ID A0A1H4AF70_9FIRM Unreviewed; 451 AA.
AC A0A1H4AF70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Butyryl-CoA:acetate CoA-transferase {ECO:0000256|HAMAP-Rule:MF_03227};
DE Short=Butyryl-CoA CoA-transferase {ECO:0000256|HAMAP-Rule:MF_03227};
DE EC=2.8.3.- {ECO:0000256|HAMAP-Rule:MF_03227};
GN ORFNames=SAMN04515656_10849 {ECO:0000313|EMBL:SEA34645.1};
OS Eubacterium aggregans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA34645.1, ECO:0000313|Proteomes:UP000199394};
RN [1] {ECO:0000313|EMBL:SEA34645.1, ECO:0000313|Proteomes:UP000199394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR12 {ECO:0000313|EMBL:SEA34645.1,
RC ECO:0000313|Proteomes:UP000199394};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Coenzyme A-transferase that converts butyryl-CoA to butyrate.
CC {ECO:0000256|HAMAP-Rule:MF_03227}.
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_03227};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000256|HAMAP-
CC Rule:MF_03227}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC Butyryl-CoA CoA-transferase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03227}.
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DR EMBL; FNRK01000008; SEA34645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4AF70; -.
DR STRING; 81409.SAMN04515656_10849; -.
DR OrthoDB; 9801795at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000199394; Unassembled WGS sequence.
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:0046358; P:butyrate biosynthetic 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_03227; But_acet_CoA_trans; 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 NCBIfam; TIGR03948; butyr_acet_CoA; 1.
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 Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_03227};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03227};
KW Reference proteome {ECO:0000313|Proteomes:UP000199394};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03227}.
FT DOMAIN 5..186
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 282..438
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 248
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 223..227
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 323
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 346
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
SQ SEQUENCE 451 AA; 49832 MW; 3E571AA38917305E CRC64;
MSYIKEYADK LKTAEEAVAI VKSGDWLDYG WTTATVRALD EALAERIKKE PELKDLKIRG
GILMWEPEIF KLPDAKEHFT WNSWHMSGIE RKAVAKGFSF YDPLRYSELP RYYRENITPP
DVAMFQVAPM DKHGYFNFGP NASHMMAVCE RAKVVIVEVN ENIPRCLGGF EEAIHISKVD
VIVEGENPAM AEMGAGGPAT DVDIAVANLI VPEIPNGACL QLGIGGMPNT VGAMIAESDL
KDLGVHTEMY VDAFVDLSRA GKVTGSHKTV NRYKQVYAFA AGTKKLYDFL DDNPECMAVP
VNYANDIDTI GNIDNFISIN NAVDIDLYGQ VNAETAGTKQ ISGAGGQLDF VLGAYKSKGG
KSFICCSSAF KDKKGELHSR IRPTLANGSV VTDTRANIHY LVTEYGIVNL KGLSTWERAE
AIIKVAHPQF QDELIAEAEK MNIWRRTNKE D
//
