ID A0A5B9DB67_9ARCH Unreviewed; 596 AA. AC A0A5B9DB67; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 24-JAN-2024, entry version 13. DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:QEE16225.1}; GN ORFNames=DSAG12_02055 {ECO:0000313|EMBL:QEE16225.1}; OS Candidatus Prometheoarchaeum syntrophicum. OC Archaea; Asgard group; Candidatus Lokiarchaeota; Candidatus Lokiarchaeia; OC Candidatus Prometheoarchaeales; Candidatus Prometheoarchaeaceae; OC Candidatus Prometheoarchaeum. OX NCBI_TaxID=2594042 {ECO:0000313|EMBL:QEE16225.1, ECO:0000313|Proteomes:UP000321408}; RN [1] {ECO:0000313|EMBL:QEE16225.1, ECO:0000313|Proteomes:UP000321408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MK-D1 {ECO:0000313|EMBL:QEE16225.1, RC ECO:0000313|Proteomes:UP000321408}; RX PubMed=31942073; RA Imachi H., Nobu M.K., Nakahara N., Morono Y., Ogawara M., Takaki Y., RA Takano Y., Uematsu K., Ikuta T., Ito M., Matsui Y., Miyazaki M., Murata K., RA Saito Y., Sakai S., Song C., Tasumi E., Yamanaka Y., Yamaguchi T., RA Kamagata Y., Tamaki H., Takai K.; RT "Isolation of an archaeon at the prokaryote-eukaryote interface."; RL Nature 577:519-525(2020). CC -!- CATALYTIC ACTIVITY: CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl- CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00024484}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; CC Evidence={ECO:0000256|ARBA:ARBA00024484}; 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; CP042905; QEE16225.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5B9DB67; -. DR KEGG; psyt:DSAG12_02055; -. DR OrthoDB; 70225at2157; -. DR Proteomes; UP000321408; Chromosome. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR CDD; cd05907; VL_LC_FACS_like; 1. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. 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 PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1. DR PANTHER; PTHR43272:SF3; LONG-CHAIN-FATTY-ACID--COA LIGASE 5; 1. DR Pfam; PF00501; AMP-binding; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 4: Predicted; KW Ligase {ECO:0000313|EMBL:QEE16225.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000321408}. FT DOMAIN 25..419 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" SQ SEQUENCE 596 AA; 66810 MW; EA4ADC80F5483C8F CRC64; MVYEEYGKNI AIMRYDDPSN WVKVLEDTVQ KFPDRPYIGQ KDENGVFQWI IYKDFAKRVD NLRAGLAKIG IVEGDCVGII AGNRMEWALG AFATFGLIAK WVPMYEKELV DTWKYIIEDS KIKVLFVANN AVHEKMKHFT DNISTLEKIY IIESDADNSL KSLEKLGEAN PIPSKEPQLN DICSIIYTSG TTGDPKGVLL SHGNITNNAL AGKNVFPSLN EKSRALSILP WAHSYAQTAE LCAFTMIGAS IGITDVDHMS EDLVKTNPTF LICVPRLFNK IYDGIHRLME EEGGIKEKLF YMAKEAAKRK RETGKAGFKY KLLDKVVFGK VRARFGTQLE CSLTASAKTE LEIANFFFDI GLPIYDAYGL TESAPAISIN CPTFHKLGSV GKPIEKVKVV ISDEGEILAY GPNIMQGYLN KPEKTAAIMV EDEKGIKGIR TGDIGHIDED GFLFITGRIK NEYKLLNGKY VHPAAMEEYI KLIPWIANCL VFGDGKDYNV ALIVPDMATA EKYAEMADLS LPPEKIIEMP EVQALIGKEI KAHLKGNFGG YEIPKKFIFT TEDFTLDNGM LTQTFKLKRR NVLQKYGEKI EGLYKE //