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Information on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase and Organism(s) Burkholderia pseudomallei and UniProt Accession Q3JW91

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IUBMB Comments
The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.
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Burkholderia pseudomallei
UNIPROT: Q3JW91
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Word Map
The taxonomic range for the selected organisms is: Burkholderia pseudomallei
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphopantetheine adenylyltransferase, 4'-phosphopantetheine adenylyltransferase, pantetheine phosphate adenylyltransferase, pantetheine-phosphate adenylyltransferase, dephospho-coa pyrophosphorylase, enterococcus faecalis ppat, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphopantetheine adenylyltransferase
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3'-dephospho-CoA pyrophosphorylase
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dephospho-CoA pyrophosphorylase
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dephospho-coenzyme A pyrophosphorylase
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pantetheine phosphate adenylyltransferase
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PPAT
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pantetheine-4'-phosphate adenylyltransferase
The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-99-7
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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
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the fourth of five steps in the coenzyme A biosynthetic pathway
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M sodium acetate pH 4.6, 30% (w/v) PEG 2000
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His Trap column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)R3 Rosetta cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Edwards, T.E.; Leibly, D.J.; Bhandari, J.; Statnekov, J.B.; Phan, I.; Dieterich, S.H.; Abendroth, J.; Staker, B.L.; Van Voorhis, W.C.; Myler, P.J.; Stewart, L.J.
Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei
Acta Crystallogr. Sect. F
67
1032-1037
2011
Burkholderia pseudomallei (Q3JW91), Burkholderia pseudomallei
Manually annotated by BRENDA team