Information on EC 6.3.4.14 -

Information on EC 6.3.4.14 - Biotin carboxylase:

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EC NUMBER	COMMENTARY
6.3.4.14	-

RECOMMENDED NAME	GeneOntology No.
Biotin carboxylase	GO:0009343

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein		-	-	-	-
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein		carboxylation proceeds via a carboxyphosphate intermediate; MgATP2- and HCO3- add to the enzyme randomly, followed by addition of biotin. Both HCO3- and MgATP2- add in rapid equilibrium	Escherichia coli	-	1420
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein		carboxylation proceeds via a carboxyphosphate intermediate	Escherichia coli	-	1423, 1424
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein		kinetic mechanism	Escherichia coli	-	654403
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein		mechanism	Escherichia coli	-	654575
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein		reaction mechanism	Escherichia coli	-	655978
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein		catalytic mechanism	Escherichia coli	-	656008

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
amination	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
biotin-carboxyl carrier protein assembly	-	PWY0-1264

SYSTEMATIC NAME	IUBMB Comments
Biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming)	-

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
ACC	-	-	-	-
AccA	Myxococcus xanthus	Q9FAF5	Myxococcus xanthus	651665
AccC	Jatropha curcas	F2WMV4	-	716633
BC	-	-	-	-
biotin carboxylase	Geobacillus thermodenitrificans	-	domain of pyruvate carboxylase	651171
biotin carboxylase	Saccharomyces cerevisiae	Q00955	domain of acetyl-coenzyme A carboxylase	662830
biotin carboxylase	Acidianus brierleyi	Q877I5	-	692103
biotin carboxylase	Cenarchaeum symbiosum	A0RY62	-	692103
biotin carboxylase	Chlorobium limicola, Chlorobium phaeobacteroides	-	-	692103
biotin carboxylase	Chloroflexus aurantiacus	A9W9X0	-	692103
biotin carboxylase	Cupriavidus metallidurans, Cytophaga hutchinsonii	-	-	692103
biotin carboxylase	Geobacter uraniireducens	A5G5L1	-	692103
biotin carboxylase	Halobacterium salinarum	Q9HPP8	-	692103
biotin carboxylase	Hyperthermus butylicus	A2BLY3	-	692103
biotin carboxylase	Maribacter sp. HTCC2170	A4APF1	-	692103
biotin carboxylase	Metallosphaera sedula	Q8J2Z4	-	692103
biotin carboxylase	Methanococcales, Methanosarcinales	-	-	692103
biotin carboxylase	Natronomonas pharaonis	Q3INT5	-	692103
biotin carboxylase	Nitrosopumilus maritimus	A9A3E8	-	692103
biotin carboxylase	Pelobacter carbinolicus	Q3A2P1	-	692103
biotin carboxylase	Pelobacter propionicus	A1ANN6	-	692103
biotin carboxylase	Polaromonas sp.	Q12EJ0	-	692103
biotin carboxylase	Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	A4SVB6	-	692103
biotin carboxylase	Sulfolobus metallicus	O52602	-	692103
biotin carboxylase	Sulfolobus solfataricus	Q97V46	-	692103
biotin carboxylase	Sulfolobus tokodaii	Q974R7	-	692103
biotin carboxylase	Synechococcus sp.	Q54755	-	692103
biotin carboxylase	Trichodesmium erythraeum	Q10YA8	-	692103
biotin carboxylase	uncultured bacterium	B1GX36	-	692103
biotin carboxylase	Staphylococcus aureus	Q99UY9	component of pyruvate carboxylase	706790
biotin carboxylase (component of acetyl CoA carboxylase)	Escherichia coli	-	-	655973
biotinoyl domain of acetyl-CoA carboxylase	Homo sapiens	-	-	695042
BirA	Escherichia coli	-	-	695042
PC-beta	Aquifex aeolicus	-	BC subunit of pyruvate carboxylase	654115
Carboxylase, biotin	-	-	-	-
additional information	Escherichia coli	-	member of the ATP-grasp superfamily	654566
additional information	Escherichia coli	-	belongs to the ATP-grasp superfamily	655978
additional information	Escherichia coli	-	ATP-grasp superfamily	656008

