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Information on EC 2.7.1.169 - pantoate kinase for references in articles please use BRENDA:EC2.7.1.169
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EC Tree
IUBMB Comments The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with beta-alanine, followed by phosphorylation (EC 6.3.2.1 and EC 2.7.1.33, respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with beta-alanine.
The enzyme appears in viruses and cellular organisms
Synonyms
mhun_0831, cog1829,
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ATP + (R)-pantoate = ADP + (R)-4-phosphopantoate
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ATP:(R)-pantoate 4-phosphotransferase
The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with beta-alanine, followed by phosphorylation (EC 6.3.2.1 and EC 2.7.1.33, respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with beta-alanine.
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ATP + (R)-pantoate
ADP + (R)-phosphopantoate
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-
-
?
ATP + pantoate
ADP + 4-phosphopantoate
ATP + pantothenate
ADP + 4'-phosphopantothenate
kcat/Km value with pantoate as a substrate is over 7fold higher than that observed with pantothenate
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-
?
CTP + pantoate
CDP + 4-phosphopantoate
-
-
-
-
?
GTP + pantoate
GDP + 4-phosphopantoate
-
-
-
-
?
UTP + (R)-pantoate
UDP + (R)-phosphopantoate
52.7% of the activity with ATP
-
-
?
UTP + pantoate
UDP + 4-phosphopantoate
-
-
-
-
?
additional information
?
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-
enzyme displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable kcat/Km values
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-
-
ATP + pantoate
ADP + 4-phosphopantoate
-
-
-
?
ATP + pantoate
ADP + 4-phosphopantoate
kcat/Km value with pantoate as a substrate is over 7fold higher than that observed with pantothenate
-
-
?
ATP + pantoate
ADP + 4-phosphopantoate
-
reaction displays Michaelis-Menten kinetics toward ATP, whereas substrate inhibition is observed with pantoate
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-
?
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ATP + pantoate
ADP + 4-phosphopantoate
Q5JHF1
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-
?
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Ca2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Co2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Fe2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
K+
-
moderate stimulation, optimum at 10 mM
Mn2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Ni2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Zn2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Mg2+
maximum activity in presence of Mg2+
additional information
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not accepted: Cu2+
additional information
not accepted: Cu2+
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CoA
-
no inhibition in presence of 0.1 mM CoA, activity decrases by 20% in presence of 1 mM CoA
malonyl-CoA
0.2 mM, 83% residual activity
Pantoate
-
substrate inhibition
additional information
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no detectable decrase in activity at 0.1 mM: acetyl-CoA, dephospho-CoA, or 4'-phosphopantothenate
-
additional information
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not inhibitory: CoA, acetyl-CoA
