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Information on EC 2.8.3.16 - formyl-CoA transferase and Organism(s) Escherichia coli and UniProt Accession P69902

for references in articles please use BRENDA:EC2.8.3.16
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     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.3 CoA-transferases
                2.8.3.16 formyl-CoA transferase
IUBMB Comments
The enzyme from Oxalobacter formigenes can also catalyse the transfer of CoA from formyl-CoA to succinate.
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Select one or more organisms in this record:
This record set is specific for:
Escherichia coli
UNIPROT: P69902
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
formyl-coenzyme a transferase, formyl coenzyme a transferase, fcoct, formyl-coa:oxalate coa-transferase, formyl-coa-transferase, formyl-coa oxalate coa-transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A-transferase, formyl coenzyme A-oxalate
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formyl coenzyme A transferase
246
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formyl-CoA oxalate CoA-transferase
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formyl-CoA-transferase
246, 286195
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formyl-coenzyme A transferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
formyl-CoA:oxalate CoA-transferase
The enzyme from Oxalobacter formigenes can also catalyse the transfer of CoA from formyl-CoA to succinate.
CAS REGISTRY NUMBER
COMMENTARY hide
128826-27-7
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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
formyl-CoA + oxalate
formate + oxalyl-CoA
show the reaction diagram
formyl-CoA + oxalate
formate + oxalyl-CoA
show the reaction diagram
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
formyl-CoA + oxalate
formate + oxalyl-CoA
show the reaction diagram
P69902
oxalate is a highly oxidized compound that may be used as C- and energy sources by oxalotrophic bacteria
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-
?
formyl-CoA + oxalate
formate + oxalyl-CoA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
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coenzyme A
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free CoA
oxalate
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substrate inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
formyl-CoA
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His-YfdW
0.51
oxalate
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His-YfdW
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23
oxalate
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K12, frc gene
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
oxalate enrichment culture
Manually annotated by BRENDA team
soil samples are collected below the Ca-oxalate producing trees Milicia excelsa and Afzelia africana and in a similar soil distant from trees
Manually annotated by BRENDA team
oxalate enrichment culture
Manually annotated by BRENDA team
soil samples are collected below the Ca-oxalate producing trees Milicia excelsa and Afzelia africana and in a similar soil distant from trees
Manually annotated by BRENDA team
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
His-tagged YfdW protein is purified by metal affinity chromatography and subsequent gel filtration on a Superdex 200 column, eluting with 5 mM HEPES buffer containing 150 mM NaCl, pH 7.5.
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli XL1
expression in Escherichia coli K12
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expression in Escherichia coli XL1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
bacterial oxalate-degrading function, microbiological processes are considered as the main oxalate sinks in natural environments, in soil oxalate from fungi, plant root exudates and decaying plant tissues display powerful metal chelating properties. Oxalate takes part in plant nutrition status by increasing the availability of phosphate and other poorly soluble micro-nutriments, through its ability to complex and remove excess metal cations. It also plays an important role in the detoxification of heavy metals in the vicinity of plant roots.
medicine
bacterial oxalate-degrading function, in humans an accumulation of oxalic acid can result in a number of pathologic conditions, including hyperoxaluria, urolithiasis, renal failure, cardiomyopathy and cardiac conductance disorders
molecular biology
use of the frc gene as template for PCR to detect oxalotrophic bacteria
environmental protection
bacterial oxalate-degrading function, microbiological processes are considered as the main oxalate sinks in natural environments, in soil oxalate from fungi, plant root exudates and decaying plant tissues display powerful metal chelating properties. Oxalate takes part in plant nutrition status by increasing the availability of phosphate and other poorly soluble micro-nutriments, through its ability to complex and remove excess metal cations. It also plays an important role in the detoxification of heavy metals in the vicinity of plant roots.
medicine
bacterial oxalate-degrading function, in humans an accumulation of oxalic acid can result in a number of pathologic conditions, including hyperoxaluria, urolithiasis, renal failure, cardiomyopathy and cardiac conductance disorders
molecular biology
use of the frc gene as template for PCR to detect oxalotrophic bacteria
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Toyota, C.G.; Berthold, C.L.; Gruez, A.; Jonsson, S.; Lindqvist, Y.; Cambillau, C.; Richards, N.G.
Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase
J. Bacteriol.
190
2556-2564
2008
Escherichia coli, Escherichia coli MG1655, Oxalobacter formigenes (O06644), Oxalobacter formigenes
Manually annotated by BRENDA team
Khammar, N.; Martin, G.; Ferro, K.; Job, D.; Aragno, M.; Verrecchia, E.
Use of the frc gene as a molecular marker to characterize oxalate-oxidizing bacterial abundance and diversity structure in soil
J. Microbiol. Methods
76
120-127
2008
Ancylobacter oerskovii, Ancylobacter polymorphus (B3VMH8), Arquibacter sp., Azorhizobium sp., Azospirillum brasilense, Azospirillum lipoferum, Bradyrhizobium japonicum (Q89QH2), Bradyrhizobium sp. (A5EGD7), Cupriavidus necator (Q0K0H8), Cupriavidus necator (Q46S66), Cupriavidus necator (Q46S72), Cupriavidus necator JMP 134-1 (Q46S72), Cupriavidus oxalaticus, Escherichia coli, Escherichia coli (P69902), Herminiimonas arsenicoxydans (A4G241), Herminiimonas arsenicoxydans (A4G242), Herminiimonas saxobsidens, Janthinobacterium sp. Marseille (A6T0J2), Methylobacterium organophilum, Methylorubrum extorquens, Methylorubrum thiocyanatum, Oxalicibacterium flavum, Oxalobacter formigenes (O06644), Pandoraea sp., Paraburkholderia xenovorans (Q13RQ4), Rhodopseudomonas palustris (Q6N8F8), Shigella flexneri (P69903), Starkeya novella, Streptomyces avermitilis (Q82M40), Streptomyces coelicolor (O87838), Streptomyces violaceoruber, Variovorax paradoxus, Xanthobacter autotrophicus (A7ICK2), Xanthobacter flavus, Xanthomonas sp.
Manually annotated by BRENDA team
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