CAS REGISTRY NUMBER	COMMENTARY
9075-71-2	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Acidianus brierleyi	gene accC	692103	Q877I5	UniProt
Aquifex aeolicus	-	654115	-	-
Arabidopsis thaliana	-	1434, 1435	-	-
Bacillus subtilis	-	1438	-	-
Brassica napus	-	1440	-	-
Cenarchaeum symbiosum	gene accC	692103	A0RY62	UniProt
Chlorobium limicola	gene accC	692103	-	-
Chlorobium phaeobacteroides	gene accC	692103	-	-
Chloroflexus aurantiacus	gene accC	692103	A9W9X0	UniProt
Corynebacterium glutamicum	protein composed of two domains: an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein	1437	-	-
Cupriavidus metallidurans	gene accC	692103	-	-
Cytophaga hutchinsonii	gene accC	692103	-	-
Escherichia coli	-	1420, 1421, 1422, 1423, 1424, 1425, 1427, 1428, 1429, 1430, 1431, 1433, 654403, 654575, 655535, 655973, 655978, 656008, 656018, 656207, 675698, 706634	-	-
Escherichia coli	-	675923, 693839, 701439, 704465, 706519	P24182	UniProt
Escherichia coli	B	1426	-	-
Escherichia coli	gene accC	695008	-	-
Escherichia coli	gene birA	695042	-	-
Escherichia coli	strain JM109	654566	-	-
Escherichia coli JM109	strain JM109	654566	-	-
Geobacillus thermodenitrificans	-	651171, 671061	-	-
Geobacter uraniireducens	gene accC	692103	A5G5L1	UniProt
Haemophilus influenzae	-	701439	-	-
Halobacterium salinarum	i.e. Halobacterium halobium, gene accC	692103	Q9HPP8	UniProt
Homo sapiens	-	702083	O00763	SwissProt
Homo sapiens	component of pyruvate carboxylase	703970	-	-
Homo sapiens	contains isozymes ACC1 and ACC2	695042	-	-
Hyperthermus butylicus	strain DSM 5456/JCM 9403; gene accC	692103	A2BLY3	UniProt
Jatropha curcas	-	716633	F2WMV4	UniProt
Magnaporthe grisea	-	660969	-	-
Maribacter sp. HTCC2170	gene accC	692103	A4APF1	UniProt
Medicago sativa	-	37620	-	-
Metallosphaera sedula	gene accC	692103	Q8J2Z4	SwissProt
Methanococcales	gene accC	692103	-	-
Methanosarcinales	gene accC	692103	-	-
Moraxella catarrhalis	-	701439	-	-
Mycobacterium leprae	a protein possessing a biotin carboxylase function as well as a biotin carrier protein	1432	-	-
Mycobacterium tuberculosis	a protein possessing a biotin carboxylase function as well as a biotin carrier protein	1432	-	-
Myxococcus xanthus	strain IFO13542/ATCC25232	651665	Q9FAF5	SwissProt
Myxococcus xanthus IFO13542/ATCC25232	strain IFO13542/ATCC25232	651665	Q9FAF5	SwissProt
Natronomonas pharaonis	strain DSM 2160/ATCC 35678; gene accC	692103	Q3INT5	UniProt
Nicotiana tabacum	-	37620	-	-
Nicotiana tabacum	transformed with antisense-expression and overexpression tobacco BC constructs, which results in the generation of plants with biotin carboxylase levels ranging from 20 to 500% of the wild-type levels	1436	-	-
Nitrosopumilus maritimus	gene accC	692103	A9A3E8	UniProt
Pelobacter carbinolicus	gene accC	692103	Q3A2P1	UniProt
Pelobacter propionicus	gene accC	692103	A1ANN6	UniProt
Phytophthora infestans	-	660969	-	-
Pisum sativum	-	37620	-	-
Pisum sativum	cv. Little Marvel	654339	-	-
Polaromonas sp.	strain JS666/ATCC BAA-500; gene accC	692103	Q12EJ0	UniProt
Polaromonas sp. JS666	strain JS666/ATCC BAA-500; gene accC	692103	Q12EJ0	UniProt
Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	strain QLW-P1DMWA-1; gene accC	692103	A4SVB6	UniProt
Pseudomonas aeruginosa	-	1441	-	-
Pseudomonas aeruginosa	strain PAO1	695008	-	-
Ricinus communis	-	37620	-	-
Saccharomyces cerevisiae	-	662830	Q00955	UniProt
Staphylococcus aureus	component of pyruvate carboxylase	706790	Q99UY9	UniProt
Staphylococcus aureus	strain Mu50	695008	-	-
Staphylococcus aureus Mu50	strain Mu50	695008	-	-
Sulfolobus metallicus	-	677847	O52602	SwissProt
Sulfolobus metallicus	gene accC	692103	O52602	SwissProt
Sulfolobus solfataricus	gene accC	692103	Q97V46	UniProt
Sulfolobus tokodaii	gene accC	692103	Q974R7	UniProt
Synechococcus sp.	gene accC	692103	Q54755	UniProt
Trichodesmium erythraeum	gene accC	692103	Q10YA8	UniProt
uncultured bacterium	gene accC	692103	B1GX36	UniProt
Ustilago maydis	-	660969	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
ADP + carbamoyl phosphate	ATP + carbamate		Escherichia coli	-	biotin carboxylase catalyzes an ATP synthesis reaction, in which a phosphate group is transferred from carbamoyl phosphate to ADP forming ATP and carbamate	654566, 654575, 656008	carbamate rapidly decomposes into carbon dioxide and ammonia	-	?
ADP + carbamoyl phosphate	ATP + carbamate		Escherichia coli	-	biotin carboxylase catalyzes the formation of ATP from ADP and carbamoyl phosphate	656207	-	-	r
ATP + 1'-N-carboxy-D-biotin + HCO3-	ADP + phosphate + ?		Escherichia coli	-	the 1'-ureido-N position of biotin is the enzymatic site of carboxylation	1425	-	1425	-
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	-	655535, 706634, 704465	-	-	?
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	also uses free biotin as substrate	656008	-	-	?
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	also utilizes free biotin as substrate	654575, 655978	-	-	?
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	biotin carboxylase component of the multienzyme complex acetyl-CoA carboxylase, also utilizes free biotin as substrate	654403	-	-	?
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	free biotin, 8000fold lower activity than with the C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein, biotin carboxylase activity of acetyl-CoA carboxylase	655973	-	-	?
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	utilizes free biotin as substrate	654566	-	-	?
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	utilizes free biotin as substrate	656207	-	-	r
ATP + biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	utilizes free biotin as substrate in vitro	656018	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Chlorobium limicola	-	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Staphylococcus aureus	-	-	695008	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	P24182	-	675923	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	695008, 695042	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pseudomonas aeruginosa	-	-	695008	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Geobacillus thermodenitrificans	-	-	651171	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Cupriavidus metallidurans, Cytophaga hutchinsonii	-	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Metallosphaera sedula	Q8J2Z4	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Sulfolobus metallicus	O52602	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Chlorobium phaeobacteroides, Methanosarcinales	-	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Synechococcus sp.	Q54755	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pelobacter propionicus	A1ANN6	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		uncultured bacterium	B1GX36	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Maribacter sp. HTCC2170	A4APF1	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	A4SVB6	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Polaromonas sp.	Q12EJ0	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Chloroflexus aurantiacus	A9W9X0	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Hyperthermus butylicus	A2BLY3	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Natronomonas pharaonis	Q3INT5	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Halobacterium salinarum	Q9HPP8	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Nitrosopumilus maritimus	A9A3E8	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Sulfolobus solfataricus	Q97V46	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Acidianus brierleyi	Q877I5	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Sulfolobus tokodaii	Q974R7	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Trichodesmium erythraeum	Q10YA8	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Geobacter uraniireducens	A5G5L1	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pelobacter carbinolicus	Q3A2P1	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Cenarchaeum symbiosum	A0RY62	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Methanococcales	-	-	692103	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	mathematical modeling and numerical simulations of the kinetics of wild-type, hybrid dimers, and mutant homodimers of biotin carboxylase are performed. Numerical simulations of biotin carboxylase kinetics are the most similar to the experimental data when an oscillating active site model is used. In contrast, alternative models where the active sites are independent do not agree with the experimental data. Thus, the numerical simulations of the proposed kinetic model support the hypothesis that the two active sites of biotin carboxylase alternate their catalytic cycles	675698	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committed step in fatty acid synthesis	693839	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Homo sapiens	-	The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview, biotin is covalently attached to a protein called the biotin-carboxyl-carrier protein. In mammals, these proteins comprise different domains in a single polypeptide chain, biotin must be attached to ACC to produce a functional enzyme	695042	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	in Gram-negative and Gram-positive bacteria biotin carboxylase, carboxyltransferase, and the biotin carboxyl carrier protein are separate proteins	693839	-	-	?
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	the biotinoyl domain interacts with the biotin-carboxyl-carrier protein, BCCP, biotin must be attached to ACC to produce a functional enzyme	695042	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Bacillus subtilis	-	-	1438	-	1438	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1420	-	1420	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1421	-	1421	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1423	-	1423	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1424	-	1424	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1425	-	1425	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1426	-	1426	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1427	-	1427	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1428	-	1428	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1429	-	1429	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1430	-	1430	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1431	-	1431	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1433	-	1433	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pisum sativum	-	-	37620	-	37620	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Nicotiana tabacum	-	-	1436	-	1436	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Nicotiana tabacum	-	-	37620	-	37620	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Arabidopsis thaliana	-	-	1434	-	1434	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Arabidopsis thaliana	-	-	1435	-	1435	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pseudomonas aeruginosa	-	-	1441	-	1441	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Brassica napus	-	-	1440	-	1440	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Corynebacterium glutamicum	-	-	1437	-	1437	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Mycobacterium leprae	-	-	1432	-	1432	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Medicago sativa, Ricinus communis	-	-	37620	-	37620	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue	654566	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase	656207	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	first half reaction of the first committed step in the biosynthesis of long-chain fatty acids, in vivo the biotin substrate is attached to biotin-carboxyl-carrier protein, natural substrate	655973	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	long-chain fatty acid synthesis, in vivo biotin is covalently attached to the biotin-carboxyl-carrier protein	654403	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue	656008	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to the biotin-carboxyl-carrier protein in vivo, fatty acid synthesis	656018	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, component of the multifunctional acetyl-CoA carboxylase, roles of Arg-338 and Lys-238 in the carboxyl transfer to biotin, Arg-338 serves to orient the carboxyphosphate intermediate for optimal carboxylation of biotin	656207	-	-	r
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pisum sativum	-	BC component of the multisubunit complex acetyl-CoA carboxylase, BC catalyzes the ATP-dependent carboxylation of the biotinyl moiety on biotin carboxyl carrier protein	654339	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Aquifex aeolicus	-	BC subunit of pyruvate carboxylase, BC/active site structure	654115	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biotin carboxylase component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the first half-reaction of the reaction catalyzed by acetyl-CoA carboxylase, the ATP-dependent carboxylation of biotin, ordered addition of substrates with ATP binding first followed by bicarbonate and then biotin	654403	-	-	r
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biotin carboxylase is one of three distinct components of acetyl-CoA carboxylase, carboxylation of the ureido ring of biotin at the N-1 position, reaction mechanism, domain structure, the biotin carboxylase B-domain moves as a result of ATP binding, enzyme structure	655978	-	-	r
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Myxococcus xanthus	Q9FAF5	biotin carboxylase subunit AccA of acetyl-CoA carboxylase	651665	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	Lys-238 interacts with the gamma-phosphate group of ATP but is not involved in catalysis, BC is a subunit of acetyl-CoA carboxylase and mediates the carboxylation of enzyme-bound biotin	655535	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, active site structure, binding of biotin accelerates the rate of ATP hydrolysis about 1100fold: substrate-induced synergism	654566	-	-	r
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, for that biotin must be deprotonated at its N1� position, mechanism for deprotonation of biotin, bicarbonate is the source of CO2, Lys-238 plays a role in the carboxylation reaction, Cys-230 and Lys-238 do not act as an acid-base pair in the deprotonation of biotin, but may be involved in ATP binding	654575	-	-	r
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, two complete active sites per homodimer	656018	-	-	?
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	the biotin carboxylase component of acetyl-CoA carboxylase catalyzes the ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding and in catalysis orienting ATP in a conformation that allows for optimal catalysis, mechanism	656008	-	-	r
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	the biotin carboxylase component of acetyl-CoA carboxylase catalyzes the first half-reaction of the reaction catalyzed by acetyl-CoA carboxylase, the half-reaction involves the phosphorylation of bicarbonate by ATP to form a carboxyphosphate intermediate, followed by transfer of the carboxyl group to biotin to form carboxybiotin, in vivo biotin is attached to biotin-carboxyl-carrier protein, the C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein form a domain that acts as excellent substrate	655973	-	-	r
ATP + biotin-carboxyl-carrier protein + HCO3-	?		Escherichia coli	-	the acetyl-CoA carboxylase catalyzes the first commited step in the biosynthesis of long chain fatty acids, the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein	1431	-	-	-
ATP + D-(+)-biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	-	1428	-	-	-
ATP + D-(+)-biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	sequential mechanism, in which HCO3- is activated by ATP in a first step	1422	-	-	-
ATP + D-(+)-biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	L-biotin is completely inactive	1421	-	1421	-
ATP + D-(+)-biotin + HCO3-	ADP + phosphate + carboxybiotin		Escherichia coli	-	L-biotin is completely inactive	1426	-	-	-
ATP + d-biotin + HCO3-	ADP + phosphate + carboxy-d-biotin		Pisum sativum	-	BC component of the multisubunit complex of acetyl-CoA carboxylase	654339	-	-	?
GTP + biotin-carboxyl-carrier protein + HCO3-	GDP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	1421	-	-	-
GTP + D-biotin + HCO3-	GDP + phosphate + carboxybiotin		Escherichia coli	-	-	1421	-	-	-
additional information	?	-	Escherichia coli	-	enzyme catalyzes ATP-hydrolysis in absence of biotin	1420, 1421	-	-	-
additional information	?	-	Myxococcus xanthus	Q9FAF5	AccA is a biotinylated protein mainly expressed in the exponential growth phase	651665	-	-	-
additional information	?	-	Aquifex aeolicus	-	BC subunit of pyruvate carboxylase, which is involved in gluconeogenesis	654115	-	-	-
additional information	?	-	Escherichia coli	-	fatty acid synthesis	655535, 655978	-	-	-
additional information	?	-	Escherichia coli	-	long-chain fatty acid synthesis	654575	-	-	-
additional information	?	-	Pisum sativum	-	pathway from acetyl-CoA to long-chain fatty acids, developmental regulation of enzyme	654339	-	-	-
additional information	?	-	Escherichia coli	-	biotin carboxylase catalyzes a slow bicarbonate-dependent ATP hydrolysis reaction in the absence of biotin	654575	-	-	-
additional information	?	-	Escherichia coli	-	in absence of biotin enzyme also catalyzes a slow bicarbonate-dependent ATP hydrolysis	656207	-	-	-
additional information	?	-	Escherichia coli	-	in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATP hydrolysis at a slow rate	656008	-	-	-
additional information	?	-	Escherichia coli	-	in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATPase reaction at a 1100fold slower rate than in the presence of biotin	654566	-	-	-
additional information	?	-	Escherichia coli	-	the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase	693839	-	-	-
additional information	?	-	Staphylococcus aureus, Escherichia coli, Pseudomonas aeruginosa	-	active site structure, substrate binding and structure-function relationship analysis, overview	695008	-	-	-
additional information	?	-	Homo sapiens	-	mechanism of ACC holoenzyme function, structure of the biotinoyl domain of isozyme ACC2, overview	695042	-	-	-
additional information	?	-	Escherichia coli	-	mechanism of ACC holoenzyme function, structure of the biotinoyl domain, overview. In thei BCCP, Glu 119 and Glu147 interact with the basic residues in BirA, overview	695042	-	-	-
additional information	?	-	Escherichia coli	-	molecular dynamics simulations of wild-type enzyme and active-site mutant E288K, overview	693839	-	-	-
additional information	?	-	Chlorobium limicola, Cupriavidus metallidurans, Cytophaga hutchinsonii	-	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Metallosphaera sedula	Q8J2Z4	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Sulfolobus metallicus	O52602	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Chlorobium phaeobacteroides, Methanosarcinales	-	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Synechococcus sp.	Q54755	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Pelobacter propionicus	A1ANN6	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	uncultured bacterium	B1GX36	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Maribacter sp. HTCC2170	A4APF1	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	A4SVB6	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Polaromonas sp.	Q12EJ0	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Chloroflexus aurantiacus	A9W9X0	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Hyperthermus butylicus	A2BLY3	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Natronomonas pharaonis	Q3INT5	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Halobacterium salinarum	Q9HPP8	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Nitrosopumilus maritimus	A9A3E8	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Sulfolobus solfataricus	Q97V46	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Acidianus brierleyi	Q877I5	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Sulfolobus tokodaii	Q974R7	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Trichodesmium erythraeum	Q10YA8	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Geobacter uraniireducens	A5G5L1	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Pelobacter carbinolicus	Q3A2P1	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Cenarchaeum symbiosum	A0RY62	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-
additional information	?	-	Methanococcales	-	the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase	692103	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Chlorobium limicola	-	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Staphylococcus aureus, Escherichia coli	-	-	695008	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	-	695042	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pseudomonas aeruginosa	-	-	695008	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Cupriavidus metallidurans, Cytophaga hutchinsonii	-	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Metallosphaera sedula	Q8J2Z4	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Sulfolobus metallicus	O52602	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Chlorobium phaeobacteroides, Methanosarcinales	-	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Synechococcus sp.	Q54755	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pelobacter propionicus	A1ANN6	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		uncultured bacterium	B1GX36	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Maribacter sp. HTCC2170	A4APF1	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	A4SVB6	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Polaromonas sp.	Q12EJ0	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Chloroflexus aurantiacus	A9W9X0	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Hyperthermus butylicus	A2BLY3	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Natronomonas pharaonis	Q3INT5	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Halobacterium salinarum	Q9HPP8	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Nitrosopumilus maritimus	A9A3E8	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Sulfolobus solfataricus	Q97V46	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Acidianus brierleyi	Q877I5	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Sulfolobus tokodaii	Q974R7	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Trichodesmium erythraeum	Q10YA8	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Geobacter uraniireducens	A5G5L1	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Pelobacter carbinolicus	Q3A2P1	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Cenarchaeum symbiosum	A0RY62	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Methanococcales	-	-	692103	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committed step in fatty acid synthesis	693839	-	-
ATP + biotin-carboxyl-carrier protein + CO2	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Homo sapiens	-	The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview	695042	-	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue	654566	-	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase	656207	-	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	first half reaction of the first committed step in the biosynthesis of long-chain fatty acids, in vivo the biotin substrate is attached to biotin-carboxyl-carrier protein, natural substrate	655973	-	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	long-chain fatty acid synthesis, in vivo biotin is covalently attached to the biotin-carboxyl-carrier protein	654403	-	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue	656008	-	-
ATP + biotin-carboxyl-carrier protein + HCO3-	ADP + phosphate + carboxybiotin-carboxyl-carrier protein		Escherichia coli	-	one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to the biotin-carboxyl-carrier protein in vivo, fatty acid synthesis	656018	-	-
ATP + biotin-carboxyl-carrier protein + HCO3-	?		Escherichia coli	-	the acetyl-CoA carboxylase catalyzes the first commited step in the biosynthesis of long chain fatty acids, the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein	1431	-	-
additional information	?	-	Myxococcus xanthus	Q9FAF5	AccA is a biotinylated protein mainly expressed in the exponential growth phase	651665	-	-
additional information	?	-	Aquifex aeolicus	-	BC subunit of pyruvate carboxylase, which is involved in gluconeogenesis	654115	-	-
additional information	?	-	Escherichia coli	-	fatty acid synthesis	655535, 655978	-	-
additional information	?	-	Escherichia coli	-	long-chain fatty acid synthesis	654575	-	-
additional information	?	-	Pisum sativum	-	pathway from acetyl-CoA to long-chain fatty acids, developmental regulation of enzyme	654339	-	-
additional information	?	-	Escherichia coli	-	the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase	693839	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ATP	Aquifex aeolicus	-	structure of the ATP-binding site	654115	2D-image
ATP	Pisum sativum	-	ATP-dependent	654339	2D-image
ATP	Escherichia coli	-	-	654403, 695008	2D-image
ATP	Escherichia coli	-	ATP-dependent, Cys-230 and Lys-238 may be involved in binding ATP	654575	2D-image
ATP	Escherichia coli	-	Lys-238 is an ATP-binding residue and interacts with the gamma-phosphate group of ATP, electrostatic interaction	655535	2D-image
ATP	Escherichia coli	-	ATP-dependent, mode of binding, Lys-116, His-236 and Glu-201 are involved in binding ATP, the biotin carboxylase B-domain moves as a result of ATP binding	655978	2D-image
ATP	Escherichia coli	-	Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding	656008	2D-image
ATP	Escherichia coli	-	ATP-dependent	656018, 693839, 695042	2D-image
ATP	Acidianus brierleyi	Q877I5	-	692103	2D-image
ATP	Cenarchaeum symbiosum	A0RY62	-	692103	2D-image
ATP	Chlorobium limicola, Chlorobium phaeobacteroides	-	-	692103	2D-image
ATP	Chloroflexus aurantiacus	A9W9X0	-	692103	2D-image
ATP	Cupriavidus metallidurans, Cytophaga hutchinsonii	-	-	692103	2D-image
ATP	Geobacter uraniireducens	A5G5L1	-	692103	2D-image
ATP	Halobacterium salinarum	Q9HPP8	-	692103	2D-image
ATP	Hyperthermus butylicus	A2BLY3	-	692103	2D-image
ATP	Maribacter sp. HTCC2170	A4APF1	-	692103	2D-image
ATP	Metallosphaera sedula	Q8J2Z4	-	692103	2D-image
ATP	Methanococcales, Methanosarcinales	-	-	692103	2D-image
ATP	Natronomonas pharaonis	Q3INT5	-	692103	2D-image
ATP	Nitrosopumilus maritimus	A9A3E8	-	692103	2D-image
ATP	Pelobacter carbinolicus	Q3A2P1	-	692103	2D-image
ATP	Pelobacter propionicus	A1ANN6	-	692103	2D-image
ATP	Polaromonas sp.	Q12EJ0	-	692103	2D-image
ATP	Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	A4SVB6	-	692103	2D-image
ATP	Sulfolobus metallicus	O52602	-	692103	2D-image
ATP	Sulfolobus solfataricus	Q97V46	-	692103	2D-image
ATP	Sulfolobus tokodaii	Q974R7	-	692103	2D-image
ATP	Synechococcus sp.	Q54755	-	692103	2D-image
ATP	Trichodesmium erythraeum	Q10YA8	-	692103	2D-image
ATP	uncultured bacterium	B1GX36	-	692103	2D-image
ATP	Pseudomonas aeruginosa, Staphylococcus aureus	-	-	695008	2D-image
ATP	Homo sapiens	-	ATP-dependent	695042	2D-image

