GDP + (phosphate)n+1
polyphosphate chains of 15-700 are all effective in synthesis, but P3 is not
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r
additional information
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enzyme catalyzes the phosphorylation of AMP and GMP into ATP and GTP through step-by-step phosphorylation
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-
additional information
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enzyme catalyzes the phosphorylation of AMP and GMP into ATP and GTP through step-by-step phosphorylation
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-
additional information
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enzyme catalyzes the phosphorylation of AMP and GMP into ATP and GTP through step-by-step phosphorylation
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-
additional information
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enzyme is able to use nucleoside diphosphates ADP, GDP, CDP, and UDP
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-
additional information
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enzyme is able to use nucleoside diphosphates ADP, GDP, CDP, and UDP
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-
additional information
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the polyphosphate-driven nucleoside diphosphate kinase synthesis of GTP from GDP is 75fold greater than the polyphosphate synthesis from GTP. GTP and ATP are equally active in polyphosphate synthesis
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-
additional information
?
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the polyphosphate-driven nucleoside diphosphate kinase synthesis of GTP from GDP is 75fold greater than the polyphosphate synthesis from GTP. GTP and ATP are equally active in polyphosphate synthesis
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-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
Mg2+ is favored over Mn2+ by 5fold at optimal concentration of 10 mM
Mn2+
Mg2+ is favored over Mn2+ by 5fold at optimal concentration of 10 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.7.4.1, class III PPK2 enzyme
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
enzyme uses inorganic polyphosphate as a donor to convert GDP to GTP. Polyphosphate chains of 30-50 residues are optimal, those of 15-700 residues can also serve. The rate of polyphosphate utilization is nearly 100fold greater than that of polyphosphate synthesis
metabolism
-
enzyme uses inorganic polyphosphate as a donor to convert GDP to GTP. Polyphosphate chains of 30-50 residues are optimal, those of 15-700 residues can also serve. The rate of polyphosphate utilization is nearly 100fold greater than that of polyphosphate synthesis
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physiological function
a PPK2 mutant strain shows significantly increased sensitivity to a range of antibiotics in a manner independent of the mode of action of the antibiotic
physiological function
PPK2 contributes to Mycobacterium tuberculosis ability to cause disease in guinea pigs. PPK2 mutant-infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild-type-infected guinea pigs at later stages of infection. In comparison to the wild-type strain, the PPK2 mutant strain is more tolerant to isoniazid and impaired for survival in THP-1 macrophages
physiological function
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Ppk2 is required for control of intrabacillary polyphosphate levels and optimal Mycobacterium tuberculosis growth and survival in macrophages and mouse lungs. A Ppk2 insertion mutant has significantly increased polyphosphate content and a 4fold increase in the MIC of isoniazid relative to the wild-type. The mutant shows reduced survival at day 7 in activated and naive J774 macrophages relative to the wild-type. Naive mutant-infected macrophages show increased expression of interleukins IL-2, IL-9, IL-10, IL-12p70, and gamma interferon relative to wild-type-infected macrophages. The mutant exhibits significantly lower lung CFU during acute murine infection
physiological function
PPK2 plays a role in mycobacterial survival under stress. A knockout mutant shows compromised survival under heat or acid stress or hypoxia, and the knockout is associated with reduction in GTP levels. PPK2 interacts with nucleoside diphosphate kinase (Ndk), the interaction requires G74 of PPK2 and 109LET111 of Ndk
physiological function
PPK2 plays a role in mycobacterial survival under stress. A knockout mutant shows compromised survival under heat or acid stress or hypoxia. PPK2 interacts with nucleoside diphosphate kinase (Ndk), the interaction requires G74 of PPK2 and 109LET111 of Ndk
physiological function
the deletion of Ppk2 results in a significant decrease in polyphosphate-dependent GTP synthesis, while displaying an increased intracellular ATP:GTP ratio. The Ppk2 deletion mutant exhibits a significant survival defect under osmotic, nutrient, aerobic, and antimicrobial stresses and displays an enhanced ability to form static biofilms. The mutant is not defective in polyphosphate and ppGpp synthesis. The Ppk2 mutant is significantly attenuated in invasion and intracellular survival within human intestinal epithelial cells as well as in chicken colonization
physiological function
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the deletion of Ppk2 results in a significant decrease in polyphosphate-dependent GTP synthesis, while displaying an increased intracellular ATP:GTP ratio. The Ppk2 deletion mutant exhibits a significant survival defect under osmotic, nutrient, aerobic, and antimicrobial stresses and displays an enhanced ability to form static biofilms. The mutant is not defective in polyphosphate and ppGpp synthesis. The Ppk2 mutant is significantly attenuated in invasion and intracellular survival within human intestinal epithelial cells as well as in chicken colonization
