ID ACSA_NITEC Reviewed; 655 AA. AC Q0AFF1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 93. 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=Neut_1690; OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=335283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 101675 / C91 / Nm57; RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x; RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.; RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas RT eutropha C91: implications for niche adaptation."; RL Environ. Microbiol. 9:2993-3007(2007). 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; CP000450; ABI59931.1; -; Genomic_DNA. DR RefSeq; WP_011634737.1; NC_008344.1. DR AlphaFoldDB; Q0AFF1; -. DR SMR; Q0AFF1; -. DR STRING; 335283.Neut_1690; -. DR KEGG; net:Neut_1690; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_4; -. DR OrthoDB; 9766486at2; -. DR Proteomes; UP000001966; 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; 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. PE 3: Inferred from homology; KW Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding. FT CHAIN 1..655 FT /note="Acetyl-coenzyme A synthetase" FT /id="PRO_1000065298" FT BINDING 196..199 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 316 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 392..394 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 416..421 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 508 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 523 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 531 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 534 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 545 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" FT BINDING 547 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" 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 MOD_RES 620 FT /note="N6-acetyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123" SQ SEQUENCE 655 AA; 73338 MW; B81E66505C045F43 CRC64; MATIESILRE NRIFPPANEF VRHANITGMK TYEALRQEAE RDYAGFWAKL AKQYITWHKP FTRILDDTNP PFYKWFDDGE LNISWNCLDR HLTTQANKTA IIFESDEGEV IRCSYRELHQ RVCRFANGLK ALGIRQGDRI VIYMPMRIEA VVAMQACARI GVIHSVVFGG FSAKSVYERI IDAGASAVIT ADEQTRGGKR HALKATVDEA LAMGDTTSVH SVIVFRHTGT DIPWQPERDR WWHNLTASQS DECEPIWVNA EHPLFTLYTS GSTGKPKGVQ HSSAGYLLGA IVSMQWVFDY HSEDIFWCTA DVGWVTGHSY VTYGPLAIGA TQVIFEGTPT YPHAGRFWEI IQKHRVTTFY TAPTAIRSLI KLGPDLPEKY DLSSLRLLGS VGEPINPEAW MWYYTVIGQS RCPVVDTWWQ TETGSHMIAP IPGAIPAKPG SCTLPLPGID AAVVDETGLP AEQGKGGFLV IKRPFPSMLR TLWNDPERFR NTYFPADIAG GHYYLAGDSA HRDQDGYFWI MGRIDDVLNV SGHRLGTMEI ESALVAHPLV AEAAVVGKPH EIRGEVIVAF VVLRGKLPDD QQAAEIAETL REWVSSEIGA IARPEEIRFG ENLPKTRSGK LMRRLLRSLA RGETITQDIS TLENPVILEQ FSQTI //