ID ACSA_SHESW Reviewed; 650 AA. AC A1RIK1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 86. 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}; GN OrderedLocusNames=Sputw3181_1659; OS Shewanella sp. (strain W3-18-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=351745; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W3-18-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella sp. W3-18-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000503; ABM24496.1; -; Genomic_DNA. DR RefSeq; WP_011788994.1; NC_008750.1. DR AlphaFoldDB; A1RIK1; -. DR SMR; A1RIK1; -. DR KEGG; shw:Sputw3181_1659; -. DR HOGENOM; CLU_000022_3_6_6; -. DR Proteomes; UP000002597; Chromosome. 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: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: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. FT CHAIN 1..650 FT /note="Acetyl-coenzyme A synthetase" FT /id="PRO_1000065325" FT BINDING 191..194 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..389 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 411..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 650 AA; 72374 MW; 3E623F228961B003 CRC64; MSSQSLYKVS GNIAANALVN NEQYKTMYQE SIVNPEGFWR EHGKRIDWIK PYTKIKKTSF DDHNLSINWF YDGTLNASAN CLDRHLAEHS DRVAIIWEGD NASEQRKITY GELHADVCKF ANALRSQGVR RGDIVTIYMP MVPEAAVAML ACARIGAVHS VVFGGFSPDS IASRVIDGKS KVVITSDEGM RGGRAIPLKR NIDDALNHPD VTSVEKVIVL KRTGGKIDWV EGRDVWWHSL LETASEHCQP EEMGAEDPLF LLYTSGSTGN PKGVLHTTGG YMVYASMTHE YVFDYKAGEV YWCTADVGWI TGHSYMVYGP LANGATVLIH EGVPNHPSPA RLGEMIDRHK VNILYTAPTL IRALMAEGKQ HFDQFDGSTL RIMGSVGEPI NPEAWRWYHE VIGHEHCPIV DTWWQTETGG ILITPLPGAT DTKPGSATRP FFGVQPALVD NMGNILEGEN EGNLVLLDSW PGQMRTVYGD HERFVLTYFK TFRGMYFTGD GARRDEDGYY WITGRVDDVI NVSGHRLGTA EVESALVSHE LVAEAAVVGY PHDIKGQGIY AYVTLTRGTE ESEELRQELR QWVRKEIGAL ATPDLIQWAS GLPKTRSGKI MRRFLRKIAA NEVTNLGDAS TLADPAVIET LIETRLNRTE //