Q8FAY8 (ACSA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	c5064

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	652 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity. HAMAP MF_01123
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123
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)
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: EC
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_0000208363
Sites
	Active site	517	1	By similarity
Amino acid modifications
	Modified residue	609	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FAY8 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 8389484535DEC4C3	FASTA	652	71,967
	10 20 30 40 50 60 MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINAPDTFWG EQGKILDWIT PYQKVKNTSF 70 80 90 100 110 120 APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY KELHRDVCRF 130 140 150 160 170 180 ANTLLELGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSSS 190 200 210 220 230 240 RLVITSDEGV RAGRSIPLKK NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL 250 260 270 280 290 300 VEQASAQHQA 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

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN83490.1.
RefSeq	NP_756916.1. NC_004431.1.
3D structure databases
ProteinModelPortal	Q8FAY8.
SMR	Q8FAY8. Positions 5-647.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000041840; EBESCP00000040189; EBESCG00000040890.
GeneID	1039151.
GenomeReviews	Gene locus c5064 in contig AE014075_GR.
KEGG	ecc:c5064.
PATRIC	18287808. VBIEscCol75197_4750.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008803.
HOGENOM	HBG547964.
OMA	TRGTEES.
PhylomeDB	Q8FAY8.
ProtClustDB	PRK00174.
Family and domain databases
HAMAP	MF_01123. Ac_CoA_synth. [Tree]
InterPro	IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01895.
PANTHER	PTHR24095:SF42. PTHR24095:SF42. 1 hit.
Pfam	PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 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_ECOL6

Accession

Primary (citable) accession number: Q8FAY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program