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Information on EC 6.3.2.36 - 4-phosphopantoate-beta-alanine ligase and Organism(s) Methanospirillum hungatei JF-1 and UniProt Accession Q2FUA9

for references in articles please use BRENDA:EC6.3.2.36
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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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Methanospirillum hungatei JF-1
UNIPROT: Q2FUA9
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The taxonomic range for the selected organisms is: Methanospirillum hungatei JF-1
The enzyme appears in selected viruses and cellular organisms
Synonyms
mhun_0832, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphopantothenate synthetase
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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
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?
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
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q2FUA9), Methanospirillum hungatei, Methanospirillum hungatei JF-1 (Q2FUA9)
Manually annotated by BRENDA team