ID A4F6L2_SACEN Unreviewed; 660 AA. AC A4F6L2; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 105. 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 ECO:0000313|EMBL:CAL99686.1}; GN OrderedLocusNames=SACE_0337 {ECO:0000313|EMBL:CAL99686.1}; OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / OS NBRC 13426 / NCIMB 8594 / NRRL 2338). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharopolyspora. OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99686.1, ECO:0000313|Proteomes:UP000006728}; RN [1] {ECO:0000313|EMBL:CAL99686.1, ECO:0000313|Proteomes:UP000006728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}; RX PubMed=17369815; DOI=10.1038/nbt1297; RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., RA Haydock S.F., Leadlay P.F.; RT "Complete genome sequence of the erythromycin-producing bacterium RT Saccharopolyspora erythraea NRRL23338."; RL Nat. Biotechnol. 25:447-453(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: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; CC Evidence={ECO:0000256|ARBA:ARBA00000131, 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|ARBA:ARBA00006432, 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; AM420293; CAL99686.1; -; Genomic_DNA. DR RefSeq; WP_011873025.1; NC_009142.1. DR AlphaFoldDB; A4F6L2; -. DR SMR; A4F6L2; -. DR STRING; 405948.SACE_0337; -. DR GeneID; 306457264; -. DR KEGG; sen:SACE_0337; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_11; -. DR Proteomes; UP000006728; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0003987; F:acetyl-CoA synthetase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016208; F:AMP binding; IEA:InterPro. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:TreeGrafter. DR CDD; cd05966; ACS; 1. DR FunFam; 3.40.50.12780:FF:000001; Acetyl-coenzyme A synthetase; 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; IPR045851; AMP-b_sf. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_synth/lig_dom. DR InterPro; IPR042099; ANL_N_sf. DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1. DR NCBIfam; NF001208; PRK00174.1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006728}. FT BINDING 198..201 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 317 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 341 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 393..395 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 417..422 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 508 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 531 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 534 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 545 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 547 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 550 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT MOD_RES 620 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" SQ SEQUENCE 660 AA; 72043 MW; F986E6A54DAD71C8 CRC64; MSEPDGQSNT LDNLLTESRT FPPSGEFAAQ ANATSELYAQ ADADREAFWA DQARHLHWDT EWEQVLDWSG APFAKWFVGG KLNVAYNCVD RHVEAGNGDR VAIHWEGEPG DSRAITYAEL AREVSRTANA LASLGVGAGD RVAIYLPMLP EAVYSMLACA RLGALHSVVF GGFSSEALRT RINDAQAKVV ITADGQYRRG KAMPLKTNVD EAVAATPSVE HVLVVQRTKT DVEWNDGRDQ WWHDVVEGRP ASHTPEFFDS EHPLFILYTS GTTGRPKGIL HTSGGYLTQA AYTHRTVFDL KPETDVYWCT ADIGWVTGHT YIVYGPLANG ATQVIYEGTP NTPHEGRHWD IVQKYGVTLY YTAPTTIRTF MKWGAEIPAR YDLSTLRVLG SVGEPINPEA WMWYREHIGG NRAPIVDTWW QTETGAIMIS PLPGVTATKP GSAQVPLPGI AAKVVDESGE QVGHGGGGLL VLDQPWPAML RGIWGDDDRY RETYWSKFAD KGYYFAGDGA KYDDDGDIWL LGRVDDVMNV SGHRISTTEV ESALVSHPTV AEAAVVGASD PTTGQGIVAF VILRGGADDQ ASGEAAIKAL RDHVAHEIGP IAKPRQIMVV PELPKTRSGK IMRRLLRDVA ENREIGDVST LADSSVMDLI SAGLGKSTED //