ID ACSA_CAMJE Reviewed; 657 AA. AC Q9PMD2; Q0P888; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 02-SEP-2026, entry version 128. 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=acsA {ECO:0000255|HAMAP-Rule:MF_01123}; Synonyms=acs; GN OrderedLocusNames=Cj1537c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), CC an essential intermediate at the junction of anabolic and catabolic CC pathways. AcsA undergoes a two-step reaction. In the first half CC reaction, AcsA 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 -!- 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; AL111168; CAL35637.1; -; Genomic_DNA. DR PIR; G81300; G81300. DR RefSeq; WP_002851288.1; NC_002163.1. DR RefSeq; YP_002344909.1; NC_002163.1. DR AlphaFoldDB; Q9PMD2; -. DR SMR; Q9PMD2; -. DR IntAct; Q9PMD2; 33. DR STRING; 192222.Cj1537c; -. DR PaxDb; 192222-Cj1537c; -. DR EnsemblBacteria; CAL35637; CAL35637; Cj1537c. DR GeneID; 905819; -. DR KEGG; cje:Cj1537c; -. DR PATRIC; fig|192222.6.peg.1514; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_7; -. DR OrthoDB; 9765680at2; -. DR Proteomes; UP000000799; 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 CDD; cd05966; ACS; 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:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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..657 FT /note="Acetyl-coenzyme A synthetase" FT /id="PRO_0000208358" FT BINDING 192 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 195 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 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 504 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 519 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 530 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 543 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 546 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 592 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT MOD_RES 617 FT /note="N6-acetyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" SQ SEQUENCE 657 AA; 73958 MW; F1E77BA491B3D0F5 CRC64; MLNQNNQELF KPSKEFSRNA RIKNLCEYYD LCDEAKEDFE GFWKRQAFEK IEWFSPFSRV LNEDKAPFYK WFEGGTLNVS YQCLDRHMKT RRNKAALIFE GEMGDYEVYT YRRLLHETCK AANLLKKFGV KKGDRVVIYM PMIPETAIVM LACARIGAIH SVVFGGFSPE ALRDRIIDAG AKLVVTADGA FRRGKPYMLK PAVDKALSEG CESVEKVLIV IRNNEPIEYI KGRDYVYNEL VKNESYKCEP EIMDSEDLLF LLYTSGSTGK PKGVMHASAG YILWAQMTME WVFDIKDYDN YWCSADVGWI TGHTYVVYGP LACGATTIMH EGTPTYPNSG RWWRMIEEYQ ISKFYTSPTA IRMLHADAPN EPRKYDLSTL EVLGTVGEPI NPSAWKWFYD EIGGTKSPIV DTWWQTETGG HMITPLPGAT PLKPGCATLP LPGIFAEVID EEGNKKDEGE DGLLCITKPW PSMIRGIWGN DERYIESYFS QAKKDGKAVY FSGDGAFYDK NGYITITGRT DDVVNVAGHR IGTAEIESAI AKHPSVAESA VVSILDTIKG ESLFAFVVLS PASSCDLGGA IETLKELNDI LRVEIGPIAK IEKILYTPGL PKTRSGKIMR RILRTIARGE EIKQDISTLE DSKVVETIVK LAKAEFE //