ID Q8FS81_COREF Unreviewed; 502 AA. AC Q8FS81; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 97. DE SubName: Full=Putative acetate CoA-transferase {ECO:0000313|EMBL:BAC17330.1}; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC17330.1, ECO:0000313|Proteomes:UP000001409}; RN [1] {ECO:0000313|EMBL:BAC17330.1, ECO:0000313|Proteomes:UP000001409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395 RC {ECO:0000313|Proteomes:UP000001409}; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family. CC {ECO:0000256|ARBA:ARBA00009632}. 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; BA000035; BAC17330.1; -; Genomic_DNA. DR RefSeq; WP_011075028.1; NC_004369.1. DR AlphaFoldDB; Q8FS81; -. DR STRING; 196164.gene:10740922; -. DR KEGG; cef:CE0520; -. DR eggNOG; COG0427; Bacteria. DR HOGENOM; CLU_019748_3_0_11; -. DR OrthoDB; 9801795at2; -. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro. DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:TreeGrafter. DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. DR FunFam; 3.40.1080.20:FF:000001; Acetyl-CoA hydrolase Ach1; 1. DR Gene3D; 3.30.750.70; 4-hydroxybutyrate coenzyme like domains; 1. DR Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1. DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1. DR InterPro; IPR026888; AcetylCoA_hyd_C. DR InterPro; IPR038460; AcetylCoA_hyd_C_sf. DR InterPro; IPR046433; ActCoA_hydro. DR InterPro; IPR003702; ActCoA_hydro_N. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR InterPro; IPR017821; Succinate_CoA_transferase. DR NCBIfam; TIGR03458; YgfH_subfam; 1. DR PANTHER; PTHR43609; ACETYL-COA HYDROLASE; 1. DR PANTHER; PTHR43609:SF1; ACETYL-COA HYDROLASE; 1. DR Pfam; PF13336; AcetylCoA_hyd_C; 1. DR Pfam; PF02550; AcetylCoA_hydro; 1. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2. PE 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000001409}; KW Transferase {ECO:0000313|EMBL:BAC17330.1}. FT DOMAIN 7..220 FT /note="Acetyl-CoA hydrolase/transferase N-terminal" FT /evidence="ECO:0000259|Pfam:PF02550" FT DOMAIN 333..466 FT /note="Acetyl-CoA hydrolase/transferase C-terminal" FT /evidence="ECO:0000259|Pfam:PF13336" FT ACT_SITE 292 FT /note="5-glutamyl coenzyme A thioester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1" FT BINDING 267..271 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" FT BINDING 362 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" FT BINDING 382 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" FT BINDING 386 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" FT BINDING 406 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" SQ SEQUENCE 502 AA; 54873 MW; 2A0DC11C27B2369B CRC64; MSERIASAEF RSKVMSAEEA AQFVNNGDTV GMSGFTGAAY PKALPTAIAN RAKEAHSKGD EYAINLLTGA STAPDCDGVL AEADAINYRM PYQSDPEMRN KINAGAMKYQ DIHLSHSGLQ VEQGFFGHLD VAIVEVCRIT EDGHLVPSSG VGNNVEYLES AHKIIIEVNS WQSLELEGMA DIYRVPHLPN RTPIPINNVN DRIGETFIRI DTNKVVAVVE TDSPDRNSPF KPFDETSKQI AGNFLDFLEG EVRAGRLTYD GYIMQSGVGN VPNAVMAGLL DSKFENIKAY TEVVQDGMLD LIDAGKMTQA SATSFALSPE YAEKMNREAS TYRKSLVLRP LQISNSPEVI RRMGLIASNG MIEADIYGNV NSTHVAGTRI MNGIGGSGDF TRNAFVSSFI SPSVAKGDAI SAVVPFASHI DHTEHDAMVV ITEYGYADLR GLAPRERAPK MISIAHPDYR PLLEEYFERA QQNKHQHTPH NLRDALSFHI NLDETGSMKG NA //