ID A0A415E8J9_9FIRM Unreviewed; 456 AA.
AC A0A415E8J9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Probable butyrate:acetyl-CoA coenzyme A-transferase {ECO:0000256|HAMAP-Rule:MF_03228};
DE Short=Butyrate CoA-transferase {ECO:0000256|HAMAP-Rule:MF_03228};
DE EC=2.8.3.- {ECO:0000256|HAMAP-Rule:MF_03228};
GN ORFNames=DW099_04530 {ECO:0000313|EMBL:RHJ90117.1};
OS Emergencia timonensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Emergencia.
OX NCBI_TaxID=1776384 {ECO:0000313|EMBL:RHJ90117.1, ECO:0000313|Proteomes:UP000284841};
RN [1] {ECO:0000313|EMBL:RHJ90117.1, ECO:0000313|Proteomes:UP000284841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM07-24 {ECO:0000313|EMBL:RHJ90117.1,
RC ECO:0000313|Proteomes:UP000284841};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Coenzyme A-transferase that converts butyrate to butyryl-CoA.
CC {ECO:0000256|HAMAP-Rule:MF_03228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + butanoate = acetate + butanoyl-CoA;
CC Xref=Rhea:RHEA:30071, ChEBI:CHEBI:17968, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57371; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03228};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000256|HAMAP-
CC Rule:MF_03228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03228}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000256|ARBA:ARBA00009632, ECO:0000256|HAMAP-Rule:MF_03228}.
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:RHJ90117.1}.
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DR EMBL; QRMS01000001; RHJ90117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415E8J9; -.
DR STRING; 1776384.GCA_900086585_03194; -.
DR OrthoDB; 9801795at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000284841; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_03228; But_CoA_trans; 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; IPR023990; Butryl-CoA_acetate_CoA_Tfrase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR21432:SF20; ACETYL-COA HYDROLASE; 1.
DR PANTHER; PTHR21432; ACETYL-COA HYDROLASE-RELATED; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03228};
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_03228};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03228};
KW Reference proteome {ECO:0000313|Proteomes:UP000284841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03228}.
FT DOMAIN 11..196
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 285..441
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 252
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 227..231
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 326
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT BINDING 349
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
SQ SEQUENCE 456 AA; 50660 MW; 5184FA295BDBA46A CRC64;
MKRLTPAEKI QDDYEAKLVS ADEAVKVVKS GDQIHLGLFC GVAVDLERAL AKRAEELTDV
TVCTTMWSYK EPPEILKADP GAKHFHYCST HLTGTERKQN KAGNCWFLPV QFRENPKFYE
ECRETFDVAM LQVAAMDASG NFNLGPQVAE YWGVLRNCKK IIVEVNQNMP VNHGQENYLN
INQIDYIVEG SNSPLPTISA KEASDAEKKM AEHIVTRIES GSTLQLGTGG FPNYVGKLIA
ESDIDDLSCH TEMFVDAYLH LFEAGKLTNN KRINQGKMTY TFAMGSKELY DWIDDNQMMQ
VAPVDYVNDV DVISQNEKMI SVNSCLQVDL FGQVNSESSG LQHIGGTGGQ LDFVMGAFKS
KGGKSFLCTP STRTLKDGRK ESLILPVLPT GSIVSTPRSA VHYIVTEYGA VNLKGRNTYE
RAELLVSIAH PDFREELIEE AKKMGIWKTS SKVVNA
//
