ID B0T280_CAUSK Unreviewed; 646 AA. AC B0T280; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 88. 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=Caul_0111 {ECO:0000313|EMBL:ABZ69249.1}; OS Caulobacter sp. (strain K31). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ69249.1}; RN [1] {ECO:0000313|EMBL:ABZ69249.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K31 {ECO:0000313|EMBL:ABZ69249.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Stephens C., Richardson P.; RT "Complete sequence of chromosome of Caulobacter sp. K31."; RL Submitted (JAN-2008) 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 --------------------------------------------------------------------------- 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; CP000927; ABZ69249.1; -; Genomic_DNA. DR AlphaFoldDB; B0T280; -. DR STRING; 366602.Caul_0111; -. DR KEGG; cak:Caul_0111; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_5; -. DR OrthoDB; 9803968at2; -. 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..81 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 86..465 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 529..607 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" FT BINDING 191..194 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 309 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 333 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 385..387 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 409..414 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 498 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 513 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 521 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 524 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 537 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 540 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 582 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT MOD_RES 607 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" SQ SEQUENCE 646 AA; 70982 MW; 1AA950EAE622162D CRC64; MSDGQVFPIP DDWAGKAHID AAGYEAALAR VEADPEGYWR DLAGRLDWIR APTQIKDVSF AKDDFRIHWY ADGVLNVSAN CIDRHLPHRK DEVALIFEGD EPGVSSTLTY GQLHEEVCRM ANVLKVQGVR KGDRVTIYLP MIPIAAVAML ACARIGAVHS VVFGGFSPDS IAGRIQDCGS HFVITADEGR RGGKRVPLKA NIDKALEHCP WVSKVLMVRW TGAETTLVRH RDVVWEDVKD SVSADCPPEP MNAEDPLFIL YTSGSTGKPK GVLHTTGGYL AWAAWTHEAV FDYRPGEVFW CTADVGWVTG HSYVVYGPLA NGGTSLIFEG VPNYPTPARF WEVVDKHQVE IFYTAPTALR ALMREGDDWV TKNDLSSLRL LGSVGEPINP EAWLWYHRVV GKDRLPIVDT WWQTETGGVL VSPLPGATAL KPGSATKPLP GVKLQLVDAE GHVLEGATEG NLLITDSWPG QMRTVYGDHG RFFDTYFSAY PGKYFTGDGC RRDADGYYWI TGRVDDVINV SGHRLGTAEI ESALVAHDTV AEAAVVGYPH DIKGQGVYAY VTLRAGVEPT DSLRKDLMLW VRQEIGPFAA PDVLQWAPGL PKTRSGKIMR RILRKIAENE LGSLGDISTL ADPSVVDDLV KNRANS //