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Database: UniProt
Entry: A0A1H3Z6V0_9FIRM
LinkDB: A0A1H3Z6V0_9FIRM
Original site: A0A1H3Z6V0_9FIRM 
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
//
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