Acetyl-coenzyme A synthetase

Details

Name
Acetyl-coenzyme A synthetase
Synonyms
  • 6.2.1.1
  • AcCoA synthetase
  • Acetate--CoA ligase
  • Acyl-activating enzyme
Gene Name
acs
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0011376|Acetyl-coenzyme A synthetase
MSQTHKHAIPANIADRCLINPEQYETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTSF
APGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDTSQSKHISYRELHRDVCRF
ANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSS
RLVITADEGVRAGRSIPLKKNVDDALKNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDL
IEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDI
YWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTA
IRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVVDTWWQTETGG
FMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGD
HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP
KIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTD
SLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIAMPS
Number of residues
652
Molecular Weight
72152.085
Theoretical pI
5.71
GO Classification
Functions
acetate-CoA ligase activity / AMP binding / ATP binding / metal ion binding
Processes
acetyl-CoA biosynthetic process from acetate / chemotaxis
General Function
Metal ion binding
Specific Function
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011377|Acetyl-coenzyme A synthetase (acs)
ATGAGCCAAACACATAAACACGCCATTCCCGCCAACATTGCGGATCGTTGCCTGATAAAT
CCAGAGCAGTATGAGACTAAATATAAACAGTCTATTAACGACCCCGATACGTTTTGGGGC
GAACAGGGAAAAATTCTCGATTGGATCACGCCGTACCAAAAAGTGAAAAACACCTCCTTT
GCGCCAGGCAATGTGTCGATTAAATGGTACGAGGACGGCACGCTGAATCTGGCGGCGAAC
TGTCTTGACCGCCATTTGCAGGAAAATGGCGATCGCACCGCCATTATCTGGGAAGGCGAT
GACACGTCGCAGAGTAAACATATCTCTTATCGCGAACTGCATCGCGATGTCTGCCGTTTC
GCGAATACGCTGCTGGATCTGGGCATTAAAAAAGGCGATGTGGTAGCGATTTATATGCCG
ATGGTGCCGGAAGCGGCGGTGGCAATGTTGGCCTGCGCCCGCATCGGTGCGGTGCATTCG
GTGATCTTCGGGGGCTTCTCGCCGGAAGCCGTCGCCGGACGCATTATCGACTCCAGCTCG
CGGCTGGTGATCACCGCTGACGAAGGTGTACGTGCCGGACGCAGTATCCCGCTGAAAAAG
AATGTCGATGACGCGCTGAAAAACCCGAATGTCACTAGCGTTGAGCATGTGATCGTCCTG
AAGCGCACCGGCAGCGACATTGACTGGCAAGAAGGCCGCGACCTGTGGTGGCGCGATTTG
ATTGAAAAAGCCAGCCCTGAGCACCAGCCTGAAGCGATGAATGCCGAAGATCCGCTGTTT
ATCCTTTATACCTCCGGCTCCACCGGCAAGCCGAAAGGCGTGCTGCACACCACCGGCGGC
TATCTGGTCTACGCCGCGACCACCTTTAAGTATGTCTTTGATTATCACCCTGGCGATATT
TACTGGTGTACCGCCGATGTGGGTTGGGTGACGGGGCACAGCTATCTGTTGTATGGCCCG
CTGGCCTGCGGCGCGACCACCTTAATGTTTGAAGGCGTGCCGAATTGGCCAACGCCCGCT
CGCATGTGCCAGGTGGTCGACAAACACCAGGTCAACATTCTCTATACCGCCCCGACGGCC
ATCCGCGCGCTGATGGCGGAAGGCGATAAAGCCATTGAAGGCACCGACCGTTCTTCACTG
CGCATTCTGGGTTCCGTCGGCGAGCCGATCAATCCCGAAGCGTGGGAATGGTACTGGAAG
AAGATCGGCAAGGAAAAATGTCCGGTCGTCGACACCTGGTGGCAGACTGAAACAGGCGGT
TTTATGATCACGCCGCTACCAGGCGCTATCGAACTGAAAGCCGGTTCCGCCACCCGTCCT
TTCTTTGGCGTACAGCCTGCGCTGGTGGATAACGAAGGCCATCCGCAAGAAGGCGCGACG
GAAGGCAATCTGGTCATCACCGATTCCTGGCCGGGCCAGGCGCGCACTCTGTTCGGCGAT
CATGAACGTTTTGAGCAGACCTATTTCTCTACCTTTAAGAATATGTATTTCAGCGGCGAC
GGCGCGCGTCGCGATGAGGACGGCTATTACTGGATCACCGGTCGCGTGGACGACGTGTTA
AACGTCTCCGGCCACCGTCTGGGTACGGCGGAAATCGAGTCAGCGCTGGTGGCGCATCCG
AAGATCGCCGAAGCGGCGGTGGTGGGTATTCCACACGCTATCAAAGGCCAGGCGATTTAC
GCTTATGTGACGCTCAACCACGGCGAGGAGCCGTCGCCAGAACTGTACGCGGAGGTGCGC
AACTGGGTACGTAAAGAGATTGGCCCACTGGCGACGCCGGACGTGCTGCACTGGACCGAC
TCACTGCCAAAAACCCGTTCCGGCAAAATTATGCGCCGCATTTTGCGCAAAATCGCGGCG
GGCGATACCAGCAATCTGGGCGATACCTCGACTCTCGCCGATCCTGGCGTGGTGGAGAAA
CTGCTCGAAGAGAAGCAGGCCATCGCGATGCCGTCATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ8ZKF6
UniProtKB Entry NameACSA_SALTY
GenBank Protein ID16422835
GenBank Gene IDAE008900
General References
  1. McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, Porwollik S, Ali J, Dante M, Du F, Hou S, Layman D, Leonard S, Nguyen C, Scott K, Holmes A, Grewal N, Mulvaney E, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
  2. Starai VJ, Celic I, Cole RN, Boeke JD, Escalante-Semerena JC: Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science. 2002 Dec 20;298(5602):2390-2. [Article]
  3. Starai VJ, Escalante-Semerena JC: Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica. J Mol Biol. 2004 Jul 23;340(5):1005-12. [Article]
  4. Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC: The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A. Biochemistry. 2003 Mar 18;42(10):2866-73. [Article]
  5. Reger AS, Carney JM, Gulick AM: Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase. Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails
DB03230Adenosine-5'-PropylphosphateexperimentalunknownDetails