ID A0A2T9WRX2_9CREN Unreviewed; 662 AA. AC A0A2T9WRX2; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 13-SEP-2023, entry version 19. DE SubName: Full=Acetate--CoA ligase {ECO:0000313|EMBL:PVU70604.1}; GN Name=acs {ECO:0000313|EMBL:PVU70604.1}; GN ORFNames=DDW09_02130 {ECO:0000313|EMBL:PVU70604.1}; OS Sulfolobus sp. SCGC AB-777_L09. OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=1987492 {ECO:0000313|EMBL:PVU70604.1, ECO:0000313|Proteomes:UP000245548}; RN [1] {ECO:0000313|EMBL:PVU70604.1, ECO:0000313|Proteomes:UP000245548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCGC AB-777_L09 {ECO:0000313|EMBL:PVU70604.1}; RX PubMed=26341207; DOI=10.1128/AEM.01539-15; RA Munson-McGee J.H., Field E.K., Bateson M., Rooney C., Stepanauskas R., RA Young M.J.; RT "Nanoarchaeota, Their Sulfolobales Host, and Nanoarchaeota Virus RT Distribution across Yellowstone National Park Hot Springs."; RL Appl. Environ. Microbiol. 81:7860-7868(2015). CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PVU70604.1}. 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; QEFI01000010; PVU70604.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2T9WRX2; -. DR Proteomes; UP000245548; Unassembled WGS sequence. DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:InterPro. DR GO; GO:0016208; F:AMP binding; IEA:InterPro. DR GO; GO:0005524; F:ATP 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 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:SF232; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:PVU70604.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000245548}. FT DOMAIN 28..81 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 91..534 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 542..620 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" SQ SEQUENCE 662 AA; 75293 MW; 4BCB704DE338CB28 CRC64; MSVNWALPFE EKIIPEDYKD RIVTPEKYKE MHRQATDNYR QFWESVASQI DWFKRWEKTL DDTNPPFYKW FVGGEINASY LAVDRHIKTV RKNKVAIIWE GEPVDDQGKP KEVKKLTYYD LYQEVNRVTY ILKEVYGIKK GDTISIYLPM IPELPIFMLA AARIGAIFSV VFSGFSSQAL ADRINDAKAK LLITADGGFR RGKIVPLKDI ADKALESTSS IQKVLVVKRT GSQVNMKEGR DEYYHDVLKQ VPLNAYIPPE PMKSEDPLFI LYTSGTTGKP KGIVHDTGGY MTILHATMNW VFDIKDTDIY WCTADIGWIT GHSYIVFGPL MEGATEVMYE GALDYPEPDR WASIIERYGV TIHYTSPTAI RSFMRYGEEI YKKHDFSTIR LMHSVGEPIN PEAFRWFFKL VGRDRIAFGS TWWMTETGGI MISHLPGLQL IPLKPGTNGM PLPGVDADVF DENGNPTNAG QRGYLVIKKP WPGMPLTIWG DPERYIKVYW SKFLGVFYPG DYAVKDSDGY FWILGRADEV IKVSGHRLGT YELESALIHH PAVAEAAVIG IPDEIKGEVP VAFVVLKVGQ KPSEELKKSL NDWVRNEVGA IATFKDIYFV SKLPKTRSGK IMRRVIRAVL TKQPIGDLTT LEDEASVEEV KKAYEELSKE IK //