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Co2+	Escherichia coli	-	divalent metal ion required, Mg2+, Mn2+ or Co2+	1420, 1421, 1426
K+	Escherichia coli	-	required	1422
Mg2+	Escherichia coli	-	divalent metal ion required, Mg2+, Mn2+ or Co2+; Km: 0.57 mM	1420
Mg2+	Escherichia coli	-	divalent metal ion required, Mg2+, Mn2+ or Co2+	1421, 1426
Mg2+	Escherichia coli	-	required	1422, 1424
Mg2+	Escherichia coli	-	requirement	654403, 654575, 655973, 655978, 656207
Mg2+	Escherichia coli	-	requires two equivalents of magnesium for activity	654566
Mg2+	Escherichia coli	-	requires two equivalents of magnesium for activity, one is complexed to ATP, the role of the other is unknown	656008
Mg2+	Acidianus brierleyi	Q877I5	-	692103
Mg2+	Cenarchaeum symbiosum	A0RY62	-	692103
Mg2+	Chlorobium limicola, Chlorobium phaeobacteroides	-	-	692103
Mg2+	Chloroflexus aurantiacus	A9W9X0	-	692103
Mg2+	Cupriavidus metallidurans, Cytophaga hutchinsonii	-	-	692103
Mg2+	Geobacter uraniireducens	A5G5L1	-	692103
Mg2+	Halobacterium salinarum	Q9HPP8	-	692103
Mg2+	Hyperthermus butylicus	A2BLY3	-	692103
Mg2+	Maribacter sp. HTCC2170	A4APF1	-	692103
Mg2+	Metallosphaera sedula	Q8J2Z4	-	692103
Mg2+	Methanococcales, Methanosarcinales	-	-	692103
Mg2+	Natronomonas pharaonis	Q3INT5	-	692103
Mg2+	Nitrosopumilus maritimus	A9A3E8	-	692103
Mg2+	Pelobacter carbinolicus	Q3A2P1	-	692103
Mg2+	Pelobacter propionicus	A1ANN6	-	692103
Mg2+	Polaromonas sp.	Q12EJ0	-	692103
Mg2+	Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	A4SVB6	-	692103
Mg2+	Sulfolobus metallicus	O52602	-	692103
Mg2+	Sulfolobus solfataricus	Q97V46	-	692103
Mg2+	Sulfolobus tokodaii	Q974R7	-	692103
Mg2+	Synechococcus sp.	Q54755	-	692103
Mg2+	Trichodesmium erythraeum	Q10YA8	-	692103
Mg2+	uncultured bacterium	B1GX36	-	692103
Mg2+	Escherichia coli	-	coordinating interactions of active-site metal ions in wild-type and mutant enzymes, Mg2+ is bridged between the alpha- and gamma-phosphoryl group of ATP and coordinated to E288, E276, and a water molecule, detailed overview	693839
Mg2+	Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus	-	binding sites structure	695008
Mg2+	Escherichia coli, Homo sapiens	-	-	695042
Mn2+	Escherichia coli	-	divalent metal ion required, Mg2+, Mn2+ or Co2+; Km: 0.11 mM	1420
Mn2+	Escherichia coli	-	divalent metal ion required, Mg2+, Mn2+ or Co2+	1421, 1426

