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Information on EC 6.4.1.3 - propionyl-CoA carboxylase and Organism(s) Ruegeria pomeroyi and UniProt Accession Q5LUF3

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EC Tree
IUBMB Comments
A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
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This record set is specific for:
Ruegeria pomeroyi
UNIPROT: Q5LUF3
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The taxonomic range for the selected organisms is: Ruegeria pomeroyi
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
propionyl-coa carboxylase, pccbc, propionyl-coenzyme a carboxylase, acetyl-coa/propionyl-coa carboxylase, pcca-1, pccb-1, pccase, propanoyl-coa:carbon-dioxide ligase (adp-forming), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
propionyl-coenzyme A carboxylase
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Carboxylase, propional coenzyme A (adenosine triphosphate-hydrolyzing)
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Pcase
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PCCase
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Propanoyl-CoA:carbon dioxide ligase
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Propionyl coenzyme A carboxylase
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Propionyl coenzyme A carboxylase (adenosine triphosphate-hydrolyzing)
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Propionyl coenzyme A carboxylase (ATP-hydrolyzing)
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propionyl-coenzyme A carboxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-94-3
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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 + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
the enzyme has a preference for propanoyl-CoA over acetyl-CoA as the substrate
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?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
the enzyme has a preference for propanoyl-CoA over acetyl-CoA as the substrate
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?
acetyl-CoA + CO2
?
show the reaction diagram
the enzyme has a preference for propionyl-CoA over acetyl-CoA as the substrate
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?
propionyl-CoA + CO2
(S)-methylmalonyl-CoA
show the reaction diagram
the enzyme has a preference for propionyl-CoA over acetyl-CoA as the substrate
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
PCC is essential for the catabolism of the amino acids L-Thr, L-Val, L-Ile and L-Met, cholesterol and fatty acids with an odd number of carbon atoms
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
750000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterododecamer
the alpha-subunit contains the biotin carboxylase and biotin carboxyl carrier protein domains, whereas the beta-subunit supplies the carboxyltransferase activity
heterododecamer
alpha6beta6-heterododecamer, the alpha-subunit contains the biotin carboxylase and biotin carboxyl carrier protein domains, whereas the beta-subunit supplies the carboxyltransferase activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch method under oil method
a PCC chimaera, containing the alpha-subunit of Ruegeria pomeroyi PCC and the beta-subunit of Roseobacter denitrificans PCC is crystallized by the microbatch method under paraffin oil, using 0.1 M HEPES (pH 8.0), 22% (w/v) PEG3350, 0.2 M NaCl and 16% (v/v) glycerol. Crystals of Ruegeria pomeroyi PCC are obtained at 20°C by the microbatch method under paraffin oil, using 0.2 M succinic acid (pH 6.5), 22% (w/v) benzamidine and 22% (w/v) PEG3000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G668R
the mutation in the biotin carboxyl carrier protein domain abolishes biotinylation
R165Q
the mutation disturbs the recognition of the adenine base of CoA
R165W
the mutation disturbs the recognition of the adenine base of CoA
R399Q
the mutation leads to a large loss in activity
D440I
the mutation does not change the substrate preference of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography and gel filtration
nickel affinity column chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, C.; Sadre-Bazzaz, K.; Shen, Y.; Deng, B.; Zhou, Z.; Tong, L.
Crystal structure of the alpha6beta6 holoenzyme of propionyl-coenzyme A carboxylase
Nature
466
1001-1005
2010
Ruegeria pomeroyi, Ruegeria pomeroyi (Q5LUF3)
Manually annotated by BRENDA team