-
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0.32
ATP
-
pH 7.5, 42°C
1.2
Pantoate
-
42°C
2.92
Pantoate
-
pH 7.5, 42°C
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1.48
ATP
-
42°C
1.56
Pantoate
-
42°C
2.82
Pantoate
-
pH 7.5, 42°C
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2.2
ATP
-
pH 7.5, 42°C
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9.75
Pantoate
-
pH 7.5, 42°C
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8 - 9.5
more than 80% of maximum activity
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UniProt
brenda
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UniProt
brenda
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malfunction
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the deletion mutant strain grows well in media supplemented with 1 mM CoA. The deletion mutant strain could not grow at all in the absence of CoA
physiological function
coexpression of genes Mhun_0831 and Mhun_0832 complements the poor growth of the temperature-sensitive Escherichia coli pantothenate kinase mutant ts9. The recombinant Mhun_0831 and Mhun_0832 genes expressed in Escherichia coli cells exhibit pantoate kinase and phosphopantothenate synthetase activities, respectively
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POK_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
270
0
30035
Swiss-Prot
POK_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
300
0
32750
Swiss-Prot
A0A2K5ANK1_9ARCH
322
0
34935
TrEMBL
A0A1V6IPC2_9EURY
295
0
31934
TrEMBL
A0A075HP04_9ARCH
298
0
32359
TrEMBL
A0A075FVN9_9ARCH
299
0
32666
TrEMBL
D3SRF2_NATMM
Natrialba magadii (strain ATCC 43099 / DSM 3394 / CIP 104546 / JCM 8861/ NBRC 102185 / NCIMB 2190 / MS3)
279
0
28522
TrEMBL
D4GT07_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
277
0
27821
TrEMBL
A0A0K1DZU0_9CREN
255
0
27467
TrEMBL
A0A1V5IGA8_9EURY
293
0
30858
TrEMBL
M1XKC6_NATM8
Natronomonas moolapensis (strain DSM 18674 / JCM 14361 / 8.8.11)
273
0
27661
TrEMBL
A0A1V4YT34_9EURY
293
0
31826
TrEMBL
A0A1V5B0M4_9EURY
291
0
30127
TrEMBL
A0A0S1XEM2_9EURY
301
0
33176
TrEMBL
A0A1V5ASW1_9EURY
276
0
28176
TrEMBL
A0A150JJ27_9EURY
295
0
31934
TrEMBL
A0A075IAZ3_9ARCH
298
0
32171
TrEMBL
A0A2Z2HMR8_9ARCH
297
0
32505
TrEMBL
A0A1V4V6K9_9EURY
276
0
28146
TrEMBL
A0A1V5AL84_9EURY
288
0
30034
TrEMBL
A0A1V4TX52_9EURY
288
0
29829
TrEMBL
A0A075GWZ9_9ARCH
298
0
32161
TrEMBL
B0R2Z2_HALS3
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
279
0
26755
TrEMBL
A0A1V4UQN1_9EURY
276
0
28641
TrEMBL
A0A075HJH5_9ARCH
298
0
32242
TrEMBL
A0A1V4ULY0_9EURY
291
0
30182
TrEMBL
A0A1V4YYZ0_9EURY
292
0
30946
TrEMBL
A0A1Q9P927_9ARCH
294
0
32754
TrEMBL
A0A150JCK2_9EURY
295
0
31934
TrEMBL
A0A150JB97_9EURY
296
0
32562
TrEMBL
A0A1V4Z4G3_9EURY
285
0
29706
TrEMBL
A0A075H3C9_9ARCH
299
0
32676
TrEMBL
A0A1V6JDF4_9EURY
280
0
29202
TrEMBL
A0A1M4MSC2_METWO
287
0
30748
TrEMBL
A0A075GJ93_9ARCH
298
0
32288
TrEMBL
A0A1V5ZCY4_9EURY
289
0
30675
TrEMBL
A0A075H0Z9_9ARCH
298
0
32284
TrEMBL
A0A1Q9NUS4_9ARCH
293
0
32082
TrEMBL
A0A1V4V6P5_9EURY
290
0
30084
TrEMBL
A0A150IMD2_9EURY
295
0
32205
TrEMBL
A0A087RMD5_9ARCH
303
0
33360
TrEMBL
A0A1V5B8Z5_9EURY
282
0
28951
TrEMBL
A0A075HTT4_9ARCH
304
0
33125
TrEMBL
A0A1V5S8J4_9EURY
246
0
26524
TrEMBL
A0A2P5K620_9EURY
284
0
29512
TrEMBL
A0A343TI53_9ARCH
265
0
27190
TrEMBL
A0A0B5HR25_ARCG5
281
0
30525
TrEMBL
A0A1V4ZKH9_9EURY
287
0
30488
TrEMBL
A0A075H2M6_9ARCH
298
0
32270
TrEMBL
