ID A8G3Y5_PROM2 Unreviewed; 660 AA. AC A8G3Y5; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 91. 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=acs {ECO:0000313|EMBL:ABV50316.1}; GN Synonyms=acsA {ECO:0000256|HAMAP-Rule:MF_01123}; GN OrderedLocusNames=P9215_07011 {ECO:0000313|EMBL:ABV50316.1}; OS Prochlorococcus marinus (strain MIT 9215). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV50316.1, ECO:0000313|Proteomes:UP000002014}; RN [1] {ECO:0000313|EMBL:ABV50316.1, ECO:0000313|Proteomes:UP000002014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV50316.1, RC ECO:0000313|Proteomes:UP000002014}; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(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; 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; CP000825; ABV50316.1; -; Genomic_DNA. DR RefSeq; WP_012007434.1; NC_009840.1. DR AlphaFoldDB; A8G3Y5; -. DR STRING; 93060.P9215_07011; -. DR KEGG; pmh:P9215_07011; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_3; -. DR OrthoDB; 9778383at2; -. DR Proteomes; UP000002014; 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 40..92 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 102..486 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 547..625 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" FT BINDING 202..205 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 322 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 398..400 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 422..427 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 516 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 531 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 539 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 542 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 553 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 555 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 558 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT MOD_RES 625 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" SQ SEQUENCE 660 AA; 74061 MW; 00F0F96C4E7DDEEB CRC64; MSLDKKNSIN NILEEKRIFP PSKKFAENSN ISTQEELLSL KKQASDNPIQ FWESFAKSEL DWFKPFQTVL DKENAPFFKW FKEGKLNITY NCLDRHIKRG LGGKTALIWE GEPGDSKKYT YEELLKEVCK AANALKAIGV KKGDLVCIYM PMIPEAMFAM LACARIGAPH SVVFGGFSSE ALKDRLIDGN ARFVITADGG FRKDKVIELK KAVDAAIESG ADKVVEKVVV VQRSQKNISM VDDRDFWWHE LLKDQKDHCE PEIMNSEDRL FILYTSGSTG KPKGVVHTTG GYNLWTHLTF KWIFDLKDDD IYWCTADVGW ITGHSYIVYG PLSNGATTLM YEGVPRPSNL GAFWEIVQKY KVSIFYTAPT AIRAFMKSGR EIPDKYNLES LRLLGTVGEP INPEAWMWYK DVIGKDKCPI VDTWWQTETG GVMISPLPGV VATKPGSATF PLPGIEVEIV DKNGDKVKEN EGGYLIIKKP WPGMMRTIHG NSERYLESYW EYISFKGEQN VYFAGDGARI DEDGYIWIMG RVDDVISVSG HRLGTMEIES ALVSHKSVAE SAVVGKKDDL KGEVIVAFVS LEKDVNGSSE LVENLKKHVV NEIGIIAKPE KIIISDFLPK TRSGKIMRRI LRSLAAGEKI SGDISTLEDS SVLEKLKELS //