ID E6WHR8_PANSA Unreviewed; 651 AA. AC E6WHR8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 74. 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:0000256|HAMAP-Rule:MF_01123}; GN OrderedLocusNames=Pat9b_0328 {ECO:0000313|EMBL:ADU67654.1}; OS Pantoea sp. (strain At-9b). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU67654.1, ECO:0000313|Proteomes:UP000001624}; RN [1] {ECO:0000313|EMBL:ADU67654.1, ECO:0000313|Proteomes:UP000001624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-9b {ECO:0000313|EMBL:ADU67654.1, RC ECO:0000313|Proteomes:UP000001624}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.; RT "Complete sequence chromosome of Pantoea sp. At-9b."; RL Submitted (DEC-2010) 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. Acs undergoes a two-step reaction. In the first half CC reaction, Acs 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 -!- FUNCTION: Enables the cell to use acetate during aerobic growth to CC generate energy via the TCA cycle, and biosynthetic compounds via the CC glyoxylate shunt. Acetylates CheY, the response regulator involved in CC flagellar movement and chemotaxis. {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; CP002433; ADU67654.1; -; Genomic_DNA. DR RefSeq; WP_013507523.1; NC_014837.1. DR AlphaFoldDB; E6WHR8; -. DR STRING; 592316.Pat9b_0328; -. DR KEGG; pao:Pat9b_0328; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_6; -. DR OrthoDB; 9803968at2; -. DR Proteomes; UP000001624; 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:UniProtKB-UniRule. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule. 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:SF243; ACETYL-COENZYME A SYNTHETASE; 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|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01123}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW 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 83..466 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 531..609 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 311 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 335 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 387..389 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 411..416 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 500 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 515 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 523 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 526 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 539 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 542 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT BINDING 584 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" FT MOD_RES 609 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123" SQ SEQUENCE 651 AA; 71523 MW; F10BEEDD2003560E CRC64; MSQIHKHPVP AAIAENALIN AEQYAAMYQQ SVDDPETFWG EQGKILDWIT PYSKVKNTSF APGNVAIRWY EDGTLNLAAN CLDRHLASRG DHPAIIWEGD DANESKTLTF RQLHADVCRF ANVLGSLGVK KGDVVAIYMP MVPEAAIAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNA KLVITADEGI RAGRGIPLKK NVDDALNNPN VTSVKNVVVF KRTGKDTGWR EGRDLWWHDL MADAADQHQP VAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPEDV YWCTADVGWV TGHSYLIYGP LACGATTLMF EGVPNWPKPS RMAEVVDKHK VTLLYTAPTA IRALMAEGDK AIEGTDRSSL RIMGSVGEPI NPEAWEWYYN KIGDGRCPIV DTWWQTETGG FMITPLPGAI ELKAGSATKP FFGVQPALVD NEGNTLEGAT EGNLVIVDSW PGQARTLFGD HDRFEQTYFS TFKNRYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI PHSIKGQAIY AYITLNHGEE PSPELYTEVR NWVRKEIGPI ATPDVLHWTD SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPGVVEK LLEEKQSIKM P //