ID A0A1H3Z6V0_9FIRM Unreviewed; 447 AA.
AC A0A1H3Z6V0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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_10531 {ECO:0000313|EMBL:SEA19012.1};
OS Eubacterium aggregans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA19012.1, ECO:0000313|Proteomes:UP000199394};
RN [1] {ECO:0000313|EMBL:SEA19012.1, ECO:0000313|Proteomes:UP000199394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR12 {ECO:0000313|EMBL:SEA19012.1,
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; FNRK01000005; SEA19012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3Z6V0; -.
DR STRING; 81409.SAMN04515656_10531; -.
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 DEACYLASE; 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 6..188
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 280..436
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 246
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 221..225
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 321
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT BINDING 344
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
SQ SEQUENCE 447 AA; 49637 MW; 5842208464117DEB CRC64;
MRFIRDYATK LTTAENAVKA VKSGDWVDYG WTTGTPRASD YALAKRIINE NLTDLKFHGG
ILMWEPEIFK IPNPSAHLVW NSWHLSGIER RAVQQGFAYY CPLRYSELPR YYRENIEPVD
VAFFQVAPMD SHGYFNFGPN ASHMMALCET AKVIVVEVNK NMPRCLGGVE EAIHISQVDY
IVEGDNPPMA EMGAGKAGEV DRRVAELIVP EIPNGACLQL GIGGMPNAVG ALIAESDLKD
LGVHTEMFVD AFVDITEAGK INGSKKAIDR FRQTYAFGAG TQKLYDFLDE NPQCMGMPVD
YTNDVRVISQ IDNFMSINNA VDIDLFGQVN AESSGYHQIS GAGGQLDFVL GAYLSKGGKS
FICCSSTFKT RSGELKSRIL PILKPGSTVT DTRPNTHYVV TEYGKVCLKG MSTWQRAEAL
IAIAHPDFRD DLIQEAEKMK IWRKSNR
//