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide	Escherichia coli	-	minimal inhibitory concentration above 64 microg per ml for wild-type, 16 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption	701439	2D-image
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide	Haemophilus influenzae	-	minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA	701439	2D-image
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide	Moraxella catarrhalis	-	minimal inhibitory concentration 8 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA	701439	2D-image
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide	Escherichia coli	-	minimal inhibitory concentration above 64 microg per ml for wild-type, 8 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption	701439	2D-image
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide	Haemophilus influenzae	-	minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA	701439	2D-image
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide	Moraxella catarrhalis	-	minimal inhibitory concentration 16 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA	701439	2D-image
2-Pyridyl disulfide	Escherichia coli	-	-	1420	2D-image
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	minimal inhibitory concentration 16 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption	701439	2D-image
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Haemophilus influenzae	-	minimal inhibitory concentration 0.125 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump acrA	701439	2D-image
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Moraxella catarrhalis	-	minimal inhibitory concentration 1 microg per ml for wild-type, 0.5 microg per ml for mutant with targeted knock-out of efflux pump acrA	701439	2D-image
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse	706519	2D-image
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse	706519	2D-image
adenosine diphosphopyridoxal	Escherichia coli	-	ATP, ADP, inorganic phosphate and bicarbonate protect against inhibition	655535	2D-image
ADP	Escherichia coli	-	-	1421	2D-image
biotin	Escherichia coli	-	above 300 mM, noncompetitive substrate inhibitor	654403	2D-image
Co2+	Escherichia coli	-	above 2 mM	1426	2D-image
ethanol	Escherichia coli	-	maximal activation, 10fold, at 15% v/v. Inactivation at 20% v/v	1426	2D-image
GDP	Escherichia coli	-	-	1421	2D-image
N-ethylmaleimide	Escherichia coli	-	pH-dependent inhibition, reacts with Lys-238	654575	2D-image
NEM	Escherichia coli	-	-	1420	2D-image
Phosphonoacetate	Escherichia coli	-	competitive inhibition versus ATP, noncompetitive versus bicarbonate	654403	2D-image
phosphonoacetate linked to the 1'-nitrogen of biotin	Escherichia coli	-	reaction intermediate analog, modest inhibition, competitive versus ATP, noncompetitive versus biotin	654403	2D-image
soraphen	Magnaporthe grisea, Phytophthora infestans, Ustilago maydis	-	-	660969	2D-image
soraphen A	Saccharomyces cerevisiae	Q00955	nanomolar inhibitor against biotin carboxylase domain of acetyl-coenzyme A carboxylase. The inhibitor may bind in the biotin carboxylase dimer interface and inhibits the biotin carboxylase activity by disrupting the oligomerization of the domain	662830	2D-image
soraphen A	Homo sapiens	O00763	macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase	702083	2D-image
Thionucleotides	Escherichia coli	-	-	1420	-
Mn2+	Escherichia coli	-	above 2 mM	1426	2D-image
additional information	Escherichia coli	-	no substrate inhibition by ATP	654403	-
additional information	Escherichia coli	-	not inhibited by PLP	655535	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
acetyl-CoA	Staphylococcus aureus	Q99UY9	allosteric activator of holoenzyme. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent	706790	2D-image
biotin	Escherichia coli	-	required for activation of the ATP synthesis reaction with carbamoyl phosphate and ADP as substrates, E211, E288, N290 and R292 are responsible, at least in part, for the substrate-induced synergism by biotin, activation via a conformational change of enzyme	654566	2D-image
biotin	Escherichia coli	-	activates the ATP synthesis reaction with ADP and carbamoyl phosphate as substrates	654575, 656008	2D-image
biotin	Escherichia coli	-	substrate-induced synergism, the reaction in presence of biotin is 1100fold faster than in its absence	695008	2D-image
biotin	Pseudomonas aeruginosa	-	substrate induced synergism, the reaction inpresence of biotin is 1100fold faster than in its absence	695008	2D-image
biotin	Staphylococcus aureus	-	substrate-induced synergism, the reaction in presence of biotin is 1100fold faster than in its absence	695008	2D-image
ethanol	Escherichia coli	-	maximal activation, 10fold, at 15% v/v. Inactivation at 20% v/v	1426	2D-image
ethanol	Escherichia coli	-	maximal activation, 11fold at 15%	1428	2D-image

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.08	-	ADP	Escherichia coli	-	pH 8, 25�C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate	654566	2D-image
0.18	-	ADP	Escherichia coli	-	pH 8, 25�C, E211A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate	654566	2D-image
0.19	-	ADP	Escherichia coli	-	pH 8, 25�C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate	656008	2D-image
0.23	-	ADP	Escherichia coli	-	pH 8, 25�C, E288A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate	654566	2D-image
0.4	-	ADP	Escherichia coli	-	pH 8, 25�C, N290A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate	654566	2D-image
0.83	-	ADP	Escherichia coli	-	pH 8, 25�C, R292A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate	654566	2D-image
0.081	-	ATP	Escherichia coli	-	25�C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
0.093	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, mutant enzyme E23R	675923	2D-image
0.0948	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, mutant enzyme R19E	675923	2D-image
0.1049	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, mutant enzyme F363A	675923	2D-image
0.1152	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, wild-type enzyme	675923	2D-image
0.17	-	ATP	Escherichia coli	-	wild-type BC	655535	2D-image
3.3	-	ATP	Escherichia coli	-	mutant G165V, pH 8.0, 25�C	706634	2D-image
3.4	-	ATP	Escherichia coli	-	mutant G166V, pH 8.0, 25�C	706634	2D-image
3.8	-	ATP	Escherichia coli	-	mutant G165V/G166V, pH 8.0, 25�C	706634	2D-image
4.23	-	ATP	Escherichia coli	-	25�C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
6.87	-	ATP	Escherichia coli	-	25�C, K238Q mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
8.6	-	ATP	Escherichia coli	-	K238Q mutant	655535	2D-image
13	-	ATP	Escherichia coli	-	K238R mutant	655535	2D-image
21	-	ATP	Escherichia coli	-	K238A mutant	655535	2D-image
22.7	-	biotin	Escherichia coli	-	pH 7.4, mutant E296A	704465	2D-image
25	-	biotin	Escherichia coli	-	R338S mutant	656207	2D-image
33.6	-	biotin	Escherichia coli	-	pH 8, 25�C, E211A mutant	654566	2D-image
35.1	-	biotin	Escherichia coli	-	pH 7.4 wild-type	704465	2D-image
41.8	-	biotin	Escherichia coli	-	pH 7.4, mutant R338A	704465	2D-image
50.9	-	biotin	Geobacillus thermodenitrificans	-	recombinant biotin carboxylase domain of pyruvate carboxylase	651171	2D-image
56	-	biotin	Escherichia coli	-	M169K mutant	656207	2D-image
60.1	-	biotin	Escherichia coli	-	pH 8, 25�C, N290A mutant	654566	2D-image
60.1	-	biotin	Escherichia coli	-	N290A mutant, homodimer	656018	2D-image
64	-	biotin	Escherichia coli	-	pH 8, 25�C, hybrid dimer K238Q/WT	656018	2D-image
67.6	-	biotin	Escherichia coli	-	pH 8, 25�C, E288A mutant	654566	2D-image
84.8	-	biotin	Escherichia coli	-	free biotin	655973	2D-image
122	-	biotin	Escherichia coli	-	25�C, free biotin, wild-type enzyme	654575	2D-image
123.6	-	biotin	Escherichia coli	-	pH 8, 25�C, R292A mutant	654566	2D-image
123.6	-	biotin	Escherichia coli	-	R292A mutant, homodimer	656018	2D-image
125	-	biotin	Escherichia coli	-	pH 8, 25�C, K159Q mutant	656008	2D-image
134	-	biotin	Escherichia coli	-	-	654403	2D-image
134	-	biotin	Escherichia coli	-	pH 8, 25�C, wild-type enzyme	654566	2D-image
134	-	biotin	Escherichia coli	-	wild-type enzyme	656008, 656207	2D-image
137	-	biotin	Escherichia coli	-	pH 8, 25�C, E276Q mutant	656008	2D-image
140	-	biotin	Escherichia coli	-	K238Q mutant	655535	2D-image
143	-	biotin	Escherichia coli	-	R338Q mutant	656207	2D-image
147	-	biotin	Escherichia coli	-	pH 8, 25�C, K116A mutant	656008	2D-image
160	-	biotin	Escherichia coli	-	wild-type BC	655535	2D-image
167	-	biotin	Escherichia coli	-	25�C, free biotin, C230A mutant	654575	2D-image
180	-	biotin	Escherichia coli	-	K238A and K238R mutant	655535	2D-image
186	-	biotin	Escherichia coli	-	mutant G166V, pH 8.0, 25�C	706634	2D-image
192.7	-	biotin	Escherichia coli	-	pH 8, 25�C, wild-type enzyme, homodimer	656018	2D-image
256	-	biotin	Escherichia coli	-	mutant G165V, pH 8.0, 25�C	706634	2D-image
321	-	biotin	Escherichia coli	-	mutant G165V/G166V, pH 8.0, 25�C	706634	2D-image
1234	-	biotin	Escherichia coli	-	pH 8, 25�C, H209A mutant	656008	2D-image
0.16	-	biotin-carboxyl-carrier protein	Escherichia coli	-	C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein	655973	2D-image
0.51	-	Carbamoyl phosphate	Escherichia coli	-	pH 8, 25�C, E211A mutant, ATP synthesis reaction with ADP as cosubstrate	654566	2D-image
2.3	-	Carbamoyl phosphate	Escherichia coli	-	pH 8, 25�C, E288A mutant, ATP synthesis reaction with ADP as cosubstrate	654566	2D-image
2.8	-	Carbamoyl phosphate	Escherichia coli	-	pH 8, 25�C, R292A mutant, ATP synthesis reaction with ADP as cosubstrate	654566	2D-image
4.8	-	Carbamoyl phosphate	Escherichia coli	-	pH 8, 25�C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate	656008	2D-image
11.2	-	Carbamoyl phosphate	Escherichia coli	-	pH 8, 25�C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate	654566	2D-image
62.2	-	CO2	Geobacillus thermodenitrificans	-	recombinant biotin carboxylase domain of pyruvate carboxylase	651171	2D-image
0.0076	-	CoATP2-	Escherichia coli	-	-	1420	2D-image
170	-	D-(+)-biotin	Escherichia coli	-	-	1421, 1428	2D-image
0.37	-	HCO3-	Escherichia coli	-	25�C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
0.5	-	HCO3-	Escherichia coli	-	mutant G165V/G166V, pH 8.0, 25�C	706634	2D-image
0.7	-	HCO3-	Escherichia coli	-	25�C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
0.8	-	HCO3-	Escherichia coli	-	mutant G166V, pH 8.0, 25�C	706634	2D-image
1.7	-	HCO3-	Escherichia coli	-	mutant G165V, pH 8.0, 25�C	706634	2D-image
1.8	-	HCO3-	Escherichia coli	-	wild-type BC	655535	2D-image
2.9	-	HCO3-	Escherichia coli	-	-	1421, 1428	2D-image
3.7	-	HCO3-	Escherichia coli	-	K238A mutant	655535	2D-image
3.9	-	HCO3-	Escherichia coli	-	K238Q mutant	655535	2D-image
6.8	-	HCO3-	Escherichia coli	-	K238R mutant	655535	2D-image
16.2	-	HCO3-	Escherichia coli	-	pH 8.5, wild-type	704465	2D-image
18.9	-	HCO3-	Escherichia coli	-	pH 8.5, mutant R338A	704465	2D-image
57.5	-	HCO3-	Escherichia coli	-	pH 8.5, mutant E296A	704465	2D-image
0.0398	-	MgADP-	Escherichia coli	-	-	1420	2D-image
0.0546	-	MgATP2-	Escherichia coli	-	-	1420	2D-image
0.11	-	MgATP2-	Escherichia coli	-	-	1421, 1428	2D-image
0.00126	-	MnADP-	Escherichia coli	-	-	1420	2D-image
0.0025	-	MnATP2-	Escherichia coli	-	-	1420	2D-image
additional information	-	additional information	Escherichia coli	-	ordered kinetic mechanism	654403	-
additional information	-	additional information	Escherichia coli	-	-	654566, 654575, 656008	-
additional information	-	additional information	Escherichia coli	-	kinetic data	656207	-

