ID ACSA_CUPNH Reviewed; 660 AA. AC P31638; Q0K8Q9; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 133. 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=acoE; GN OrderedLocusNames=H16_A2525; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBSTRATE SPECIFICITY. RX PubMed=1356967; DOI=10.1128/jb.174.20.6590-6599.1992; RA Priefert H., Steinbuechel A.; RT "Identification and molecular characterization of the acetyl coenzyme A RT synthetase gene (acoE) of Alcaligenes eutrophus."; RL J. Bacteriol. 174:6590-6599(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia RT eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). 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. Although acetate is the preferred substrate of AcsA, CC propionate is also used, but at a diminished rate compared with that of CC acetate. Fatty acids with more than three carbon atoms are usually not CC accepted as substrates by AcsA. {ECO:0000255|HAMAP-Rule:MF_01123, CC ECO:0000269|PubMed:1356967}. 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 -!- PATHWAY: Ketone degradation; acetoin degradation. 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; M97217; AAA21945.1; -; Genomic_DNA. DR EMBL; AM260479; CAJ93612.1; -; Genomic_DNA. DR PIR; A45736; A45736. DR RefSeq; WP_011615709.1; NZ_CP039287.1. DR AlphaFoldDB; P31638; -. DR SMR; P31638; -. DR STRING; 381666.H16_A2525; -. DR GeneID; 57644651; -. DR KEGG; reh:H16_A2525; -. DR PATRIC; fig|381666.6.peg.2916; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_4; -. DR OrthoDB; 9766486at2; -. DR BioCyc; MetaCyc:MONOMER-13637; -. DR UniPathway; UPA00040; -. DR Proteomes; UP000008210; Chromosome 1. DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016208; F:AMP binding; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro. DR CDD; cd05966; ACS; 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; IPR025110; AMP-bd_C. DR InterPro; IPR045851; AMP-bd_C_sf. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig_com. DR InterPro; IPR042099; ANL_N_sf. DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 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..660 FT /note="Acetyl-coenzyme A synthetase" FT /id="PRO_0000208353" FT BINDING 197..200 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 317 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 397..399 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 421..426 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 512 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 528 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 536 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 539 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 550 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 555 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT MOD_RES 625 FT /note="N6-acetyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" SQ SEQUENCE 660 AA; 72602 MW; EA03022F82C5C502 CRC64; MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYQALCDEAE RDYEGFWARH ARELLHWTKP FTKVLDQSNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV AIVFEADDGS VTRVTYRELH GKVCRFANGL KALGIRKGDR VVIYMPMSVE GVVAMQACAR LGATHSVVFG GFSAKSLQER LVDVGAVALI TADEQMRGGK ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD RWMEDVSAGQ PDTCEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWTFD IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD MIARHKVSIF YTAPTAIRSL IKAAEADEKI HPKQYDLSSL RLLGTVGEPI NPEAWMWYYK NIGNERCPIV DTFWQTETGG HMITPLPGAT PLVPGSCTLP LPGIMAAIVD ETGHDVPNGN GGILVVKRPW PAMIRTIWGD PERFRKSYFP EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM GTMEIESALV SNPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPTGEEAVK IATELRNWVG KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP AILEQLKQAQ //