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Information on EC 6.3.2.36 - 4-phosphopantoate-beta-alanine ligase and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JIZ8

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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 [pantoate---beta-alanine ligase] and EC 2.7.1.33 [pantothenate kinase], respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with beta-alanine. The two archaeal enzymes that catalyse this conversion are EC 2.7.1.169, pantoate kinase, and this enzyme.
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Thermococcus kodakarensis
UNIPROT: Q5JIZ8
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The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The enzyme appears in selected viruses and cellular organisms
Synonyms
mhun_0832, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphopantothenate synthetase
-
SYSTEMATIC NAME
IUBMB Comments
(R)-4-phosphopantoate:beta-alanine ligase (AMP-forming)
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 [pantoate---beta-alanine ligase] and EC 2.7.1.33 [pantothenate kinase], respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with beta-alanine. The two archaeal enzymes that catalyse this conversion are EC 2.7.1.169, pantoate kinase, and this enzyme.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + 4-phosphopantoate + beta-alanine
AMP + diphosphate + 4'-phosphopantothenate
show the reaction diagram
additional information
?
-
substrate binding structures, overview
-
-
?
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
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + 4-phosphopantoate + beta-alanine
AMP + diphosphate + 4'-phosphopantothenate
show the reaction diagram
the pantoate kinase/phosphopantothenate synthetase system represents the pathway for 4'-phosphopantothenate biosynthesis in Thermococcus kodakaraensis. The enzymes are necessary for CoA biosynthesis in this organism
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
nuleotide binding structure analysis, modeling, overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the deletion mutant strain grows well in media supplemented with 1 mM CoA. The deletion mutant strain can not grow at all in the absence of CoA
metabolism
the common pathway for coenzyme A biosynthesis which involves two enzymes to convert pantoate to 4'-phosphopantothenate involves two enzymes, pantoate kinase, and phosphopantothenate synthetase (PPS), they are responsible for this conversion in archaea. In archea, In these archaea, pantoate is phosphorylated by PoK to produce 4-phosphopantoate (PPo), and then condensation of PPo and beta-alanine is catalyzed by PPS, generating 4'-phosphopantothenate
physiological function
enzyme PPS catalyzes the ATP-dependent condensation of 4-phosphopantoate and beta-alanine generating 4'-phosphopantothenate
additional information
enzyme structure and substrate binding analysis, structure comparisons, structure-function analysis, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29843
2 * 29843, calculated from sequence
60000
about, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 29843, calculated from sequence
homodimer
2 x 30000, about, sequence calculation
additional information
PPS forms an asymmetric homodimer, in which two monomers composing a dimer, deviated from the exact twofold symmetry, displaying 4°–13° distortion
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified free enzyme, and enzyme in complexes with ATP, and ATP and 4-phosphopantoate, sitting drop vapor diffusion method, for the free enzyme: mixing of 0.001 ml of 20 mg/ml of protein in 50 mM Tris-HC, pH 8.0, and 150 mM NaCl, with 0.001 ml of reservoir solution containing 18-20% PEG 3350, 200 mM ammonium acetate, and 100 mM Bis-Tris, pH 6.5, 20°C, 1 week, method optimization, for the enzyme-ATP-Mg2+ complex: 20 mg/ml protein is incubated for several hours at 4°C in the presence of 10 mM ATP and 10 mM MgCl2, mixing of 0.001 ml protein solution with 0.001 ml of reservoir solution containing 17% PEG 10000, 100 mM ammonium acetate, and 100 mM Bis-Tris, pH 5.5, equilibration with reservoir solution, 20°C, 2 weeks, for the enzyme-ATP-Mg2+-4-phosphopantoate complex, mixing of 0.001 ml of 20 mg/ml of protein in 50 mM Tris-HC, pH 8.0, 150 mM NaCl, mM ATP, 5 mM MgCl2, and 5 mM PPo, with 0.001 ml of reservoir solution containing 50% tacsimate, pH 4.0, 1% PEG 3350, and 100 mM sodium acetate trihydrate, pH 4.5, 4°C, 3 days, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene TK1686, DNA and amino acid sequence determination and analysis, sequence comparisons
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q5JIZ8)
Manually annotated by BRENDA team
Kishimoto, A.; Kita, A.; Ishibashi, T.; Tomita, H.; Yokooji, Y.; Imanaka, T.; Atomi, H.; Miki, K.
Crystal structure of phosphopantothenate synthetase from Thermococcus kodakarensis
Proteins
82
1924-1936
2014
Thermococcus kodakarensis (Q5JIZ8), Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 (Q5JIZ8)
Manually annotated by BRENDA team