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.0012	-	ATP	Escherichia coli	-	25�C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
0.0017	-	ATP	Escherichia coli	-	25�C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
0.00195	-	ATP	Escherichia coli	-	25�C, K238Q mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin	654575	2D-image
0.071	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, mutant enzyme E23R	675923	2D-image
0.075	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, mutant enzyme R19E	675923	2D-image
0.207	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, mutant enzyme F363A	675923	2D-image
0.228	-	ATP	Escherichia coli	-	biotin-dependent ATP hydrolysis, wild-type enzyme	675923	2D-image
0.513	-	ATP	Escherichia coli	-	25�C, C230A mutant, biotin-dependent ATP hydrolysis	654575	2D-image
1.23	-	ATP	Escherichia coli	-	25�C, wild-type enzyme, biotin-dependent ATP hydrolysis	654575	2D-image
0.0025	-	biotin	Escherichia coli	-	pH 7.4, mutant R338A	704465	2D-image
0.0037	-	biotin	Escherichia coli	-	mutant G166V, pH 8.0, 25�C	706634	2D-image
0.005	-	biotin	Escherichia coli	-	mutant G165V, pH 8.0, 25�C	706634	2D-image
0.007	-	biotin	Escherichia coli	-	mutant G165V/G166V, pH 8.0, 25�C	706634	2D-image
0.028	-	biotin	Escherichia coli	-	pH 7.4, mutant E296A	704465	2D-image
0.58	-	biotin	Escherichia coli	-	pH 7.4 wild-type	704465	2D-image
1.05	-	biotin	Escherichia coli	-	Vmax, free biotin	655973	2D-image
16.68	-	biotin-carboxyl-carrier protein	Escherichia coli	-	Vmax, C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein	655973	2D-image
0.0016	-	HCO3-	Escherichia coli	-	mutant G165V/G166V, pH 8.0, 25�C; mutant G166V, pH 8.0, 25�C	706634	2D-image
0.0019	-	HCO3-	Escherichia coli	-	pH 8.5, mutant R338A	704465	2D-image
0.0025	-	HCO3-	Escherichia coli	-	mutant G165V, pH 8.0, 25�C	706634	2D-image
0.034	-	HCO3-	Escherichia coli	-	pH 8.5, mutant E296A	704465	2D-image
0.44	-	HCO3-	Escherichia coli	-	pH 8.5, wild-type	704465	2D-image
additional information	-	additional information	Escherichia coli	-	-	654566, 654575, 656008, 656018	-
additional information	-	additional information	Escherichia coli	-	kinetic data	656207	-

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
6e-05	-	biotin	Escherichia coli	-	pH 7.4, mutant R338A	704465	8026
0.00123	-	biotin	Escherichia coli	-	pH 7.4, mutant E296A	704465	8026
0.0165	-	biotin	Escherichia coli	-	pH 7.4 wild-type	704465	8026
0.0001	-	HCO3-	Escherichia coli	-	pH 8.5, mutant R338A	704465	11306
0.000594	-	HCO3-	Escherichia coli	-	pH 8.5, mutant E296A	704465	11306
0.0272	-	HCO3-	Escherichia coli	-	pH 8.5, wild-type	704465	11306

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
7	-	Phosphonoacetate	Escherichia coli	-	-	654403	2D-image
8	-	phosphonoacetate linked to the 1'-nitrogen of biotin	Escherichia coli	-	-	654403	2D-image

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
5e-06	-	6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	or below, wild-type	706519	2D-image
0.00016	-	6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	mutant H438P	706519	2D-image
0.00056	-	6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	mutant I437T	706519	2D-image
2.8e-05	-	6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	wild-type	706519	2D-image
0.0012	-	6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	wild-type	706519	2D-image
0.0073	-	6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	wild-type	706519	2D-image

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	-	Escherichia coli	-	-	1420, 1421, 1426
additional information	-	Pisum sativum	-	-	654339
additional information	-	Escherichia coli	-	-	655535

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.5	-	Escherichia coli	-	Mn2+-activated reaction	1426
7.3	-	Escherichia coli	-	assay at	695042
8	-	Escherichia coli	-	Mg2+-activated reaction	1426
8	-	Pisum sativum	-	assay at	654339
8	-	Escherichia coli	-	assay at	654566, 656008, 656018, 656207

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
25	-	Pisum sativum	-	assay at	654339
25	-	Escherichia coli	-	assay at	654566, 654575, 656008, 656018, 656207
30	-	Escherichia coli	-	assay at	695042
37	-	Escherichia coli	-	assay at	656207

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
endosperm	Jatropha curcas	F2WMV4	expression of the accA, accB1, accC and accD genes in Jatropha endosperm varies greatly at different developmental stages. The peak expression of the four genes is observed at about 42 days after fertilization when storage lipids are synthesized at their maximal levels	716633
leaf	Nicotiana tabacum	-	-	1436
leaf	Pisum sativum	-	developing, 7 days old	654339
leaf	Jatropha curcas	F2WMV4	-	716633
seed	Pisum sativum	-	7 days old	654339

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
chloroplast	Arabidopsis thaliana	-	-	9507	1434
chloroplast	Pisum sativum	-	BC is present in the major plastid compartments envelopes, stroma and thylakoids, but predominantly localized in the stroma, presumably due to partial dissociation as a result of the isolation procedure	9507	654339
chloroplast	Jatropha curcas	F2WMV4	sequence contains a potential 50-amino acid chloroplast transit peptide	9507	716633
membrane	Pisum sativum	-	might be associated with the membrane, BC of the undissociated complex acetyl-CoA carboxylase	16020	654339
plastid	Medicago sativa, Nicotiana tabacum, Pisum sativum, Ricinus communis	-	-	9536	37620

PDB	SCOP	CATH	ORGANISM
3ouu, download	SCOP (3ouu)	CATH (3ouu)	Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
3ouz, download	SCOP (3ouz)	CATH (3ouz)	Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
1bnc, download	SCOP (1bnc)	CATH (1bnc)	Escherichia coli (strain K12)
1dv1, download	SCOP (1dv1)	CATH (1dv1)	Escherichia coli (strain K12)
1dv2, download	SCOP (1dv2)	CATH (1dv2)	Escherichia coli (strain K12)
1k69, download	SCOP (1k69)	CATH (1k69)	Escherichia coli (strain K12)
2gps, download	SCOP (2gps)	CATH (2gps)	Escherichia coli (strain K12)
2gpw, download	SCOP (2gpw)	CATH (2gpw)	Escherichia coli (strain K12)
2j9g, download	SCOP (2j9g)	CATH (2j9g)	Escherichia coli (strain K12)
2v58, download	SCOP (2v58)	CATH (2v58)	Escherichia coli (strain K12)
2v59, download	SCOP (2v59)	CATH (2v59)	Escherichia coli (strain K12)
2v5a, download	SCOP (2v5a)	CATH (2v5a)	Escherichia coli (strain K12)
2vr1, download	SCOP (2vr1)	CATH (2vr1)	Escherichia coli (strain K12)
2w6m, download	SCOP (2w6m)	CATH (2w6m)	Escherichia coli (strain K12)
2w6n, download	SCOP (2w6n)	CATH (2w6n)	Escherichia coli (strain K12)
2w6o, download	SCOP (2w6o)	CATH (2w6o)	Escherichia coli (strain K12)
2w6p, download	SCOP (2w6p)	CATH (2w6p)	Escherichia coli (strain K12)
2w6q, download	SCOP (2w6q)	CATH (2w6q)	Escherichia coli (strain K12)
2w6z, download	SCOP (2w6z)	CATH (2w6z)	Escherichia coli (strain K12)
2w70, download	SCOP (2w70)	CATH (2w70)	Escherichia coli (strain K12)
2w71, download	SCOP (2w71)	CATH (2w71)	Escherichia coli (strain K12)
3g8c, download	SCOP (3g8c)	CATH (3g8c)	Escherichia coli (strain K12)
3g8d, download	SCOP (3g8d)	CATH (3g8d)	Escherichia coli (strain K12)
3jzf, download	SCOP (3jzf)	CATH (3jzf)	Escherichia coli (strain K12)
3jzi, download	SCOP (3jzi)	CATH (3jzi)	Escherichia coli (strain K12)
3rup, download	SCOP (3rup)	CATH (3rup)	Escherichia coli (strain K12)
3rv3, download	SCOP (3rv3)	CATH (3rv3)	Escherichia coli (strain K12)
3rv4, download	SCOP (3rv4)	CATH (3rv4)	Escherichia coli (strain K12)
2kcc, download	SCOP (2kcc)	CATH (2kcc)	Homo sapiens
2yl2, download	SCOP (2yl2)	CATH (2yl2)	Homo sapiens
3ff6, download	SCOP (3ff6)	CATH (3ff6)	Homo sapiens
3gid, download	SCOP (3gid)	CATH (3gid)	Homo sapiens
3glk, download	SCOP (3glk)	CATH (3glk)	Homo sapiens
3jrw, download	SCOP (3jrw)	CATH (3jrw)	Homo sapiens
3jrx, download	SCOP (3jrx)	CATH (3jrx)	Homo sapiens
4asi, download	SCOP (4asi)	CATH (4asi)	Homo sapiens
2c00, download	SCOP (2c00)	CATH (2c00)	Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
2vqd, download	SCOP (2vqd)	CATH (2vqd)	Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
3h0j, download	SCOP (3h0j)	CATH (3h0j)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3h0q, download	SCOP (3h0q)	CATH (3h0q)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3h0s, download	SCOP (3h0s)	CATH (3h0s)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3k8x, download	SCOP (3k8x)	CATH (3k8x)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3tv5, download	SCOP (3tv5)	CATH (3tv5)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3tvu, download	SCOP (3tvu)	CATH (3tvu)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3tvw, download	SCOP (3tvw)	CATH (3tvw)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3tz3, download	SCOP (3tz3)	CATH (3tz3)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
2vpq, download	SCOP (2vpq)	CATH (2vpq)	Staphylococcus aureus (strain Mu50 / ATCC 700699)

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
95000	-	Escherichia coli	-	gel filtration, analytical ultracentrifugation	1421, 1428
additional information	-	Escherichia coli	-	X-ray model of the enzyme. Those amino acid residues believed to form part of the active site pocket include His209-Glu211, His236-Glu241, Glu276, Ile287-Glu296, and Arg338	1433

