ID Q59323_THETR Unreviewed; 498 AA. AC Q59323; O08504; O08515; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 08-NOV-2023, entry version 78. DE SubName: Full=Butyryl-CoA: acetate coenzyem A transferase {ECO:0000313|EMBL:CAB04794.1}; DE EC=2.8.3.8 {ECO:0000313|EMBL:CAA93155.1, ECO:0000313|EMBL:CAB04794.1}; DE SubName: Full=Butyryl-CoA:Acetate Coenzyme A transferase {ECO:0000313|EMBL:CAA93155.1}; DE SubName: Full=Butyryl-CoA:acetate CoA transferase {ECO:0000313|EMBL:CAB07501.1}; GN Name=actA {ECO:0000313|EMBL:CAA93155.1}; OS Thermoanaerobacterium thermosaccharolyticum (Clostridium OS thermosaccharolyticum). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacterium. OX NCBI_TaxID=1517 {ECO:0000313|EMBL:CAA93155.1}; RN [1] {ECO:0000313|EMBL:CAA93155.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 571 {ECO:0000313|EMBL:CAA93155.1}; RA Joerges A., Bronnenmeier K., Lottspeich F., Staudenbauer W.L.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAB04794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 571 {ECO:0000313|EMBL:CAB04794.1}; RA Van Rinsum A., Bronnenmeier K., Staudenbauer W.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CAB07501.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 571 {ECO:0000313|EMBL:CAB07501.1}; RA Van Rinsum A., Bronnenmeier K., Staudenbauer W.L.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. 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; Z69031; CAA93155.1; -; Genomic_DNA. DR EMBL; Z82038; CAB04794.1; -; Genomic_DNA. DR EMBL; Z92974; CAB07501.1; -; Genomic_DNA. DR PIR; T45465; T45465. DR AlphaFoldDB; Q59323; -. DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:UniProtKB-EC. DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. 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 Transferase {ECO:0000313|EMBL:CAA93155.1}. FT DOMAIN 14..215 FT /note="Acetyl-CoA hydrolase/transferase N-terminal" FT /evidence="ECO:0000259|Pfam:PF02550" FT DOMAIN 317..463 FT /note="Acetyl-CoA hydrolase/transferase C-terminal" FT /evidence="ECO:0000259|Pfam:PF13336" FT ACT_SITE 288 FT /note="5-glutamyl coenzyme A thioester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1" FT BINDING 263..267 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" FT BINDING 358 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" FT BINDING 378 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 402 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2" SQ SEQUENCE 498 AA; 55204 MW; 7A8A5E3DB7CAD7BD CRC64; MNFEERIRCN IIKNKVMSAE EAALLIKDGM TIGTSGFVTG GPKAVPLAIA ERYKNEKIKL NLYTGAIVGD ELDGAFAREG LVNKRIPYQT NKDMRNAINN GSVKFIDMHL SHMPQQIRYG FLGKIDIAII EATAITEDGG IIPTMSVGNS PTFVNMADKV IVEINTSQPI ELEGMHDIYE PKDPPYREPI PISKVSDRIG VPYIPCNPDK IAAVVFSDMK DTTLQLTSIN ETSKKISDYL IDFLQTEIKH GRLPKTFLPL QSGIGNVANA VLGGFIELKY NNLNLYSEVI QDAVLDLIDA DKVEKVSGTA LTLSEEGLKR FYTNINKYKD KIILRPQELS NNPEIIRRLG VISINTAIEV DIYGNVNSTH ILGTKMMNGI GGSADFTRNA YISIFATPST AKDDNISCIV PMVSHVDHTE HDVMVVVTEQ GLADLRGLSP KERAIAIIKN CAHPDYKDVL MEYYERAIKK HGAVQTPNLL DEAFLWHTRY SNTGSMKI //