Information on EC 2.7.7.61 - citrate lyase holo-[acyl-carrier protein] synthase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.7.7.61
-
RECOMMENDED NAME
GeneOntology No.
citrate lyase holo-[acyl-carrier protein] synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2'-(5-triphosphoribosyl)-3'-dephospho-CoA + citrate lyase apo-[acyl-carrier protein] = citrate lyase holo-[acyl-carrier protein] + diphosphate
show the reaction diagram
2'-(5'-triphosphoribosyl)-3'-dephospho-CoA: prosthetic group of the gamma-subunit of the citrate lyase
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2'-(5-triphosphoribosyl)-3'-dephospho-CoA + citrate lyase apo-[acyl-carrier protein] = citrate lyase holo-[acyl-carrier protein] + diphosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenylyl group transfer
-
-
-
-
nucleotidyl group transfer
-
-
-
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transfer of phosphoribosyl-dephospho-CoA
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-
-
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PATHWAY
KEGG Link
MetaCyc Link
citrate lyase activation
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SYSTEMATIC NAME
IUBMB Comments
2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate-lyase 2'-(5-phosphoribosyl)-3'-dephospho-CoA-transferase
The gamma-subunit of EC 4.1.3.6, citrate (pro-3S) lyase, serves as an acyl-carrier protein (ACP) and contains the prosthetic group 2'-(5-triphosphoribosyl)-3'-dephospho-CoA [1,3]. Synthesis and attachment of the prosthetic group requires the concerted action of this enzyme and EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase [1]. In the enzyme from Escherichia coli, the prosthetic group is attached to serine-14 of the ACP via a phosphodiester bond.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2'-(5'-phosphoribosyl)-3'-dephospho-CoA transferase
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-
-
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2'-(5'-triphosphoribosyl)-3'-dephospho-CoA:apo-ACP 2'-(5'-phosphoribosyl)-3'-dephospho-CoA transferase
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-
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2'-(5'-triphosphoribosyl)-3'-dephospho-CoA:apo-acyl-carrier protein phosphoribosyl-dephospho-coenzyme A transferase
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2'-(5'-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase
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apo-citrate lyase phosphoribosyl dephospho-CoA transferase
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citrate lyase holo-ACP synthetase
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CitX
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-
-
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holo-ACP synthase
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-
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holo-citrate lyase synthase
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malonate decarboxylase holo-ACP synthetase
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malonate decarboxylase holo-acyl-carrier protein synthetase
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synthetase, malonate decarboxylase holo-acyl-carrier protein
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-
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transferase, 2'-(5'-triphosphoribosyl)-3'-dephospho-CoA:apo-acyl-carrier protein 2'-(5'-phosphoribosyl)-3'-dephospho-CoA
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-
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CAS REGISTRY NUMBER
COMMENTARY
312492-44-7
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 13882
UniProt
Manually annotated by BRENDA team
biovar diacetylactis CRL264
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase
holo-citrate lyase + diphosphate
show the reaction diagram
-
-
-
?
apo-ACP + ATP
AMP-ACP + diphosphate
show the reaction diagram
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side activity of the CitX in absence of its natural substrates, besides ATP, CTP, GTP, and UTP serve as nucleotidyl donors in vitro, ACP: acyl carrier protein, gamma-subunit of the citrate lyase
-
?
additional information
?
-
-
no substrate in vitro: NAD+
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-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase
holo-citrate lyase + diphosphate
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-, Q8VS41
maximal CitX content is present in cells grown anaerobically with citrate as the sole carbon and energy source
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20100
-
-, Q8VS41
calculated from the amino acids number
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 20300, SDS-PAGE, autoradiography
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21-DE3
-
expressed in Escherichia coli BL21-DE3
-, Q8VS41