ID Q98AG0_RHILO Unreviewed; 562 AA. AC Q98AG0; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 27-MAR-2024, entry version 106. DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:BAB52370.1}; GN OrderedLocusNames=mll6017 {ECO:0000313|EMBL:BAB52370.1}; OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OS (Mesorhizobium loti (strain MAFF 303099)). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB52370.1, ECO:0000313|Proteomes:UP000000552}; RN [1] {ECO:0000313|EMBL:BAB52370.1, ECO:0000313|Proteomes:UP000000552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099 RC {ECO:0000313|Proteomes:UP000000552}; RX PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., RA Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). 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; BA000012; BAB52370.1; -; Genomic_DNA. DR RefSeq; WP_010913699.1; NC_002678.2. DR AlphaFoldDB; Q98AG0; -. DR KEGG; mlo:mll6017; -. DR PATRIC; fig|266835.9.peg.4790; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_59_10_5; -. DR Proteomes; UP000000552; Chromosome. DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt. DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt. 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; IPR020845; AMP-binding_CS. 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. DR PROSITE; PS00455; AMP_BINDING; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000256|ARBA:ARBA00022598}. FT DOMAIN 31..406 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 460..538 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" SQ SEQUENCE 562 AA; 61281 MW; 64118BA2EA72A8F2 CRC64; MLFEKDSFEE VRRSFQWSIP ERFNIGVDIC DKWAEADPTR LAIVDVDPAG FTREYTFSDL RTMSNRLANA LFGHGVGRQV GETGDRVGVL LPQRVETAVA HIAVTKLGCV SIPLFTLFGP EALEHRLRDS GARVVITDRA GAERVASIRS RVPSIELVVC VDGRGEGDEV SFQEMCSEQS DTFIPVDTHS DDPAILIYTS GTTGNPKGAL HAHRVLLGHL PGVEISHDFL PKPDDRFWTP ADWAWIGGLL DVLMPALHHG IPVVACRFSK FTTEAAITLI RSQRIRNVFL PPTALKMLKL KPAEECSGLD LRSVASGGET LGAELIQWGK DALGVTINEF YGQTECNMIV SSCAALEPPA LGSMGRPVPG HDVDVIDPVS RLRQPAGVEG AIAALAPDPV MFLGYWNNPD ATREKFIHGP EGRWLVTGDR GVRDNDGRLR FVGRDDDVIG SAGYRIGPAE IEDCLLGHPS VRLAGAVGKP DEIRGSVVAA YVVLREGFSP SQNLAEDIAA HVKSRLAAHE YPRVVRFIDE MPMTTTGKII RGALRKIAQE EAALEARSRQ KD //