A0A081S724_9ARCH
303
0
33360
TrEMBL
A0A1V4YDQ0_9EURY
246
0
25694
TrEMBL
A0A1Q9NBF7_9ARCH
303
0
33309
TrEMBL
A0A150J1C6_9EURY
295
0
32205
TrEMBL
A0A1Q9P090_9ARCH
313
0
33510
TrEMBL
A0A0A7LDZ5_9EURY
294
0
31174
TrEMBL
A0A075WHL2_ARCFL
261
0
27794
TrEMBL
A0A128A617_9ARCH
307
0
33635
TrEMBL
A0A343TJ07_9ARCH
284
0
28671
TrEMBL
A0A0F7IEU1_9EURY
270
0
28948
TrEMBL
A0A1V4UAN5_9EURY
288
0
30034
TrEMBL
A0A075GX33_9ARCH
298
0
32319
TrEMBL
A0A075GNK0_9ARCH
304
0
33181
TrEMBL
A0A075MVF0_9ARCH
308
0
32462
TrEMBL
A0A1V5YGT1_9EURY
290
0
30287
TrEMBL
A0A1V5AME3_9EURY
276
0
28609
TrEMBL
A0A075GJR5_9ARCH
298
0
32161
TrEMBL
A0A1V4TDV5_9EURY
286
0
30666
TrEMBL
A0A1V4U6U4_9EURY
288
0
29812
TrEMBL
A0A150J897_9EURY
295
0
32111
TrEMBL
A0A1D8S5M0_9EURY
277
0
28065
TrEMBL
A0A1V4ZDL9_9EURY
288
0
29829
TrEMBL
A0A1V5AMP7_9EURY
290
0
30098
TrEMBL
A0A075H4A5_9ARCH
297
0
32744
TrEMBL
A0A075GQ15_9ARCH
298
0
32288
TrEMBL
A0A1V4TDS9_9EURY
196
0
20723
TrEMBL
G0LHM3_HALWC
Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23)
304
0
31036
TrEMBL
A0A150JP86_9EURY
295
0
31934
TrEMBL
U2DZ49_9EURY
292
0
29845
TrEMBL
A0A366MFG1_9EURY
278
0
28920
TrEMBL
Q18KP4_HALWD
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
304
0
31036
TrEMBL
A0A150IU82_9EURY
295
0
32205
TrEMBL
A0A075HFZ9_9ARCH
298
0
32204
TrEMBL
Q2FUB2_METHJ
Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)
289
0
31027
TrEMBL
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32748
-
2 * 32748, calculated from sequence
34000
-
2 * 34000, SDS-PAGE
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dimer
-
2 * 32748, calculated from sequence; 2 * 34000, SDS-PAGE
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D143
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residue is the base responsible for proton abstraction from the pantoate hydroxy group
E134A
-
residue is involved in binding with Mg2+
H131A
-
residue is involved in pantoate recognition. 77% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
R155A
-
residue is involved in pantoate recognition and plays an important role in catalysis
S104A
-
residue is involved in binding with phosphate
S28A
-
residue is involved in pantoate recognition. 3.7% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
T186A
-
residue is involved in pantoate recognition and plays an important role in catalysis. Thr186 is involved in dimer assambly
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expression in Escherichia coli
expression in Thermococcus kodakarensis
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Yokooji, Y.; Tomita, H.; Atomi, H.; Imanaka, T.
Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the archaea
J. Biol. Chem.
284
28137-28145
2009
Thermococcus kodakarensis (Q5JHF1), Thermococcus kodakarensis
brenda
Tomita, H.; Yokooji, Y.; Ishibashi, T.; Imanaka, T.; Atomi, H.
Biochemical characterization of pantoate kinase, a novel enzyme necessary for coenzyme A biosynthesis in the Archaea
J. Bacteriol.
194
5434-5443
2012
Thermococcus kodakarensis (Q5JHF1), Thermococcus kodakarensis
brenda
Katoh, H.; Tamaki, H.; Tokutake, Y.; Hanada, S.; Chohnan, S.
Identification of pantoate kinase and phosphopantothenate synthetase from Methanospirillum hungatei
J. Biosci. Bioeng.
115
372-376
2013
Methanospirillum hungatei, Methanospirillum hungatei (Q2FUB2)
brenda
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2.7.1.169 pantoate kinase
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