ID I4CUB2_STUST Unreviewed; 651 AA. AC I4CUB2; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 24-JAN-2024, entry version 57. 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 ORFNames=A458_12170 {ECO:0000313|EMBL:AFM33669.1}; OS Stutzerimonas stutzeri CCUG 29243. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Stutzerimonas. OX NCBI_TaxID=1196835 {ECO:0000313|EMBL:AFM33669.1, ECO:0000313|Proteomes:UP000006063}; RN [1] {ECO:0000313|EMBL:AFM33669.1, ECO:0000313|Proteomes:UP000006063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 29243 {ECO:0000313|EMBL:AFM33669.1, RC ECO:0000313|Proteomes:UP000006063}; RX PubMed=23144395; DOI=10.1128/JB.01753-12; RA Brunet-Galmes I., Busquets A., Pena A., Gomila M., Nogales B., RA Garcia-Valdes E., Lalucat J., Bennasar A., Bosch R.; RT "Complete Genome Sequence of the Naphthalene-Degrading Bacterium RT Pseudomonas stutzeri AN10 (CCUG 29243)."; RL J. Bacteriol. 194:6642-6643(2012). 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; CP003677; AFM33669.1; -; Genomic_DNA. DR RefSeq; WP_014820603.1; NC_018028.1. DR AlphaFoldDB; I4CUB2; -. DR KEGG; psc:A458_12170; -. DR PATRIC; fig|1196835.3.peg.2453; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_3_6_6; -. DR Proteomes; UP000006063; 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: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; 71716 MW; D85BB766C8B3B657 CRC64; MSAASVYPVR PEVAAQSLTN EASYKAMYQQ SVINPEGFWR EQAARLNWIR PFTEVKRTSF DDHHVDIKWF ADGTLNVSAN CLDRHLAERG DQLAIIWEGD DPSEHREITY RELHQEVSKF ANALRGQDVH RGDVVTIYMP MIPEAAVAML ACARIGAIHS VVFGGFSPEA LAGRIIDGQS KIVITADEGV RGGKPVPLKG NVDEALTNPQ TSCVKKIIVV RRTGADIRWH SHRDICYDDL MRVAGEVCAP KEMGAEEPLF ILYTSGSTGK PKGVLHTCGG YLLYAALTHE RVFDYRPGEV YWCTADIGWI TGHSYLIYGP LANGATTLMY EGVPNHPDVT RIARIIDKHK VNILYTAPTA IRAMMAEGAA AVEGADGSSL RLLGTVGEPI NPEAWHWYYE TVGQSRCPIV DTWWQTETGG ILISPLPGAT TLKPGSATRP MFGVVPGLVD NLGNLLEGPA EGNLVILDSW PGQMRTIYKD HDRFVDTYFK TFRGMYFTGD GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHA KVAEAAAVGV PHKLKGQAIY VYVTLVSGVQ PSDALRQELQ QWVRKEIGPI AVPDVIQWAP GLPKTRSGKI MRRLLRKIAT DDYDALGDTS TLADPGVVDQ LIEAHEAVRK R //