Q8X5T5 (ACSA_ECO57) 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:	Z5668, ECs5051

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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_0000208364
Sites
	Active site	517	1	By similarity
Amino acid modifications
	Modified residue	609	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X5T5 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: A1ACE8469025E8C6	FASTA	652	72,110
	10 20 30 40 50 60 MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINAPDTFWG EQGKILDWIK PYQKVKNTSF 70 80 90 100 110 120 APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY KELHRDVCRF 130 140 150 160 170 180 ANTLLKLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNS 190 200 210 220 230 240 RLVITSDEGV RAGRSIPLKK NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDQ 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 GARRDEDSYY 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]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG59267.1. BA000007 Genomic DNA. Translation: BAB38474.1.
PIR	C91260. G86100.
RefSeq	NP_290702.1. NC_002655.2. NP_313078.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X5T5.
SMR	Q8X5T5. Positions 5-647.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000027568; EBESCP00000026461; EBESCG00000026620. EBESCT00000058502; EBESCP00000056330; EBESCG00000057550.
GeneID	914284. 960055.
GenomeReviews	Gene locus Z5668 in contig AE005174_GR. Gene locus ECs5051 in contig BA000007_GR.
KEGG	ece:Z5668. ecs:ECs5051.
PATRIC	18359703. VBIEscCol44059_4988.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008803.
HOGENOM	HBG547964.
OMA	LIQWAGG.
ProtClustDB	PRK00174.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS5051-MONOMER.
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_ECO57

Accession

Primary (citable) accession number: Q8X5T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program