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Escherichia coli	-	x * 49320, calculation from nucleotide sequence	1429
?	Corynebacterium glutamicum	-	x * 63400, calculation from nucleotide sequence, protein composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein	1437
?	Myxococcus xanthus	Q9FAF5	x * 61500, sequence calculation, x * 65000, SDS-PAGE	651665
?	Escherichia coli	-	x * 51000, SDS-PAGE	655535
?	Ustilago maydis	-	x * 64700, recombinant biotin carboxylase domain	660969
?	Sulfolobus metallicus	O52602	x * 60000, SDS-PAGE, x * 58235, calculated	677847
?	Jatropha curcas	F2WMV4	x * 58300, calculated	716633
dimer	Escherichia coli	-	2 * 51000, SDS-PAGE	1420, 1428
dimer	Escherichia coli	-	-	1421, 655978
dimer	Escherichia coli	-	2 * 50000, SDS-PAGE	1426
dimer	Aquifex aeolicus	-	2 * 50000	654115
dimer	Geobacillus thermodenitrificans	-	-	671061
dimer	Escherichia coli	-	wild-type enzyme, dimerization is not an absolute requirement for the catalytic activity of the Escherichia coli biotin carboxylase subunit	675923
dimer	Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus	-	homodimer	695008
homodimer	Escherichia coli	-	2 * 50000	654566, 654575, 655973, 656008
homodimer	Escherichia coli	-	2 * 50000, both subunits are required for activity and the two subunits must be in communication during enzyme function	656018
homodimer	Escherichia coli	-	2 * 50000, cooperativity between the subunits	656207
monomer	Escherichia coli	-	mutant enzyme R19E and E23R are monomeric in solution	675923
additional information	Escherichia coli	-	the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein	1421
additional information	Escherichia coli	-	geometry of the consensus Met-Lys-Met, MKM, motif, and structure of the biotinoyl domain of BCCP, overview. Binding pattern and interacting surfaces for the biotinoyl domain with BirA, overview	695042
additional information	Homo sapiens	-	3D structure of the hACC2 biotinoyl domain, geometry of the consensus Met-Lys-Met, MKM, motif, overview. The biotin group of hACC2 does not affect the structure of the biotinoyl domain, the human enzyme does not possess a thumb structure. Binding pattern and interacting surfaces for the ACC2 biotinoyl domain with Escherichia coli BirA enzyme, overview	695042
additional information	Jatropha curcas	F2WMV4	biotin carboxylase contains three conserved domains, an N-terminal domain of carbamoyl-phosphate synthase L chain residues 73-181, a ATP binding domain of carbamoyl-phosphate synthase L chain, residues 186-395, and a C-terminal domain of biotin carboxylase	716633

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
proteolytic modification	Jatropha curcas	F2WMV4	sequence contains a potential 50-amino acid chloroplast transit peptide	716633

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
hanging-drop vapor-diffusion method, X-ray analysis	Aquifex aeolicus	-	654115
-	Escherichia coli	-	1421, 1426, 1427, 1431
enzyme in complex with ATP analogues AMP-PNP and ADP-CF2P, hanging drop vapour diffusion, from 0.1 M Bis-Tris, pH 6.5, 0.2 M CaCl2, 45% methylpentanediol, and 10% ethylene glycol or 0.1 M KCl, 3-8% PEG 8000 and 20% ethylene glycol, respectively, X-ray diffraction structure determination and analysis at 2.05 and 2.69 A resolution, respectively, structure modelling	Escherichia coli	-	695008
in absence and presence of ATP. Upon ATP binding, the central B-domain closes. Residues G165 and G166 play a role in ATP binding	Escherichia coli	-	706634
in complex with inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	Escherichia coli	-	706519
sitting-drop vapor diffusion method, crystallization of mutant enzyme E23R and F363A	Escherichia coli	-	675923
wild-type Escherichia coli biotin carboxylase and mutant E296A in complex with its substrates biotin, bicarbonate, and Mg-ADP, at 2.0 A resolution. Residue Glu296 is the general base that extracts the proton from bicarbonate, and Arg338 is the residue that stabilizes the enolate biotin intermediate in the carboxylation reaction. The B domain of biotin carboxylase is positioned closer to the active site, leading to a 2-A shift in the bound position of the adenine nucleotide and bringing it near the bicarbonate for catalysis. One of the oxygenatoms of bicarbonate is located in the correct position to initiate the nucleophilic attack on ATP to form the carboxyphosphate intermediate. The phosphate group, derived from decomposition of carboxyphosphate, is the general base that extracts the proton on this N1 atom	Escherichia coli	-	704465
x-ray structure	Escherichia coli	-	656018
X-ray structure, native and E288K mutant enzyme, both complexed with ATP	Escherichia coli	-	655978
the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans is crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6 A, b = 116.0 A, c = 115.7 A by hanging-drop vapour-diffusion method. Two biotin carboxylase protomers are contained in the asymmetric unit. Diffraction data are collected at -173�C and the crystal structure is solved by the molecular-replacement method and refined against reflections in the 20.0�2.4 A resolution range	Geobacillus thermodenitrificans	-	671061
crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK	Homo sapiens	O00763	702083
recombinant apoenzyme or enzyme in complex with ATP analogue AMP-PCP, sitting drop vapour diffusion, from 0.1 M HEPES, pH 7.0, 0.2 M MgCl2, 15-20% PEG 3350, and 10% ethylene glycol in the well solution, X-ray diffraction structure determination and analysis at 2.4 A resolution, structure modelling	Pseudomonas aeruginosa	-	695008
crystal structure of the recombinant biotin carboxylase domain alone and in complex with soraphen A, sitting drop vapor diffusion method, crystals belong to space group P2(1), with cell parameters of a = 63.83 A, b = 96.52 A, c = 139.95 A and beta = 96.82 A	Saccharomyces cerevisiae	Q00955	662830
in complex with acetyl-CoA. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent	Staphylococcus aureus	Q99UY9	706790
recombinant enzyme in complex with ATP analogue AMP-PNP, sitting drop vapour diffusion, from 0.2 M KCl, 20% PEG 3350, and 20% ethylene glycol in the well solution, X-ray diffraction structure determination and analysis at 2.10, structure modelling	Staphylococcus aureus	-	695008

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	-	Escherichia coli	-	glycerol protects against thermal inactivation	1422

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
glycerol protects against thermal inactivation	Escherichia coli	-	1422
the truncated biotin carboxylase domain is more stable than the full-length enzyme	Ustilago maydis	-	660969

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
recombinant enzyme	Aquifex aeolicus	-	654115
-	Escherichia coli	-	1420, 1421, 1426, 1428, 654403, 656207
hybrid dimers composed of one subunit having an active site mutation and a second with a wild-type active site	Escherichia coli	-	656018
native and E288K mutant enzyme	Escherichia coli	-	655978
recombinant His-tagged biotinoyl domain from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration	Escherichia coli	-	695042
recombinant His-tagged enzyme from Escherichia coli strain BL21-AI by nickel affinity chromatography and gel filtration	Escherichia coli	-	695008
wild-type and mutant enzymes	Escherichia coli	-	654566, 654575
wild-type and mutant, overexpressed BC	Escherichia coli	-	655535
recombinant biotin carboxylase domain of pyruvate carboxylase	Geobacillus thermodenitrificans	-	651171
recombinant wild-type and mutant His-tagged biotinoyl domains from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration	Homo sapiens	-	695042
partial	Pisum sativum	-	654339
recombinant His-tagged enzyme from Escherichia coli srrain BL21-AI by nickel affinity and anion exchange chromatography, and gel filtration	Pseudomonas aeruginosa	-	695008
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration	Staphylococcus aureus	-	695008

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Acidianus brierleyi	Q877I5	692103
overexpression in Escherichia coli JM109	Aquifex aeolicus	-	654115
-	Arabidopsis thaliana	-	1435
expression in Escherichia coli	Arabidopsis thaliana	-	1434
-	Bacillus subtilis	-	1438
-	Brassica napus	-	1440
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Cenarchaeum symbiosum	A0RY62	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Chlorobium limicola, Chlorobium phaeobacteroides	-	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Chloroflexus aurantiacus	A9W9X0	692103
gene encoding a protein composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein	Corynebacterium glutamicum	-	1437
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Cupriavidus metallidurans, Cytophaga hutchinsonii	-	692103
-	Escherichia coli	-	1429, 1430
accC gene, overexpression in Escherichia coli	Escherichia coli	-	656018
expression in Escherichia coli BL21(DE3)pLysS	Escherichia coli	-	654566
expression of the His-tagged biotinoyl domain in Escherichia coli strain AVB101	Escherichia coli	-	695042
gene accC, expression in Escherichia coli strain BL21-AI as His-tagged enzyme	Escherichia coli	-	695008
overexpression in Escherichia coli JM109	Escherichia coli	-	655535
overexpression system	Escherichia coli	-	656207
expression of biotin carboxylase domain of pyruvate carboxylase in Escherichia coli	Geobacillus thermodenitrificans	-	651171
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Geobacter uraniireducens	A5G5L1	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Halobacterium salinarum	Q9HPP8	692103
expression of wild-type and mutant His-tagged biotinoyl domains in Escherichia coli strain AVB101	Homo sapiens	-	695042
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Hyperthermus butylicus	A2BLY3	692103
-	Jatropha curcas	F2WMV4	716633
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli	Magnaporthe grisea	-	660969
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Maribacter sp. HTCC2170	A4APF1	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Metallosphaera sedula	Q8J2Z4	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Methanococcales, Methanosarcinales	-	692103
accA gene, sequencing, expression in Escherichia coli, forms together with accB a two-gene operon	Myxococcus xanthus	Q9FAF5	651665
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Natronomonas pharaonis	Q3INT5	692103
-	Nicotiana tabacum	-	37620
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Nitrosopumilus maritimus	A9A3E8	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Pelobacter carbinolicus	Q3A2P1	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Pelobacter propionicus	A1ANN6	692103
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli	Phytophthora infestans	-	660969
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Polaromonas sp.	Q12EJ0	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1	A4SVB6	692103
expression in Escherichia coli	Pseudomonas aeruginosa	-	1441
gene accC, expression in Escherichia coli srrain BL21-AI as His-tagged enzyme	Pseudomonas aeruginosa	-	695008
expression of biotin carboxylase domain of acetyl-coenzyme A carboxylase in Escherichia coli	Saccharomyces cerevisiae	Q00955	662830
gene accC, overexpression in Escherichia coli strain BL21(DE3) as His-tagged enzyme	Staphylococcus aureus	-	695008
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Sulfolobus metallicus	O52602	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Sulfolobus solfataricus	Q97V46	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Sulfolobus tokodaii	Q974R7	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Synechococcus sp.	Q54755	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	Trichodesmium erythraeum	Q10YA8	692103
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview	uncultured bacterium	B1GX36	692103
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli	Ustilago maydis	-	660969

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
expression of the accA, accB1, accC and accD genes in Jatropha endosperm varies greatly at different developmental stages. The peak expression of the four genes is observed at about 42 days after fertilization when storage lipids are synthesized at their maximal levels	Jatropha curcas	F2WMV4	716633

