Sequence of ACSA_ECOLI
EC Number:6.2.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
Other sequences found for EC No. 6.2.1.1
General information:
Sequence
0 MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINVPDTFWG EQGKILDWIK PYQKVKNTSF
60 APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY KELHRDVCRF
120 ANTLLELGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNS
180 RLVITSDEGV RAGRSIPLKK NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL
240 VEQASDQHQA EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI
300 YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ VNILYTAPTA
360 IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGNEKCPVV DTWWQTETGG
420 FMITPLPGAT ELKAGSATRP FFGVQPALVD NEGNPLEGAT EGSLVITDSW PGQARTLFGD
480 HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP
540 KIAEAAVVGI PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
600 SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
511330
Blattner F.R.,Burland V.D.,Plunkett G. III,Sofia H.J.,Daniels D.L.
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
1993
511331
Blattner F.R.,Plunkett G. III,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.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
511332
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
511333
Wu G.,Williams H.D.,Zamanian M.,Gibson F.,Poole R.K.
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
1992
511334
Brown T.D.,Jones-Mortimer M.C.,Kornberg H.L.
The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli.
J. Gen. Microbiol.
102
327-336
1977
511335
Kumari S.,Tishel R.,Eisenbach M.,Wolfe A.J.
Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli.
J. Bacteriol.
177
2878-2886
1995
511336
Kumari S.,Beatty C.M.,Browning D.F.,Busby S.J.,Simel E.J.,Hovel-Miner G.,Wolfe A.J.
Regulation of acetyl coenzyme A synthetase in Escherichia coli.
J. Bacteriol.
182
4173-4179
2000
511337
Barak R.,Welch M.,Yanovsky A.,Oosawa K.,Eisenbach M.
Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch.
Biochemistry
31
10099-10107
1992
511338
Barak R.,Abouhamad W.N.,Eisenbach M.
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
1998
511339
Barak R.,Eisenbach M.
Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis.
Mol. Microbiol.
40
731-743
2001
511340
Zhao K.,Chai X.,Marmorstein R.
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli.
J. Mol. Biol.
337
731-741
2004
511341
Barak R.,Prasad K.,Shainskaya A.,Wolfe A.J.,Eisenbach M.
Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli.
J. Mol. Biol.
342
383-401
2004
511342
Li R.,Gu J.,Chen Y.Y.,Xiao C.L.,Wang L.W.,Zhang Z.P.,Bi L.J.,Wei H.P.,Wang X.D.,Deng J.Y.,Zhang X.E.
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
Mol. Microbiol.
76
1162-1174
2010
