Reviewed, UniProtKB/Swiss-Prot P27550 (ACSA_ECOLI)

Names and origin

Protein names

Recommended name:
    Acetyl-coenzyme A synthetase
    EC=6.2.1.1
Alternative name(s):
    Acetate--CoA ligase
    Acyl-activating enzyme

Gene names

Name:	acs
Synonyms:	yfaC
Ordered Locus Names:	b4069, JW4030

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	652 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.5
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123
Induction	By CRP and FNR, in response to rising cAMP levels, falling oxygen partial pressure and changes in carbon flux. May also be induced by acetate. Ref.7
Post-translational modification	Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP MF_01123
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 652	652	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_0000208362
Sites
	Active site	517	1	By similarity
Amino acid modifications
	Modified residue	609	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27550-1 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: F464062B6E82C099	FASTA	652	72,094
	10 20 30 40 50 60 MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINVPDTFWG EQGKILDWIK PYQKVKNTSF 70 80 90 100 110 120 APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY KELHRDVCRF 130 140 150 160 170 180 ANTLLELGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNS 190 200 210 220 230 240 RLVITSDEGV RAGRSIPLKK NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL 250 260 270 280 290 300 VEQASDQHQA EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI 310 320 330 340 350 360 YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ VNILYTAPTA 370 380 390 400 410 420 IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGNEKCPVV DTWWQTETGG 430 440 450 460 470 480 FMITPLPGAT ELKAGSATRP FFGVQPALVD NEGNPLEGAT EGSLVITDSW PGQARTLFGD 490 500 510 520 530 540 HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP 550 560 570 580 590 600 KIAEAAVVGI PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 610 620 630 640 650 SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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." Wu G., Williams H.D., Zamanian M., Gibson F., Poole R.K. J. Gen. Microbiol. 138:2101-2112(1992) [PubMed: 1479344] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-652. Strain: K12.
[5]	"The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli." Brown T.D., Jones-Mortimer M.C., Kornberg H.L. J. Gen. Microbiol. 102:327-336(1977) [PubMed: 21941] [Abstract] Cited for: FUNCTION.
[6]	"Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli." Kumari S., Tishel R., Eisenbach M., Wolfe A.J. J. Bacteriol. 177:2878-2886(1995) [PubMed: 7751300] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Regulation of acetyl coenzyme A synthetase in Escherichia coli." Kumari S., Beatty C.M., Browning D.F., Busby S.J., Simel E.J., Hovel-Miner G., Wolfe A.J. J. Bacteriol. 182:4173-4179(2000) [PubMed: 10894724] [Abstract] Cited for: INDUCTION. Strain: K12.
[8]	"Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch." Barak R., Welch M., Yanovsky A., Oosawa K., Eisenbach M. Biochemistry 31:10099-10107(1992) [PubMed: 1390767] [Abstract] Cited for: ACETYLATION OF CHEY.
[9]	"Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli." Barak R., Abouhamad W.N., Eisenbach M. J. Bacteriol. 180:985-988(1998) [PubMed: 9473056] [Abstract] Cited for: INVOLVEMENT IN CHEMOTAXIS.
[10]	"Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis." Barak R., Eisenbach M. Mol. Microbiol. 40:731-743(2001) [PubMed: 11359578] [Abstract] Cited for: INVOLVEMENT IN CHEMOTAXIS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00006 Genomic DNA. Translation: AAC43163.1. U00096 Genomic DNA. Translation: AAC77039.1. AP009048 Genomic DNA. Translation: BAE78071.1. M87509 Genomic DNA. Translation: AAA24715.1. Sequence problems.
PIR	D65215.
RefSeq	AP_004570.1. NP_418493.1.
3D structure databases
SMR	P27550. Positions 5-647.
ModBase	Search...
Protein-protein interaction databases
STRING	P27550.
Proteomic databases
PRIDE	P27550.
Genome annotation databases
GeneID	948572.
GenomeReviews	Gene locus JW4030 in contig AP009048_GR. Gene locus b4069 in contig U00096_GR.
KEGG	ecj:JW4030. eco:b4069.
Organism-specific databases
EchoBASE	EB1417.
EcoGene	EG11448. acs.
CMR	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HBG547964.
OMA	TRVKNTS.
Enzyme and pathway databases
BioCyc	EcoCyc:ACS-MONOMER. ECOL168927:B4069-MONOMER. MetaCyc:ACS-MONOMER.
Gene expression databases
Genevestigator	P27550.
Family and domain databases
HAMAP	MF_01123. Ac_CoA_synth. [Tree]
InterPro	IPR011904. Ac_CoA_lig_AcsA. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSA_ECOLI

Accession

Primary (citable) accession number: P27550
Secondary accession number(s): Q2M6N5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	October 1, 1993
Last modified:	February 9, 2010
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)