Identification
Name:Acetyl-coenzyme A synthetase
Synonyms:
  • Acetate--CoA ligase
  • Acyl-activating enzyme
Gene Name:acs
Enzyme Class:
Biological Properties
General Function:Involved in acetate-CoA ligase activity
Specific Function:Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
Thumb+Thumb+ThumbPropionyl-CoA+Thumb+Pyrophosphate+Thumb
Thumb+Thumb+ThumbPyrophosphate+Thumb+Thumb
EcoCyc Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00042Acetic acidMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB21433Adenosine tetraphosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00237Propionic acidMetaboCard
ECMDB01275Propionyl-CoAMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
acetate-CoA ligase activity
adenyl nucleotide binding
adenyl ribonucleotide binding
AMP binding
binding
catalytic activity
CoA-ligase activity
ligase activity
ligase activity, forming carbon-sulfur bonds
nucleoside binding
purine nucleoside binding
Process
metabolic process
Gene Properties
Blattner:b4069
Gene OrientationCounterclockwise
Centisome Percentage:92.32
Left Sequence End4283436
Right Sequence End4285394
Gene Sequence:
>1959 bp
ATGAGCCAAATTCACAAACACACCATTCCTGCCAACATCGCAGACCGTTGCCTGATAAAC
CCTCAGCAGTACGAGGCGATGTATCAACAATCTATTAACGTACCTGATACCTTCTGGGGC
GAACAGGGAAAAATTCTTGACTGGATCAAACCTTACCAGAAGGTGAAAAACACCTCCTTT
GCCCCCGGTAATGTGTCCATTAAATGGTACGAGGACGGCACGCTGAATCTGGCGGCAAAC
TGCCTTGACCGCCATCTGCAAGAAAACGGCGATCGTACCGCCATCATCTGGGAAGGCGAC
GACGCCAGCCAGAGCAAACATATCAGCTATAAAGAGCTGCACCGCGACGTCTGCCGCTTC
GCCAATACCCTGCTCGAGCTGGGCATTAAAAAAGGTGATGTGGTGGCGATTTATATGCCG
ATGGTGCCGGAAGCCGCGGTTGCGATGCTGGCCTGCGCCCGCATTGGCGCGGTGCATTCG
GTGATTTTCGGCGGCTTCTCGCCGGAAGCCGTTGCCGGGCGCATTATTGATTCCAACTCA
CGACTGGTGATCACTTCCGACGAAGGTGTGCGTGCCGGGCGCAGTATTCCGCTGAAGAAA
AACGTTGATGACGCGCTGAAAAACCCGAACGTCACCAGCGTAGAGCATGTGGTGGTACTG
AAGCGTACTGGCGGGAAAATTGACTGGCAGGAAGGGCGCGACCTGTGGTGGCACGACCTG
GTTGAGCAAGCGAGCGATCAGCACCAGGCGGAAGAGATGAACGCCGAAGATCCGCTGTTT
ATTCTCTACACCTCCGGTTCTACCGGTAAGCCAAAAGGTGTGCTGCATACTACCGGCGGT
TATCTGGTGTACGCGGCGCTGACCTTTAAATATGTCTTTGATTATCATCCGGGTGATATC
TACTGGTGCACCGCCGATGTGGGCTGGGTGACCGGACACAGTTACTTGCTGTACGGCCCG
CTGGCCTGCGGTGCGACCACGCTGATGTTTGAAGGCGTACCCAACTGGCCGACGCCTGCC
CGTATGGCGCAGGTGGTGGACAAGCATCAGGTCAATATTCTCTATACCGCACCCACGGCG
ATCCGCGCGCTGATGGCGGAAGGCGATAAAGCGATCGAAGGCACCGACCGTTCGTCGCTG
CGCATTCTCGGTTCCGTGGGCGAGCCAATTAACCCGGAAGCGTGGGAGTGGTACTGGAAA
AAAATCGGCAACGAGAAATGTCCGGTGGTCGATACCTGGTGGCAGACCGAAACCGGCGGT
TTCATGATCACCCCGCTGCCTGGCGCTACCGAGCTGAAAGCCGGTTCGGCAACACGTCCG
TTCTTCGGCGTGCAACCGGCGCTGGTCGATAACGAAGGTAACCCGCTGGAGGGGGCCACC
GAAGGTAGCCTGGTAATCACCGACTCCTGGCCGGGTCAGGCGCGTACGCTGTTTGGCGAT
CACGAACGTTTTGAACAGACCTACTTCTCCACCTTCAAAAATATGTATTTCAGCGGCGAC
GGCGCGCGTCGCGATGAAGATGGCTATTACTGGATAACCGGGCGTGTGGACGACGTGCTG
AACGTCTCCGGTCACCGTCTGGGGACGGCAGAGATTGAGTCGGCGCTGGTGGCGCATCCG
AAGATTGCCGAAGCCGCCGTAGTAGGTATTCCGCACAATATTAAAGGTCAGGCGATCTAC