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physiological function
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PPK2 plays a role in mycobacterial survival under stress. A knockout mutant shows compromised survival under heat or acid stress or hypoxia, and the knockout is associated with reduction in GTP levels. PPK2 interacts with nucleoside diphosphate kinase (Ndk), the interaction requires G74 of PPK2 and 109LET111 of Ndk
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physiological function
-
PPK2 contributes to Mycobacterium tuberculosis ability to cause disease in guinea pigs. PPK2 mutant-infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild-type-infected guinea pigs at later stages of infection. In comparison to the wild-type strain, the PPK2 mutant strain is more tolerant to isoniazid and impaired for survival in THP-1 macrophages
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physiological function
-
PPK2 plays a role in mycobacterial survival under stress. A knockout mutant shows compromised survival under heat or acid stress or hypoxia. PPK2 interacts with nucleoside diphosphate kinase (Ndk), the interaction requires G74 of PPK2 and 109LET111 of Ndk
-
physiological function
-
Ppk2 is required for control of intrabacillary polyphosphate levels and optimal Mycobacterium tuberculosis growth and survival in macrophages and mouse lungs. A Ppk2 insertion mutant has significantly increased polyphosphate content and a 4fold increase in the MIC of isoniazid relative to the wild-type. The mutant shows reduced survival at day 7 in activated and naive J774 macrophages relative to the wild-type. Naive mutant-infected macrophages show increased expression of interleukins IL-2, IL-9, IL-10, IL-12p70, and gamma interferon relative to wild-type-infected macrophages. The mutant exhibits significantly lower lung CFU during acute murine infection
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physiological function
-
PPK2 contributes to Mycobacterium tuberculosis ability to cause disease in guinea pigs. PPK2 mutant-infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild-type-infected guinea pigs at later stages of infection. In comparison to the wild-type strain, the PPK2 mutant strain is more tolerant to isoniazid and impaired for survival in THP-1 macrophages
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PK21A_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
357
0
40788
Swiss-Prot
-
A0A0H3PAX2_CAMJJ
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
162
0
18703
TrEMBL
-
PK21_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
283
0
33047
Swiss-Prot
-
PK23_MEIRD
Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21)
267
0
31559
Swiss-Prot
-
PK21_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
295
0
34124
Swiss-Prot
-
Q5NEQ5_FRATT
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
269
0
32082
TrEMBL
-
Q9RY20_DEIRA
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
266
0
30502
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
4 * 44000, SDS-PAGE, 4 * 40786, calculated from sequence
tetramer
-
4 * 44000, SDS-PAGE, 4 * 40786, calculated from sequence
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
sites of autophosphorylation, H115 and H247, as well as G74 are critical for GTP-synthesizing activity
phosphoprotein
-
sites of autophosphorylation, H115 and H247, as well as G74 are critical for GTP-synthesizing activity
-
phosphoprotein
sites of autophosphorylation, H115 and H247, as well as G74 arecritical for GTP-synthesizing activity
phosphoprotein
-
sites of autophosphorylation, H115 and H247, as well as G74 arecritical for GTP-synthesizing activity
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure to 2.23 A resolution, class I PPK2. Comparison with the structure of Meiothermus ruber PKK2, a class III PKK2
structure to 2.23 resolution. The structure consists of a six-stranded parallel beta-sheet surrounded by 12 alpha-helices, with a high degree of similarity to other members of the PPK2 family
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
30 min, 96% loss of activity. With polyphospate present, the activity is fully retained even after 30 min at 50°C
70
stable in the presence of both Mn2+ and polyphosphate but immediately loses its activity in the absence of either Mn2+ or polyphosphate
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of Ppk2 increases in the exponential phase of growth and remains at a steady level up to the stationary phase
expression of Ppk2 increases in the exponential phase of growth and remains at a steadylevel up to the stationary phase
PPK2 appears in the stationary phase of growth and reaches nucleoside diphosphate kinase levels of 5-10% that of the classic nucleoside diphosphate kinase
expression of Ppk2 increases in the exponential phase of growth and remains at a steady level up to the stationary phase
expression of Ppk2 increases in the exponential phase of growth and remains at a steady level up to the stationary phase
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expression of Ppk2 increases in the exponential phase of growth and remains at a steadylevel up to the stationary phase
expression of Ppk2 increases in the exponential phase of growth and remains at a steadylevel up to the stationary phase
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PPK2 appears in the stationary phase of growth and reaches nucleoside diphosphate kinase levels of 5-10% that of the classic nucleoside diphosphate kinase
PPK2 appears in the stationary phase of growth and reaches nucleoside diphosphate kinase levels of 5-10% that of the classic nucleoside diphosphate kinase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Motomura, K.; Hirota, R.; Okada, M.; Ikeda, T.; Ishida, T.; Kuroda, A.
