ID Q3APY8_CHLCH Unreviewed; 666 AA. AC Q3APY8; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 101. 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=Cag_1685 {ECO:0000313|EMBL:ABB28937.1}; OS Chlorobium chlorochromatii (strain CaD3). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=340177 {ECO:0000313|EMBL:ABB28937.1}; RN [1] {ECO:0000313|EMBL:ABB28937.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CaD3 {ECO:0000313|EMBL:ABB28937.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Chlorobium chlorochromatii CaD3."; RL Submitted (AUG-2005) 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; CP000108; ABB28937.1; -; Genomic_DNA. DR AlphaFoldDB; Q3APY8; -. DR STRING; 340177.Cag_1685; -. DR KEGG; cch:Cag_1685; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_10; -. 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 50..103 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 111..490 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 551..629 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" FT REGION 1..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..23 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 213..216 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 331 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 355 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 407..409 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 431..436 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 520 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 535 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 543 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 546 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 557 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 559 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 562 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT MOD_RES 629 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" SQ SEQUENCE 666 AA; 74565 MW; BAC348AF52226EDF CRC64; MATETPSSSQ QEAAANPAED SISSVLTEKR KFPPPASFSE QAHLSTMEQY EKLYADAAAD PEGYWAGIAE QFHWFKKWDS VLEWNSPYAK WFNGGKTNIC YNALDVHVKS WRKNKAAVIW EGEQGDQRIL TYGELHRQVC KFANVLKIAG IKPGDRIAIY MGMVPELMIA VLACARVGAV HNVIFAGFSA HAITERVNDS RAKMVICADG TRRRGSTINL KNIVDEAIVN TPSVRNVIVL KTTGETIKMH DGMDHWWHDL MGLAVDESEA VELDAEHPLF VLYTSGSTGK PKGILHTTAG YMVHAASSFR YVFDIKDEDI YFCTADIGWI TGHSYMVYGP LLNGATLLMY EGAPNYPQWD RFWDIINRHK VTILYTAPTA IRAFIRAGNE WVTKHNLNSL RLLGTVGEPI NPEAWMWYHK VVGQEKCPIV DTWWQTETGG IMVSPMPGAT PTKPGTATRP LPGIMVDVVH KDGTPCGANE GGYLVIKKPW PSMLRTIYGD NERYEKTYWS EFKDMYFTGD GARKDDDGYI WIMGRVDDVV NVSGHRLGTS EVESALVSHE AVAEAAVVSR PDDIKGNSLV AFVTLKDEYE GDMKLRESLR NHVAREIGPI AKPDEIRWAK ALPKTRSGKI MRRLLRELAT SNEIKGDVTT LEDFGVLENL RDQENE //