ID C1DFK2_AZOVD Unreviewed; 645 AA. AC C1DFK2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 82. 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 Synonyms=acsA2 {ECO:0000313|EMBL:ACO80398.1}; GN OrderedLocusNames=Avin_42750 {ECO:0000313|EMBL:ACO80398.1}; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO80398.1, ECO:0000313|Proteomes:UP000002424}; RN [1] {ECO:0000313|EMBL:ACO80398.1, ECO:0000313|Proteomes:UP000002424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424}; RX PubMed=19429624; DOI=10.1128/JB.00504-09; RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G., RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A., RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S., RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I., RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L., RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., RA Dean D.R., Dixon R., Wood D.; RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized RT to support diverse anaerobic metabolic processes."; RL J. Bacteriol. 191:4534-4545(2009). 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; CP001157; ACO80398.1; -; Genomic_DNA. DR RefSeq; WP_012702766.1; NC_012560.1. DR AlphaFoldDB; C1DFK2; -. DR STRING; 322710.Avin_42750; -. DR EnsemblBacteria; ACO80398; ACO80398; Avin_42750. DR KEGG; avn:Avin_42750; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_6; -. DR OrthoDB; 9803968at2; -. DR Proteomes; UP000002424; 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: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 24..80 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 82..464 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 528..606 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" FT BINDING 190..193 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 308 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 332 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 384..386 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 408..413 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 497 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 512 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 520 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 523 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 534 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 536 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 539 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT MOD_RES 606 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" SQ SEQUENCE 645 AA; 71897 MW; 2196F80A1AE5C342 CRC64; MFKIANHPVS EALRQHSWLN NDDYLRLYRQ SVEQPDSFWA EQATLFLDWF KPWRNIHRGD MNKGEIHWFE GSQLNVAHNC IDRHLKQRGD QVAIIWEGDN PADSARITYR QLHEQVCRLA NLLKSRGIGK GDRVCIYMPM IPEAAYAMLA CARIGAVHSV VFGGFSPEAL RDRILDADCR LLITADESVR GGKVVPLKRN ADKALQSCSG VSSVIVVRRT GGAIDWNVGR DLWYHEAVPG CSADCPAEPM DAEAPLFILY TSGSTGKPKG VLHTTGGYLL QAAMTHQYVF DYHDGDIYWC SADIGWITGH SYIVYGPLAN GATTLIFEGV PNYPDASRFW QVVDKHRVNI FYTAPTALRS LMREGEGPVR KTSRASLRLL GSVGEPINPE AWEWYYHVVG DSRCPIVDTW WQTETGAIMI TPLPGATLLK PGSATRPFFG VQPVLLDDKG KEIEGPGAGI LAIKASWPSQ IRSIYGDHQR LIDTYFKPCP GYYFTGDGAR RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDSIA EAAVVGCPHD VKGQCVYAFV TLVTGSRPSD QLKRELIDQV SREIGGFAKP DFLQWAPRLP KTRSGKIMRR ILRKIACNEL DNLGDTSTLS DPSVLQELID NRLSH //