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Information on EC 2.1.3.15 - acetyl-CoA carboxytransferase
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EC Tree
2.1.3.15 acetyl-CoA carboxytransferaseIUBMB Comments
The enzyme catalyses the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14, biotin carboxylase (see EC 6.4.1.2, acetyl-CoA carboxylase). Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (cf. EC 6.4.1.3, propionyl-CoA carboxylase).
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Word Map
- 2.1.3.15
- mycobacterium
- tuberculosis
-
mycolic
- acyl-coas
- smegmatis
- carboxylases
- malonyl-coa
- propionyl-coa
-
acyl-coenzyme
- methylmalonyl-coa
- haloxyfop
- isoniazid
- accases
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
accd6, accd5, accad, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACC
accAD
-
-
-
-
ACCase
accD5
accD6
acetyl-CoA carboxylase
acetyl-CoA carboxylase carboxyltransferase domain
carboxyltransferase
accD5
-
gene name, encoding a functional acetyl-CoA carboxylase subunit
accD5
-
gene name, encoding a functional acetyl-CoA carboxylase subunit
-
accD6
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gene name, encoding a functional acetyl-CoA carboxylase subunit
accD6
-
gene name, encoding a functional acetyl-CoA carboxylase subunit
-
accD6
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gene name, encoding a functional acetyl-CoA carboxylase subunit
accD6
-
gene name, encoding a functional acetyl-CoA carboxylase subunit
-
acetyl-CoA carboxylase
the enzyme consists of four catalytic subunits: biotin carboxylase, carboxyltransferase-alpha, carboxyltransferase-beta, and biotin carboxyl carrier protein
acetyl-CoA carboxylase
-
the enzyme consists of a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase activity
acetyl-CoA carboxylase
-
the enzyme is composed of three proteins: biotin carboxylase, a biotin carboxyl carrier protein, and carboxyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine:acetyl-CoA:carboxytransferase
The enzyme catalyses the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14, biotin carboxylase (see EC 6.4.1.2, acetyl-CoA carboxylase). Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (cf. EC 6.4.1.3, propionyl-CoA carboxylase).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[biotin carboxyl-carrier protein 87]-N6-biotinyl-L-lysine + malonyl-CoA
[biotin carboxyl-carrier protein 87]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
-
-
-
-
r
[biotin carboxyl-carrier protein 87]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein 87]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
r
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
-
-
-
-
r
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
r
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
-
-
-
-
r
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
r
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
?
[biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
palmitoyl-acyl carrier protein
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allosteric, time-dependent, competitive inhibition
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additional information
-
incorporation of biotin attachment domain-containing proteins (inactive analogs of biotin carboxyl transfer proteins that lack biotin) into the enzyme down-regulates its activity by displacing active (biotin-containing) biotin carboxyltransferase protein subunits
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
although biotin/lipoyl attachment domain containing (BADC) proteins do not directly impact formation of the carboxyltransferase-alphabeta subcomplex of acetyl-CoA carboxylase, the BADC-facilitated biotin carboxyl carrier protein-BADC-biotin carboxylase subcomplex can more readily interact with the carboxyltransferase-alphabeta subcomplex to facilitate the generation of malonyl-CoA
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
AccD6, a key carboxyltransferase essential for mycolic acid synthesis in Mycobacterium tuberculosis, is dispensable in a nonpathogenic strain.
Tuberculosis
AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis.
Tuberculosis
Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis.
Tuberculosis
Pleiotropic effect of AccD5 and AccE5 depletion in acyl-coenzyme A carboxylase activity and in lipid biosynthesis in mycobacteria.
Tuberculosis
Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis.
Tuberculosis
Structure, activity, and inhibition of the Carboxyltransferase ?-subunit of acetyl coenzyme A carboxylase (AccD6) from Mycobacterium tuberculosis.
Tuberculosis
Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
[biotin carboxyl-carrier protein 87]-N6-biotinyl-L-lysine
-
pH and temperature not specified in the publication
0.16
[biotin carboxyl-carrier protein 87]-N6-carboxybiotinyl-L-lysine
-
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000005
moiramide B
-
at pH 8.0, temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (65811 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, using 1 M NaH2PO4, 1 M K2HPO4, 0.2 M Li2SO4, and 0.1 M CAPS at pH 9.5
moiramide B bound to carboxyltransferase, sitting drop vapor diffusion method, using 0.1 M MES (pH 5.0) and 1.6 M NH4SO4
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vapor diffusion method, using 30% (w/v) PEG-400, 0.1 M HEPES at pH 8.0, and 0.2 M MgCl2
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography, Hi-Trap column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-Gold (DE3) and Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21-Gold (DE3) and Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli BL21-Gold (DE3) and Escherichia coli BL21(DE3)pLysS cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Evans, A.; Ribble, W.; Schexnaydre, E.; Waldrop, G.L.
Acetyl-CoA carboxylase from Escherichia coli exhibits a pronounced hysteresis when inhibited by palmitoyl-acyl carrier protein
Arch. Biochem. Biophys.
636
100-109
2017
Escherichia coli
brenda
Bilder, P.; Lightle, S.; Bainbridge, G.; Ohren, J.; Finzel, B.; Sun, F.; Holley, S.; Al-Kassim, L.; Spessard, C.; Melnick, M.; Newcomer, M.; Waldrop, G.
The structure of the carboxyltransferase component of acetyl-CoA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme
Biochemistry
45
1712-1722
2006
Staphylococcus aureus, Escherichia coli (P0ABD5)
brenda
Broussard, T.C.; Pakhomova, S.; Neau, D.B.; Bonnot, R.; Waldrop, G.L.
Structural analysis of substrate, reaction intermediate, and product binding in Haemophilus influenzae biotin carboxylase
Biochemistry
54
3860-3870
2015
Haemophilus influenzae
brenda
Raymer, B.; Kavana, M.; Price, A.; Wang, B.; Corcoran, L.; Kulathila, R.; Groarke, J.; Mann, T.
Synthesis and characterization of a BODIPY-labeled derivative of Soraphen A that binds to acetyl-CoA carboxylase
Bioorg. Med. Chem. Lett.
19
2804-2807
2009
Homo sapiens
brenda
Blanchard, C.; Chapman-Smith, A.; Wallace, J.; Waldrop, G.
The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin
J. Biol. Chem.
274
31767-31769
1999
Escherichia coli
brenda
Silvers, M.A.; Pakhomova, S.; Neau, D.B.; Silvers, W.C.; Anzalone, N.; Taylor, C.M.; Waldrop, G.L.
Crystal structure of carboxyltransferase from Staphylococcus aureus bound to the antibacterial agent moiramide B
Biochemistry
55
4666-4674
2016
Staphylococcus aureus
brenda
Keereetaweep, J.; Liu, H.; Zhai, Z.; Shanklin, J.
Biotin attachment domain-containing proteins irreversibly inhibit acetyl CoA carboxylase
Plant Physiol.
177
208-215
2018
Arabidopsis thaliana
brenda
Shivaiah, K.K.; Ding, G.; Upton, B.; Nikolau, B.J.
Non-catalytic subunits facilitate quaternary organization of plastidic acetyl-CoA carboxylase
Plant Physiol.
182
756-775
2020
Arabidopsis thaliana (Q9LD43 and P56765)
brenda
Pawelczyk, J.; Viljoen, A.; Kremer, L.; Dziadek, J.
The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium
Sci. Rep.
7
42692
2017
Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis mc(2)155
brenda
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Release 2023.1 (January 2023)
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