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Information on EC 2.3.1.222 - phosphate propanoyltransferase and Organism(s) Rhodopseudomonas palustris and UniProt Accession Q21A54

for references in articles please use BRENDA:EC2.3.1.222
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IUBMB Comments
Part of the degradation pathway for propane-1,2-diol .
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Rhodopseudomonas palustris
UNIPROT: Q21A54
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The taxonomic range for the selected organisms is: Rhodopseudomonas palustris
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
phosphotransacylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:phosphate propanoyltransferase
Part of the degradation pathway for propane-1,2-diol .
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
propanoyl-CoA + phosphate
CoA + propanoyl phosphate
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the phosphotransacylase (PTAC) predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). PduL and Pta exemplify functional, but not structural, convergent evolution
metabolism
the fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt bacterial microcompartments(BMC)-based metabolism, while not affecting most commensal organisms that require phosphotransacylase (PTAC) activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are obtained from sitting drop experiments at 22°C. High-resolution PduL crystal structures with bound substrates. The PduL fold is unrelated to that of Pta. It contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping phosphotransacylase (PTAC)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Erbilgin, O.; Sutter, M.; Kerfeld, C.A.
The structural basis of coenzyme A recycling in a bacterial organelle
PLoS Biol.
14
e1002399
2016
Rhodopseudomonas palustris (Q21A54), Rhodopseudomonas palustris BisB18 (Q21A54), Salmonella enterica subsp. enterica serovar Typhimurium (Q9XDN5)
Manually annotated by BRENDA team