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Information on EC 6.2.1.18 - citrate-CoA ligase for references in articles please use BRENDA:EC6.2.1.18Word Map on EC 6.2.1.18
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA
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Acid-thiol ligation
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reductive TCA cycle II
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Carbon fixation pathways in prokaryotes
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Microbial metabolism in diverse environments
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citrate:CoA ligase (ADP-forming)
The enzyme is a component of EC 2.3.3.8 ATP citrate synthase.
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CCS
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citryl-CoA synthetase
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citryl-CoA synthetase
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citryl-CoA synthetase
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large subunit, gene ccsA
UniProt
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small subunit, gene ccsB
UniProt
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evolution
phylogenetic analysis of the distribution of the alternative CO2 fixation pathway catalyzed by two separate enzymes, citryl-CoA synthetase and citryl-CoA lyase in Aquificaceae populations, phylogenetic analysis, overview; phylogenetic analysis of the distribution of the alternative CO2 fixation pathway catalyzed by two separate enzymes, citryl-CoA synthetase and citryl-CoA lyase in Aquificaceae populations, phylogenetic analysis, overview
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ATP + citrate + CoA
ADP + phosphate + (3S)-citryl-CoA
ATP + citrate + CoA
ADP + phosphate + citryl-CoA
ATP + citrate + CoA
ADP + phosphate + (3S)-citryl-CoA
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ATP + citrate + CoA
ADP + phosphate + (3S)-citryl-CoA
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ATP + citrate + CoA
ADP + phosphate + citryl-CoA
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ATP + citrate + CoA
ADP + phosphate + citryl-CoA
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ATP + citrate + CoA
ADP + phosphate + citryl-CoA
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ATP + citrate + CoA
ADP + phosphate + (3S)-citryl-CoA
Q75VW6, Q75VW8
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ATP
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0.071
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in 100 mM HEPES/NaOH, pH 8.3, 5 mM dithioerythritol, 5 mM MgCl2, 3 mM ATP, 0.5 mM CoA, 0.4 mM NADH, and 3 mM D-citrate
0.082
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in 100 mM HEPES/NaOH, pH 8.3, 5 mM dithioerythritol, 5 mM MgCl2, 3 mM ATP, 0.5 mM CoA, 0.4 mM NADH, and 3 mM D-citrate
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additional information
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the enzyme is a component of EC 4.1.3.8
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gene ccsA, DNA and amino acid sequence analysis and phylogenetic analysis; gene ccsA, DNA and amino acid sequence analysis and phylogenetic analysis
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Q0PQT2_9GAMM
141
15540
TrEMBL
Q75VW8_HYDTH
429
47580
TrEMBL
Q75VW6_HYDTH
344
37013
TrEMBL
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Lill, U.; Schreil, A.; Eggerer, H.
Isolation of enzymically active fragments formed by limited proteolysis
Eur. J. Biochem.
125
645-650
1982
Rattus norvegicus
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Hugler, M.; Huber, H.; Molyneaux, S.J.; Vetriani, C.; Sievert, S.M.
Autotrophic CO2 fixation via the reductive tricarboxylic acid cycle in different lineages within the phylum Aquificae: Evidence for two ways of citrate cleavage
Environ. Microbiol.
9
81-92
2007
Aquifex aeolicus, Hydrogenobacter hydrogenophilus, Thermocrinis ruber
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Takacs-Vesbach, C.; Inskeep, W.P.; Jay, Z.J.; Herrgard, M.J.; Rusch, D.B.; Tringe, S.G.; Kozubal, M.A.; Hamamura, N.; Macur, R.E.; Fouke, B.W.; Reysenbach, A.L.; McDermott, T.R.; Jennings, R.d.; Hengartner, N.W.; Xie, G.
Metagenome sequence analysis of filamentous microbial communities obtained from geochemically distinct geothermal channels reveals specialization of three aquificales lineages
Front. Microbiol.
4
84
2013
Hydrogenobacter thermophilus (Q75VW6), Hydrogenobacter thermophilus (Q75VW8)
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