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
C230A	Escherichia coli	-	kinetic data, 50fold increased Km for ATP, no effect on the formation of carboxybiotin	654575
E211A	Escherichia coli	-	300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data	654566
E23R	Escherichia coli	-	mutant enzyme is monomeric in solution, mutant shows 3fold loss in catalytic activity, mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is 2.6fold lower than wild-type value	675923
E276Q	Escherichia coli	-	kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP	656008
E288A	Escherichia coli	-	300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data	654566
E288K	Escherichia coli	-	mutant with completely abolished ability to hydrolyze ATP	655978
E288K	Escherichia coli	-	completely inactive mutant, hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 285fold decreased activity, reduced rate of fatty acid synthesis	656018
E288K	Escherichia coli	-	inactive active-site mutant	693839
E296A	Escherichia coli	-	50fold decrease in catalytic efficiency, crystallization data	704465
F363A	Escherichia coli	-	mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is identical to wild-type value	675923
G165V	Escherichia coli	-	site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows increased Km for ATP and 100fold decreased reaction velocity compared to the wild-type enzyme	695008
G165V	Escherichia coli	-	the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold	706634
G165V/G166V	Escherichia coli	-	the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold	706634
G166V	Escherichia coli	-	site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows increased Km for ATP and 100fold decreased reaction velocity compared to the wild-type enzyme	695008
G166V	Escherichia coli	-	the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold	706634
H209A	Escherichia coli	-	kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP	656008
H438P	Escherichia coli	-	decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	706519
I437T	Escherichia coli	-	decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine	706519
K116A	Escherichia coli	-	kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP	656008
K116Q	Escherichia coli	-	kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP	656008
K116Q	Escherichia coli	-	site-directed mutagenesis, the phosphate binding site mutant has the residue of the Staphylococcus aureus enzyme and shows a 50fold increased Km for ATP compared to the wild-type enzyme	695008
K159Q	Escherichia coli	-	kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP	656008
K159Q	Escherichia coli	-	site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows a 90fold higher Km for ATP compared to the wild-type enzyme	695008
K238A	Escherichia coli	-	ATP-binding residue, mutant with much decreased activity, kinetic data	655535
K238Q	Escherichia coli	-	kinetic data, 50fold increased Km for ATP, no formation of carboxybiotin	654575
K238Q	Escherichia coli	-	ATP-binding residue, mutant with much decreased activity, kinetic data	655535
K238Q	Escherichia coli	-	hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 94fold decreased activity, reduced rate of fatty acid synthesis	656018
K238R	Escherichia coli	-	ATP-binding residue, mutant with much decreased activity, kinetic data	655535
M169K	Escherichia coli	-	kinetic data, 5fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate	656207
N290A	Escherichia coli	-	300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data	654566
N290A	Escherichia coli	-	hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 28fold decreased activity, reduced rate of fatty acid synthesis	656018
N290A	Escherichia coli	-	active site mutant, negative cooperativity with respect to bicarbonate	656207
R19E	Escherichia coli	-	mutant enzyme is monomeric in solution, mutant shows 3fold loss in catalytic activity. kcat/Km for ATP-hydrolysis is 2.5fold lower than wild-type value	675923
R292A	Escherichia coli	-	300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data	654566
R292A	Escherichia coli	-	hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 39fold decreased activity, reduced rate of fatty acid synthesis	656018
R292A	Escherichia coli	-	site-directed mutagenesis, the mutant has a Km for ATP similar to the wild-type enzyme	695008
R338A	Escherichia coli	-	250fold decrease in catalytic efficiency	704465
R338Q	Escherichia coli	-	kinetic data, 100fold lower Vmax than wild-type enzyme, negative cooperativity with respect to bicarbonate	656207
R338S	Escherichia coli	-	kinetic data, 140fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate	656207
R366E	Escherichia coli	-	mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP	675923
R401E	Escherichia coli	-	mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP	675923
additional information	Homo sapiens	-	identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive	703970
V927A/I931M/M932N/T933Q	Homo sapiens	-	site-directed mutagenesis, substitution of four amino acids in the vicinity of human MKM motif in analogy to the Escherichia coli biotinylation site	695042
additional information	Myxococcus xanthus	Q9FAF5	accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity	651665

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
medicine	Escherichia coli	-	the three biotin carboxylase mutants M169K, R338Q and R338S are used for study in order to mimic the disease-causing mutations M204K and R374Q of propionyl-CoA carboxylase and R385S of 3-methylcrotonyl-CoA carboxylase, which are mutations found in propionic acidemia or methylcrotonylglycinuria patients	656207
medicine	Homo sapiens	-	identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive	703970

DISEASE	TITLE OF PUBLICATION	LINK TO PUBMED
Infection	Evaluation of pharmacokinetic/pharmacodynamic relationships of PD-0162819, a biotin carboxylase inhibitor representing a new class of antibacterial compounds, using in vitro infection models.	PubMed
Propionic Acidemia	Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase.	PubMed
Tuberculosis	AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis.	PubMed

