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Information on EC 6.4.1.2 - acetyl-CoA carboxylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q38970
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6.4.1.2 acetyl-CoA carboxylaseIUBMB Comments
This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
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Word Map
- 6.4.1.2
-
amp-activated
- triglyceride
-
lipogenesis
- adipose
-
lipogenic
- sterol
- peroxisome
- cholesterol
- obesity
- carnitine
- malonyl-coa
-
proliferator-activated
-
high-fat
- adipocytes
- lipoprotein
-
element-binding
- biotin
- steatosis
- lipase
-
obese
-
herbicide
- srebp-1c
- triacylglycerols
-
diet-induced
- stearoyl-coa
-
malic
- adiponectin
- nafld
-
lipolysis
-
monophosphate-activated
-
hfd-induced
- protein-1c
-
weed
- carboxylases
- aicar
-
atp-citrate
-
malonyl
-
desaturase-1
-
anti-obesity
-
biotin-dependent
-
hormone-sensitive
-
chrebp
-
5'-amp-activated
-
palmitoyltransferase-1
-
target-site
- adenoid
-
srebf1
-
anti-adipogenic
- lolium
- biotechnology
- medicine
-
herbicide-resistant
- pharmacology
- synthesis
- drug development
- biofuel production
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acetyl-coa carboxylase, accase, acetyl coa carboxylase, acetyl-coenzyme a carboxylase, acaca, acc-2, acetyl coenzyme a carboxylase, acetyl-coa carboxylase 1, acc-1, acacb, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACCase
Acetyl CoA carboxylase
-
-
-
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Acetyl coenzyme A carboxylase
-
-
-
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Acetyl-coenzyme A carboxylase
-
-
-
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BCCP1
BCCP2
Carboxylase, acetyl coenzyme A
-
-
-
-
additional information
-
the enzyme belongs to the family of biotin-dependent carboxylases
ACCase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA
two-step reaction mechanism, structure-activity relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
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-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:hydrogencarbonate ligase (ADP-forming)
This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
CAS REGISTRY NUMBER
COMMENTARY
9023-93-2
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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
ATP + acetyl-CoA + HCO3-
?
-
synthesis of malonyl-CoA, which is used as the substrate in the biosynthesis of a variety of polyketide derivatives, including fatty acids, flavonoids, and stilbenoids. In addition malonyl-CoA is used as the substrate for the malonation of a variety of plant phytochemicals
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-
?
additional information
?
-
ACCase 1 is essential for correct plant development
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-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
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-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first committed step of fatty acid synthesis, physiological roles of the isozymes, regulation by RNA editing, post-transcriptional, and by stromal pH, photosynthetic redox cascade, and Mg2+ concentration, overview
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-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
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the enzyme exhibits malonyl-CoA carboxylase and biotin carboxylase activity
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
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the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase
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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
ATP + acetyl-CoA + HCO3-
?
-
synthesis of malonyl-CoA, which is used as the substrate in the biosynthesis of a variety of polyketide derivatives, including fatty acids, flavonoids, and stilbenoids. In addition malonyl-CoA is used as the substrate for the malonation of a variety of plant phytochemicals
-
-
?
additional information
?
-
ACCase 1 is essential for correct plant development
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first committed step of fatty acid synthesis, physiological roles of the isozymes, regulation by RNA editing, post-transcriptional, and by stromal pH, photosynthetic redox cascade, and Mg2+ concentration, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fenoxaprop
-
a specific inhibitor of the cytosolic ACCase, does not affect the activity of chloroplast ACCase
PII protein
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recombinant Arabidopsis PII protein inhibits chloroplastic ACCase activity dose-dependently and noncompetitively via binding to its BCCP subunit, and this is completely reversed in the presence of 2-oxoglutarate, pyruvate, or oxaloacetate. PII protein decreases the Vmax of the ACCase reaction without altering the Km for acetyl-CoA
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soraphen A
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macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00015
PII protein
Arabidopsis thaliana
-
apparent value, in 100 mM Tricine (pH 8.2), at 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
plastidic isozyme, associated with the chloroplast envelope
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
transfer DNA insertional alleles that completely eliminate the accumulation of subunit BCCP2 have no perceptible effect on plant growth, development, and fatty acid accumulation. In contrast, transfer DNA insertional null allele of the CAC1A gene for subunit BCCP1 is embryo lethal and deleteriously affects pollen development and germination. Reducing BCCP1 accumulation to 35% of wild type levels, decreases fatty acid accumulation and severely affects normal vegetative plant growth
physiological function
physiological function
-
ACCase is a key enzyme initiating the synthesis of fatty acids in plastids
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACC1_ARATH
2254
0
251382
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heteromer
-
the enzyme is composed of four subunits: biotin carboxyl carrier protein, biotin carboxylase, alpha-carboxyltransferase, and beta-carboxyltransferase
tetramer
-
heterotetrameric plastidic enzyme form, the heterotetramer is composed of the subunits biotin carboxyl carrier protein BCCP, biotin carboxylase BC, and alpha and beta subunits of the carboxyltransferase CT
additional information
?
