ID F8GWA8_CUPNN Unreviewed; 560 AA. AC F8GWA8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 46. DE SubName: Full=Acetyl-coenzyme A synthetase AcsA {ECO:0000313|EMBL:AEI81683.1}; DE EC=6.2.1.1 {ECO:0000313|EMBL:AEI81683.1}; GN Name=acsA1 {ECO:0000313|EMBL:AEI81683.1}; GN OrderedLocusNames=CNE_BB1p02590 {ECO:0000313|EMBL:AEI81683.1}; OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 OS / N-1) (Ralstonia eutropha). OG Plasmid pBB1 {ECO:0000313|EMBL:AEI81683.1, OG ECO:0000313|Proteomes:UP000006798}. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI81683.1, ECO:0000313|Proteomes:UP000006798}; RN [1] {ECO:0000313|EMBL:AEI81683.1, ECO:0000313|Proteomes:UP000006798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1 RC {ECO:0000313|Proteomes:UP000006798}; RC PLASMID=pBB1 {ECO:0000313|EMBL:AEI81683.1, RC ECO:0000313|Proteomes:UP000006798}; RX PubMed=21742890; DOI=10.1128/JB.05660-11; RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.; RT "Complete genome sequence of the type strain Cupriavidus necator N-1."; RL J. Bacteriol. 193:5017-5017(2011). CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000256|ARBA:ARBA00006432}. 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; CP002879; AEI81683.1; -; Genomic_DNA. DR AlphaFoldDB; F8GWA8; -. DR KEGG; cnc:CNE_BB1p02590; -. DR HOGENOM; CLU_000022_59_10_4; -. DR Proteomes; UP000006798; Plasmid pBB1. DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR045851; AMP-bd_C_sf. DR InterPro; IPR000873; AMP-dep_Synth/Lig_com. DR InterPro; IPR042099; ANL_N_sf. DR PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1. DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEI81683.1}; KW Plasmid {ECO:0000313|EMBL:AEI81683.1}. FT DOMAIN 51..394 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 459..537 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" SQ SEQUENCE 560 AA; 60445 MW; 6BD21686CC296463 CRC64; MEILSPLAEL GERVSELIDH YADSSASLAW MLCDRHDPAS VAYDIVDANL RVERLTYGEL RVQSEAFAAG LLDLGVRSGD RVATLAGKSL EYLVALLGIW RIGAVHVPLF TAFAPPAVAL RLEGSGARVV VCDASQRSKL SSSEDGEPAP RYDIVVISDD ELSLEEPALH RYQDVLKAGH RVSPAALGGD APFIHIYTSG TTGKPKGVVV PSRAIAAFHA YVEFGIGLRA DDVYWCAADP GWAYGLYFGV VGSLCTGVQS VFQKGGFDPA LTYDVLRQCG VTNFAAAPTV FRSLMCADVT APAGLHLRSA SSAGEPLTPD VNEWAAQALG VSVYDHYGQT EAGMLINNHH DPRLVRPIQS GCMGISMPGW KAVVLDRTED VEVPPGTVGR IAFKLADSPL AWFAGYDGLP EKSAEKFSRD GQYYLSGDLA RADETGAFFF SSREDDVIIM AGYRIGPFEV ESVLTAHPAV AECAVIAVPD KVRGEVIEAY VVLRPGFEAT DEAAVELQQW VKTRYAAHAY PRRVTFISEL PKTPSGKVQR FVLREARKNA DLDGKGDEKH //