GCCTACGTCACGCTTAATCACGGGGAGGAACCGTCACCAGAACTGTACGCAGAAGTCCGC
AACTGGGTGCGTAAAGAGATTGGCCCGCTGGCGACGCCAGACGTGCTGCACTGGACCGAC
TCCCTGCCTAAAACCCGCTCCGGCAAAATTATGCGCCGTATTCTGCGCAAAATTGCGGCG
GGCGATACCAGCAACCTGGGCGATACCTCGACGCTTGCCGATCCTGGCGTAGTCGAGAAG
CTGCTTGAAGAGAAGCAGGCTATCGCGATGCCATCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:652
Protein Molecular Weight:72093
Protein Theoretical pI:6
PDB File:1PG4
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetyl-coenzyme A synthetase
MSQIHKHTIPANIADRCLINPQQYEAMYQQSINVPDTFWGEQGKILDWIKPYQKVKNTSF
APGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDASQSKHISYKELHRDVCRF
ANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNS
RLVITSDEGVRAGRSIPLKKNVDDALKNPNVTSVEHVVVLKRTGGKIDWQEGRDLWWHDL
VEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDI
YWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTA
IRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGG
FMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGD
HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP
KIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTD
SLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIAMPS
References
External Links:
ResourceLink
Uniprot ID:P27550
Uniprot Name:ACSA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676821
PDB ID:1PG4
Ecogene ID:EG11448
Ecocyc:EG11448
ColiBase:b4069
Kegg Gene:b4069
EchoBASE ID:EB1417
CCDB:ACSA_ECOLI
BacMap:16131895
General Reference:
  • Barak, R., Abouhamad, W. N., Eisenbach, M. (1998). "Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli." J Bacteriol 180:985-988. Pubmed: 9473056
  • Barak, R., Eisenbach, M. (2001). "Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis." Mol Microbiol 40:731-743. Pubmed: 11359578
  • Barak, R., Welch, M., Yanovsky, A., Oosawa, K., Eisenbach, M. (1992). "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch." Biochemistry 31:10099-10107. Pubmed: 1390767
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Brown, T. D., Jones-Mortimer, M. C., Kornberg, H. L. (1977). "The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli." J Gen Microbiol 102:327-336. Pubmed: 21941
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kumari, S., Beatty, C. M., Browning, D. F., Busby, S. J., Simel, E. J., Hovel-Miner, G., Wolfe, A. J. (2000). "Regulation of acetyl coenzyme A synthetase in Escherichia coli." J Bacteriol 182:4173-4179. Pubmed: 10894724
  • Kumari, S., Tishel, R., Eisenbach, M., Wolfe, A. J. (1995). "Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli." J Bacteriol 177:2878-2886. Pubmed: 7751300
  • Wu, G., Williams, H. D., Zamanian, M., Gibson, F., Poole, R. K. (1992). "Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG. Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases." J Gen Microbiol 138:2101-2112. Pubmed: 1479344