-
plastid-localized enzyme, 4 different types of subunits: 1. biotin carboxyl carrier subunit, 2. biotin carboxylase subunit, 3. alpha-subunit of carboxyltransferase, 4. beta-subunit of carboxyltransferase
additional information
-
plants possess a homomeric single polypeptide enzyme form in the cytosol, and a heterotetrameric plastidic enzyme form
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
mutations gurke, gk-SC allele, and pasticcino3, pas3-1 and pas3-2 alleles, affect cell division and the bilateral symmetry due to severe defects in the apical region, the mutations are allelic to the lethal acc1 mutation, acc1-1 and acc1-2 alleles, leading to a similar phenotype in embryos, altered fatty acid composition, the phenotype can be partially complemented by malonate, overview
additional information
-
construction of transgenic potato plants by overexpression of the Arabidopsis thaliana isozyme ACC1 in the amyloplast of Solanum tuberosum tubers leads to an increased fatty acid synthesis and a 5fold increased amount of triacylglycerol in the tubers
additional information
-
missense mutation of the biotin carboxylase domain located at the active site disrupts catalysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ACC1, DNA and amino acid sequence determination of wild-type and mutants acc1, gk, and pas
overexpression of isozyme ACC1 in the amyloplast of Solanum tuberosum tubers using the Agrobacterium transfection system
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subunit BCCP is encoded by 2 genes, while the other 3 subunits are single gene-encoded
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
accumulation of BCCP1 is 5ffold higher than that of BCCP2 in developing siliques
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choi, J.K.; Ke, J.; McKean, A.L.; Weaver, L.M.; Wen, T.N.; Sun, J.; Diez, T.; Yu, F.; Guan, X.; Wurtele, E.S.; Nikolau, B.J.
Molecular biology of biotin-containing enzymes required in lipid metabolism
Physiol. Biochem. Mol. Biol. Plant Lipids (Proc. Int. Symp. Plant Lipids)
12
363-367
1997
Arabidopsis thaliana
-
Ke, J.; Choi, J.K.; Smith, M.; Horner, H.T.; Nikolau, B.J.; Wurtele, E.S.
Structure of the CAC1 gene and in situ characterization of its expression. The Arabidopsis thaliana gene coding for the biotin-containing subunit of the plastidic acetyl-coenzyme A carboxylase
Plant Physiol.
113
357-365
1997
Arabidopsis thaliana, Arabidopsis sp.
Choi, J.K.; Yu, F.; Wurtele, E.S.; Nikolau, B.J.
Molecular cloning and characterization of the cDNA coding for the biotin-containing subunit of the chloroplastic acetyl-coenzyme A carboxylase
Plant Physiol.
109
619-625
1995
Arabidopsis thaliana, Arabidopsis sp.
Sasaki, Y.; Nagano, Y.
Plant acetyl-CoA carboxylase: structure, biosynthesis, regulation, and gene manipulation for plant breeding
Biosci. Biotechnol. Biochem.
68
1175-1184
2004
Arabidopsis thaliana, Brassica napus, Escherichia coli, Nicotiana tabacum, Oryza sativa, Pisum sativum, Triticum aestivum
Tong, L.
Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery
Cell. Mol. Life Sci.
62
1784-1803
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Hordeum vulgare, Mus musculus, Oryza sativa, Rattus norvegicus, Schizosaccharomyces pombe, Streptomyces coelicolor, Toxoplasma gondii
Baud, S.; Bellec, Y.; Miquel, M.; Bellini, C.; Caboche, M.; Lepiniec, L.; Faure, J.D.; Rochat, C.
Gurke and pasticcino3 mutants affected in embryo development are impaired in acetyl-CoA carboxylase
EMBO Rep.
5
515-520
2004
Arabidopsis thaliana (Q38970)
Klaus, D.; Ohlrogge, J.B.; Neuhaus, H.E.; Dormann, P.
Increased fatty acid production in potato by engineering of acetyl-CoA carboxylase
Planta
219
389-396
2004
Arabidopsis thaliana, Solanum tuberosum
Li, X.; Ilarslan, H.; Brachova, L.; Qian, H.R.; Li, L.; Che, P.; Wurtele, E.S.; Nikolau, B.J.
Reverse-genetic analysis of the two biotin-containing subunit genes of the heteromeric acetyl-coenzyme A carboxylase in Arabidopsis indicates a unidirectional functional redundancy
Plant Physiol.
155
293-314
2011
Arabidopsis thaliana
Bourrellier, A.; Valot, B.; Guillot, A.; Ambard-Bretteville, F.; Vidal, J.; Hodges, M.
Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate-regulated by interaction of PII with the biotin carboxyl carrier subunit
Proc. Natl. Acad. Sci. USA
107
502-507
2010
Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 6.4.1.2)
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