ID ACSA_YERPS Reviewed; 652 AA. AC Q66FM8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 104. DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123}; DE Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123}; DE Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123}; DE EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123}; DE AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123}; DE AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123}; GN Name=acs {ECO:0000255|HAMAP-Rule:MF_01123}; GN OrderedLocusNames=YPTB0308; OS Yersinia pseudotuberculosis serotype I (strain IP32953). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Yersiniaceae; Yersinia. OX NCBI_TaxID=273123; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP32953; RX PubMed=15358858; DOI=10.1073/pnas.0404012101; RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M., RA Derbise A., Hauser L.J., Garcia E.; RT "Insights into the evolution of Yersinia pestis through whole-genome RT comparison with Yersinia pseudotuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004). CC -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), CC an essential intermediate at the junction of anabolic and catabolic CC pathways. Acs undergoes a two-step reaction. In the first half CC reaction, Acs combines acetate with ATP to form acetyl-adenylate CC (AcAMP) intermediate. In the second half reaction, it can then transfer CC the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the CC product AcCoA. {ECO:0000255|HAMAP-Rule:MF_01123}. CC -!- FUNCTION: Enables the cell to use acetate during aerobic growth to CC generate energy via the TCA cycle, and biosynthetic compounds via the CC glyoxylate shunt. Acetylates CheY, the response regulator involved in CC flagellar movement and chemotaxis. {ECO:0000255|HAMAP-Rule:MF_01123}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01123}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01123}; CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase CC activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000255|HAMAP-Rule:MF_01123}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX936398; CAH19548.1; -; Genomic_DNA. DR RefSeq; WP_011191563.1; NC_006155.1. DR AlphaFoldDB; Q66FM8; -. DR SMR; Q66FM8; -. DR GeneID; 49787698; -. DR KEGG; ypo:BZ17_2260; -. DR KEGG; yps:YPTB0308; -. DR PATRIC; fig|273123.14.peg.2394; -. DR Proteomes; UP000001011; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0003987; F:acetyl-CoA synthetase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016208; F:AMP binding; IEA:InterPro. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:TreeGrafter. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule. DR CDD; cd05966; ACS; 1. DR FunFam; 3.30.300.30:FF:000004; Acetyl-coenzyme A synthetase; 1. DR FunFam; 3.40.50.12780:FF:000001; Acetyl-coenzyme A synthetase; 1. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. DR HAMAP; MF_01123; Ac_CoA_synth; 1. DR InterPro; IPR011904; Ac_CoA_lig. DR InterPro; IPR032387; ACAS_N. DR InterPro; IPR045851; AMP-b_sf. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_synth/lig_dom. DR InterPro; IPR042099; ANL_N_sf. DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1. DR NCBIfam; NF001208; PRK00174.1; 1. DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1. DR PANTHER; PTHR24095:SF243; ACETYL-COENZYME A SYNTHETASE; 1. DR Pfam; PF16177; ACAS_N; 1. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 3: Inferred from homology; KW Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..652 FT /note="Acetyl-coenzyme A synthetase" FT /id="PRO_1000065337" FT BINDING 191 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 194 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 306 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 311 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 335 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 387 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 411 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 412 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 416 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 500 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 515 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 523 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 526 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 537 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 539 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 542 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 584 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT MOD_RES 609 FT /note="N6-acetyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" SQ SEQUENCE 652 AA; 72072 MW; 92FA2E582F1F7B76 CRC64; MSQIHKHPIP AAIAEHALIT PEKYQHYYQQ SVQNPDEFWG EQGKIIDWIK PYKTVKNTSF DPGHVSIRWF EDGTLNLAAN CLDRHLAERG DQTAIIWEGD DPNQSKTVTY KQLHHDVCQF ANVLKSLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPDA VAGRIIDSHS KLVITADEGI RAGRAIPLKK NVDEALKNPA ITSIKNVVVF QRTGNASYWE DGRDVWWHDL IKEASADCPP EEMNAEDPLF ILYTSGSTGK PKGVVHTTGG YLVYAALTFK YVFDYHPGDI YWCTADVGWV TGHSYLLYGP LACGAITLMF EGVPNYPGVN RLSQVVDKHK VNILYTAPTA IRALMAEGDK AIEGTKRDSL RIMGSVGEPI NPEAWEWYYN KIGNSKCPIV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD NLGNPQEGVA EGNLVITDSW PGQARTLFGD HDRFEQTYFS TFKGMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGV PHNIKGQAIY AYITLNHGEE PTPELYTEVR NWVRKEIGPL ATPDILHWTD SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVEK LLEEKQSMQT PS //