ID Q01NE9_SOLUE Unreviewed; 643 AA. AC Q01NE9; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123}; DE Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123}; DE Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123}; DE EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123}; DE AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123}; DE AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123}; GN Name=acsA {ECO:0000256|HAMAP-Rule:MF_01123}; GN OrderedLocusNames=Acid_7927 {ECO:0000313|EMBL:ABJ88821.1}; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae; OC Solibacter. OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ88821.1}; RN [1] {ECO:0000313|EMBL:ABJ88821.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ88821.1}; 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 Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Janssen P.H., Kuske C.R., Richardson P.; RT "Complete sequence of Solibacter usitatus Ellin6076."; RL Submitted (OCT-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:0000256|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:0000256|HAMAP- CC Rule:MF_01123}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01123}; CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase CC activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000256|HAMAP-Rule:MF_01123}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CP000473; ABJ88821.1; -; Genomic_DNA. DR AlphaFoldDB; Q01NE9; -. DR STRING; 234267.Acid_7927; -. DR KEGG; sus:Acid_7927; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_0; -. DR InParanoid; Q01NE9; -. DR OrthoDB; 9778383at2; -. 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: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 {ECO:0000256|ARBA:ARBA00022990, ECO:0000256|HAMAP- KW Rule:MF_01123}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01123}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01123}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01123}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01123}. FT DOMAIN 25..79 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 88..470 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 527..605 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" FT BINDING 189..192 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 307 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 383..385 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 407..412 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 496 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 511 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 519 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 522 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 533 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 535 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 538 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT MOD_RES 605 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" SQ SEQUENCE 643 AA; 72281 MW; 207212BA2B0D0D0E CRC64; MADANVYPPS AEFVSTANVK GMAGYRALYQ RAAEKPEEFW GELADQELHW FRKWTHVFEW DPPFAKWFAG GKINASYNCI DRHLSTPRKN KVAILWEGEP GDQRMITYQE LHRLVCRFAN VLKARGLKAG DRAIIYMGMV PELPVAVLAC ARLGIIHSVV FGGFSAEALK ARIQDLEAQV VITCDGAWRR GKEVRLKDAV DESLAGCDTV KDVIVYRRTG GSIPMQEGRD HWWHDLDTEA SEVCPAEELD SEHPLYVLYT SGTTGKPKGI VHTTGGYLLQ AHMTMKWVFD LHEEDTYWCT ADIGWVTGHS YIVYGPLSAG ATSVMYEGAP DFPQPDRFWR LIEKYKVNIF YTSPTAIRSF VRQGDQWPNA HDMSSLRLLG SVGEPINPAA WEWYYKVIGK ERCPIVDTWW QTETGAIMIA PMPGAVPLKP GSGTLPLPGV IADIVDLQGN PVEANREGFL IVRRPWPSIA RTLWREPDRY KQAYWERVPG VYLAGDAARR DEDGYFWILG RVDDVMNVSG HRLSTMELES ALVRHPAVAE AAVVGKPHEI TGQAVACFVT LKKGTWDHTA LAEELRKWVA HEIGSFAKPE QIRFTDSLPK TRSGKIMRRL LREIVTSNSV TGDVTTLEDL SVVTRLSAQH DED //