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
1420	Tipton, P.A.; Cleland, W.W.	Catalytic mechanism of biotin carboxylase: steady-state kinetic investigation	Biochemistry	27	4317-4325	1988	Escherichia coli	PubMed
1421	Guchhait, R.B.; Polakis, S.E.; Lane, M.D.	Biotin carboxylase component of acetyl-CoA carboxylase from Escherichia coli	Methods Enzymol.	35B	25-31	1975	Escherichia coli	PubMed
1422	Climent, I.; Rubio, V.	ATPase activity of biotin carboxylase provides evidence for initial activation of HCO3- by ATP in the carboxylation of biotin	Arch. Biochem. Biophys.	251	465-470	1986	Escherichia coli	PubMed
1423	Polakis, S.E.; Guchhait, R.B.; Lane, M.D.	On the possible involvement of a carbonyl phosphate intermediate in the adenosine triphosphate-dependent carboxylation of biotin	J. Biol. Chem.	247	1335-1337	1972	Escherichia coli	PubMed
1424	Polakis, S.E.; Guchhait, R.B.; Zwergel, E.E.; Lane, M.D.	Acetyl coenzyme A carboxylase system of Escherichia coli. Studies on the mechanism of the biotin carboxylase- and carboxyltransferase-catalyzed reactions	J. Biol. Chem.	249	6657-6667	1974	Escherichia coli	PubMed
1425	Guchhait, R.B.; Polakis, S.E.; Hollis, D.; Fenselau, C.; Lane, M.D.	Acetyl coenzyme A carboxylase system of Escherichia coli. Site of carboxylation of biotin and enzymatic reactivity of 1'-N-(ureido)-carboxybiotin derivatives	J. Biol. Chem.	24 9	6646-6656	1974	Escherichia coli	PubMed
1426	Guchhait, R.B.; Polakis, S.E.; Dimroth, P.; Stoll, E.; Moss, J.; Lane, M.D.	Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components	J. Biol. Chem.	249	6633-6645	1974	Escherichia coli	PubMed
1427	Dimroth, P.; Guchhait, R.B.; Lane, M.D.	Crystallization of biotin carboxylase, a component enzyme of the acetyl-CoA carboxylase system from Escherichia coli	Hoppe-Seyler's Z. Physiol. Chem.	352	351-354	1971	Escherichia coli	PubMed
1428	Dimroth, P.; Guchhait, R.B.; Stoll, E.; Lane, M.D.	Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase	Proc. Natl. Acad. Sci. USA	67	1353-1360	1970	Escherichia coli	PubMed
1429	Kondo, H.; Shiratsuchi, K.; Yoshimoto, T.; Masuda, T.; Kitazono, A.; Tsuru, D.; Anai, M.; Sekiguchi, M.; Tanabe, T.	Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit	Proc. Natl. Acad. Sci. USA	88	9730-9733	1991	Escherichia coli	PubMed
1430	Li, S.J.; Cronan, J.E.	The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase	J. Biol. Chem.	267	855-863	1992	Escherichia coli	PubMed
1431	Waldrop, G.; Holden, H.M.; Rayment, I.	Preliminary X-ray crystallographic analysis of biotin carboxylase isolated from Escherichia coli	J. Mol. Biol.	235	367-369	1994	Escherichia coli	PubMed
1432	Norman, E.; de Smet, K.A.L.; Stoker, N.G.; Ratledge, C.; Wheeler, P.R.; Dale, J.W.	Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis	J. Bacteriol.	176	2525-2531	1994	Mycobacterium leprae, Mycobacterium tuberculosis	PubMed
1433	Waldrop, G.L.; Rayment, I.; Holden, H.M.	Three-dimensional structure of the biotin carboxylase subunit of the acetyl-CoA carboxylase	Biochemistry	33	10249-10256	1994	Escherichia coli	PubMed
1434	Sun, J.; Ke, J.; Johnson, J.L.; Nikolau, B.J.; Wurtele, E.S.	Biochemical and molecular biological characterization of CAC2, the Arabidopsis thaliana gene coding for the biotin carboxylase subunit of the plastidic acetyl-coenzyme A carboxylase	Plant Physiol.	115	1371-1383	1997	Arabidopsis thaliana	PubMed
1435	Bao, X.; Shorrosh, B.S.; Ohlrogge, J.B.	Isolation and characterization of an Arabidopsis biotin carboxylase gene and its promoter	Plant Mol. Biol.	35	539-550	1997	Arabidopsis thaliana	PubMed
1436	Shintani, D.; Roesler, K.; Shorrosh, B.; Savage, L.; Ohlrogge, J.	Antisense expression and overexpression of biotin carboxylase in tobacco leaves	Plant Physiol.	114	881-886	1997	Nicotiana tabacum	PubMed
1437	Jager, W.; Peters-Wendisch, P.G.; Kalinowski, J.; Puhler, A.	A Corynebacterium glutamicum gene encoding a two-domain protein similar to biotin carboxylases and biotin-carboxyl-carrier proteins	Arch. Microbiol.	166	76-82	1996	Corynebacterium glutamicum	PubMed
1438	Marini, P.; Li, S.J.; Gardiol, D.; Cronan, J.E.; de Mendoza, D.	The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis	J. Bacteriol.	177	7003-7006	1995	Bacillus subtilis	PubMed
1440	Elborough, K.M.; Swinhoe, R.; Winz, R.; Kroon, J.T.; Farnsworth, L.; Fawcett, T.; Martinez-Rivas, J.M.; Slabas, A.R.	Isolation of cDNAs from Brassica napus encoding the biotin-binding and transcarboxylase: assignment of the domain structure ina full-length Arabidopsis thaliana genomuic clone	Biochem. J.	301	599-605	1994	Brassica napus	PubMed
1441	Best, E.A.; Knauf, V.C.	Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase	J. Bacteriol.	175	6881-6889	1993	Pseudomonas aeruginosa	PubMed
37620	Shorrosh, B.S.; Roesler, K.R.; Shintani, D.; van de Loo, F.J.; Ohlrogge, J.B.	Structural analysis, plastid localization, and expression of the biotin carboxylase subunit of acetyl-coenzyme A carboxylase from tobacco	Plant Physiol.	108	805-812	1995	Medicago sativa, Nicotiana tabacum, Pisum sativum, Ricinus communis	PubMed
651171	Sueda, S.; Islam, M.N.; Kondo, H.	Protein engineering of pyruvate carboxylase	Eur. J. Biochem.	271	1391-1400	2004	Geobacillus thermodenitrificans	PubMed
651665	Kimura, Y.; Miyake, R.; Tokumasu, Y.; Sato, M.	Molecular cloning and characterization of two genes for the biotin carboxylase and carboxyltransferase subunits of acetyl coenzyme A carboxylase in Myxococcus xanthus	J. Bacteriol.	182	5462-5469	2000	Myxococcus xanthus	PubMed
654115	Kondo, S.; Nakajima, Y.; Sugio, S.; Yong-Biao, J.; Sueda, S.; Kondo, H.	Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution	Acta Crystallogr. Sect. D	60	486-492	2004	Aquifex aeolicus	PubMed
654339	Thelen, J.J.; Ohlrogge, J.B.	The multisubunit acetyl-CoA carboxylase is strongly associated with the chloroplast envelope through non-ionic interactions to the carboxyltransferase subunits	Arch. Biochem. Biophys.	400	245-257	2002	Pisum sativum	PubMed
654403	Blanchard, C.Z.; Amspacher, D.; Strongin, R.; Waldrop, G.L.	Inhibition of biotin carboxylase by a reaction intermediate analog: implications for the kinetic mechanism	Biochem. Biophys. Res. Commun.	266	466-471	1999	Escherichia coli	PubMed
654566	Blanchard, C.Z.; Lee, Y.M.; Frantom, P.A.; Waldrop, G.L.	Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin	Biochemistry	38	3393-3400	1999	Escherichia coli	PubMed
654575	Levert, K.L.; Lloyd, R.B.; Waldrop, G.L.	Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?	Biochemistry	39	4122-4128	2000	Escherichia coli	PubMed
655535	Kazuta, Y.; Tokunaga, E.; Aramaki, E.; Kondo, H.	Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue	FEBS Lett.	427	377-380	1998	Escherichia coli	PubMed
655973	Blanchard, C.Z.; Chapman-Smith, A.; Wallace, J.C.; Waldrop, G.L.	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	PubMed
655978	Thoden, J.B.; Blanchard, C.Z.; Holden, H.M.; Waldrop, G.L.	Movement of the biotin carboxylase B-domain as a result of ATP binding	J. Biol. Chem.	275	16183-16190	2000	Escherichia coli	PubMed
656008	Sloane, V.; Blanchard, C.Z.; Guillot, F.; Waldrop, G.L.	Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis	J. Biol. Chem.	276	24991-24996	2001	Escherichia coli	PubMed
656018	Janiyani, K.; Bordelon, T.; Waldrop, G.L.; Cronan, J.E., Jr.	Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer	J. Biol. Chem.	276	29864-29870	2001	Escherichia coli	PubMed
656207	Sloane, V.; Waldrop, G.L.	Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase	J. Biol. Chem.	279	15772-15778	2004	Escherichia coli	PubMed
660969	Weatherly, S.C.; Volrath, S.L.; Elich, T.D.	Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain	Biochem. J.	380	105-110	2004	Magnaporthe grisea, Phytophthora infestans, Ustilago maydis	PubMed
662830	Shen, Y.; Volrath, S.L.; Weatherly, S.C.; Elich, T.D.; Tong, L.	A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product	Mol. Cell	16	881-891	2004	Saccharomyces cerevisiae	PubMed
671061	Kondo, S.; Nakajima, Y.; Sugio, S.; Sueda, S.; Islam, M.N.; Kondo, H.	Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans	Acta Crystallogr. Sect. D	63	885-890	2007	Geobacillus thermodenitrificans	PubMed
675698	de Queiroz, M.S.; Waldrop, G.L.	Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity	J. Theor. Biol.	246	167-175	2007	Escherichia coli	PubMed
675923	Shen, Y.; Chou, C.Y.; Chang, G.G.; Tong, L.	Is dimerization required for the catalytic activity of bacterial biotin carboxylase?	Mol. Cell	22	807-818	2006	Escherichia coli	PubMed
677847	Burton, N.P.; Williams, T.D.; Norris, P.R.	Carboxylase genes of Sulfolobus metallicus	Arch. Microbiol.	172	349-353	1999	Sulfolobus metallicus	PubMed
692103	Auguet, J.C.; Borrego, C.M.; Baneras, L.; Casamayor, E.O.	Fingerprinting the genetic diversity of the biotin carboxylase gene (accC) in aquatic ecosystems as a potential marker for studies of carbon dioxide assimilation in the dark	Environ. Microbiol.	10	2527-2536	2008	Acidianus brierleyi, Cenarchaeum symbiosum, Chlorobium limicola, Chlorobium phaeobacteroides, Chloroflexus aurantiacus, Cupriavidus metallidurans, Cytophaga hutchinsonii, Geobacter uraniireducens, Halobacterium salinarum, Hyperthermus butylicus, Maribacter sp. HTCC2170, Metallosphaera sedula, Methanococcales, Methanosarcinales, Natronomonas pharaonis, Nitrosopumilus maritimus, Pelobacter carbinolicus, Pelobacter propionicus, Polaromonas sp., Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1, Sulfolobus metallicus, Sulfolobus solfataricus, Sulfolobus tokodaii, Synechococcus sp., Trichodesmium erythraeum, uncultured bacterium	PubMed
693839	Nilsson Lill, S.O.; Gao, J.; Waldrop, G.L.	Molecular dynamics simulations of biotin carboxylase	J. Phys. Chem. B	112	3149-3156	2008	Escherichia coli	PubMed
695008	Mochalkin, I.; Miller, J.R.; Evdokimov, A.; Lightle, S.; Yan, C.; Stover, C.K.; Waldrop, G.L.	Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase	Protein Sci.	17	1706-1718	2008	Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus	PubMed
695042	Lee, C.K.; Cheong, H.K.; Ryu, K.S.; Lee, J.I.; Lee, W.; Jeon, Y.H.; Cheong, C.	Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism	Proteins	72	613-624	2008	Escherichia coli, Homo sapiens	PubMed
701439	Mochalkin, I.; Miller, J.R.; Narasimhan, L.; Thanabal, V.; Erdman, P.; Cox, P.B.; Prasad, J.V.; Lightle, S.; Huband, M.D.; Stover, C.K.	Discovery of antibacterial biotin carboxylase inhibitors by virtual screening and fragment-based approaches	ACS Chem. Biol.	4	473-483	2009	Escherichia coli, Haemophilus influenzae, Moraxella catarrhalis	PubMed
702083	Cho, Y.S.; Lee, J.I.; Shin, D.; Kim, H.T.; Jung, H.Y.; Lee, T.G.; Kang, L.W.; Ahn, Y.J.; Cho, H.S.; Heo, Y.S.	Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK	Biochem. Biophys. Res. Commun.	391	187-192	2010	Homo sapiens	PubMed
703970	Monnot, S.; Serre, V.; Chadefaux-Vekemans, B.; Aupetit, J.; Romano, S.; De Lonlay, P.; Rival, J.M.; Munnich, A.; Steffann, J.; Bonnefont, J.P.	Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency	Hum. Mutat.	30	734-740	2009	Homo sapiens	PubMed
704465	Chou, C.Y.; Yu, L.P.; Tong, L.	Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism	J. Biol. Chem.	284	11690-11697	2009	Escherichia coli	PubMed
706519	Miller, J.R.; Dunham, S.; Mochalkin, I.; Banotai, C.; Bowman, M.; Buist, S.; Dunkle, B.; Hanna, D.; Harwood, H.J.; Huband, M.D.; Karnovsky, A.; Kuhn, M.; Limberakis, C.; Liu, J.Y.; Mehrens, S.; Mueller, W.T.; Narasimhan, L.; Ogden, A.; Ohren, J.; Prasad, J.V.; Shelly, J.A.; Skerlos, L.; Sulavik, M.; Thomas,	A class of selective antibacterials derived from a protein kinase inhibitor pharmacophore	Proc. Natl. Acad. Sci. USA	106	1737-1742	2009	Escherichia coli	PubMed
706634	Bordelon, T.; Nilsson Lill, S.; Waldrop, G.	The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase	Proteins Struct. Funct. Bioinform.	74	808-819	2009	Escherichia coli	PubMed
706790	Yu, L.P.; Xiang, S.; Lasso, G.; Gil, D.; Valle, M.; Tong, L.	A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A	Structure	17	823-832	2009	Staphylococcus aureus	PubMed
716633	Gu, K.; Chiam, H.; Tian, D.; Yin, Z.	Molecular cloning and expression of heteromeric ACCase subunit genes from Jatropha curcas	Plant Sci.	180	642-649	2011	Jatropha curcas	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 6.3.4.14)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

All organisms
Acidianus brierleyi
Aquifex aeolicus
Arabidopsis thaliana
Bacillus subtilis
Brassica napus
Cenarchaeum symbiosum
Chlorobium limicola
Chlorobium phaeobacteroides
Chloroflexus aurantiacus
Corynebacterium glutamicum
Cupriavidus metallidurans
Cytophaga hutchinsonii
Escherichia coli
Escherichia coli JM109
Geobacillus thermodenitrificans
Geobacter uraniireducens
Haemophilus influenzae
Halobacterium salinarum
Homo sapiens
Hyperthermus butylicus
Jatropha curcas
Magnaporthe grisea
Maribacter sp. HTCC2170
Medicago sativa
Metallosphaera sedula
Methanococcales
Methanosarcinales
Moraxella catarrhalis
Mycobacterium leprae
Mycobacterium tuberculosis
Myxococcus xanthus
Myxococcus xanthus IFO13542/ATCC25232
Natronomonas pharaonis
Nicotiana tabacum
Nitrosopumilus maritimus
Pelobacter carbinolicus
Pelobacter propionicus
Phytophthora infestans
Pisum sativum
Polaromonas sp.
Polaromonas sp. JS666
Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1
Pseudomonas aeruginosa
Ricinus communis
Saccharomyces cerevisiae
Staphylococcus aureus
Staphylococcus aureus Mu50
Sulfolobus metallicus
Sulfolobus solfataricus
Sulfolobus tokodaii
Synechococcus sp.
Trichodesmium erythraeum
uncultured bacterium
Ustilago maydis