A new subfamily of polyphosphate kinase 2 (class III PPK2) catalyzes both nucleoside monophosphate phosphorylation and nucleoside diphosphate phosphorylation
Appl. Environ. Microbiol.
80
2602-2608
2014
Meiothermus ruber (M9XB82), Meiothermus ruber NBRC 106122 (M9XB82)
brenda
Batten, L.; Parnell, A.; Wells, N.; Murch, A.; Oyston, P.; Roach, P.
Biochemical and structural characterization of polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis
Biosci. Rep.
36
e00294
2016
Francisella tularensis subsp. tularensis (Q5NEQ5)
brenda
Ogawa, M.; Uyeda, A.; Harada, K.; Sato, Y.; Kato, Y.; Watanabe, H.; Honda, K.; Matsuura, T.
Class III polyphosphate kinase 2 enzymes catalyze the pyrophosphorylation of adenosine-5-monophosphate
ChemBioChem
20
2961-2967
2019
Delftia tsuruhatensis (A0A072T2U3), Deinococcus radiodurans (Q9RY20), Deinococcus radiodurans DSM 20539 (Q9RY20)
brenda
Chuang, Y.M.; Belchis, D.A.; Karakousis, P.C.
The polyphosphate kinase gene ppk2 is required for Mycobacterium tuberculosis inorganic polyphosphate regulation and virulence
mBio
4
e00039
2013
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
brenda
Sureka, K.; Sanyal, S.; Basu, J.; Kundu, M.
Polyphosphate kinase 2 a modulator of nucleoside diphosphate kinase activity in mycobacteria
Mol. Microbiol.
74
1187-1197
2009
Mycolicibacterium smegmatis (A0QQV6), Mycobacterium tuberculosis (O05877), Mycolicibacterium smegmatis ATCC 700084 (A0QQV6), Mycobacterium tuberculosis H37Rv (O05877)
brenda
Gangaiah, D.; Liu, Z.; Arcos, J.; Kassem, I.; Sanad, Y.; Torrelles, J.; Rajashekara, G.
Polyphosphate kinase 2 A novel determinant of stress responses and pathogenesis in Campylobacter jejuni
PLoS ONE
5
e12142
2010
Campylobacter jejuni subsp. jejuni (A0A0H3PAX2), Campylobacter jejuni subsp. jejuni 81-176 (A0A0H3PAX2)
brenda
Parnell, A.E.; Mordhorst, S.; Kemper, F.; Giurrandino, M.; Prince, J.P.; Schwarzer, N.J.; Hofer, A.; Wohlwend, D.; Jessen, H.J.; Gerhardt, S.; Einsle, O.; Oyston, P.C.F.; Andexer, J.N.; Roach, P.L.
Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures
Proc. Natl. Acad. Sci. USA
115
3350-3355
2018
Francisella tularensis subsp. tularensis (Q5NEQ5), Francisella tularensis subsp. tularensis Schu 4 (Q5NEQ5)
brenda
Zhang, H.; Ishige, K.; Kornberg, A.
A polyphosphate kinase (PPK2) widely conserved in bacteria
Proc. Natl. Acad. Sci. USA
99
16678-16683
2002
Pseudomonas aeruginosa (Q9I6Z1), Pseudomonas aeruginosa DSM 22644 (Q9I6Z1)
brenda
Ishige, K.; Zhang, H.; Kornberg, A.
Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP
Proc. Natl. Acad. Sci. USA
99
16684-16688
2002
Pseudomonas aeruginosa (Q9I6Z1), Pseudomonas aeruginosa DSM 22644 (Q9I6Z1)
brenda
Singh, M.; Tiwari, P.; Arora, G.; Agarwal, S.; Kidwai, S.; Singh, R.
Establishing Virulence Associated Polyphosphate Kinase 2 as a drug target for Mycobacterium tuberculosis
Sci. Rep.
6
26900
2016
Mycobacterium tuberculosis (O05877), Mycobacterium tuberculosis ATCC 25618 (O05877)
brenda
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