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Database: UniProt
Entry: A0A3A9G556_9FIRM
LinkDB: A0A3A9G556_9FIRM
Original site: A0A3A9G556_9FIRM 
ID   A0A3A9G556_9FIRM        Unreviewed;       446 AA.
AC   A0A3A9G556;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=D7Y06_19460 {ECO:0000313|EMBL:RKJ61735.1};
OS   Roseburia sp. 1XD42-69.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=2320088 {ECO:0000313|EMBL:RKJ61735.1, ECO:0000313|Proteomes:UP000279120};
RN   [1] {ECO:0000313|EMBL:RKJ61735.1, ECO:0000313|Proteomes:UP000279120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1XD42-69 {ECO:0000313|EMBL:RKJ61735.1,
RC   ECO:0000313|Proteomes:UP000279120};
RA   Liu C.;
RT   "Murine metabolic-syndrome-specific gut microbial biobank.";
RL   Submitted (SEP-2018) 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}.
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:RKJ61735.1}.
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DR   EMBL; RAZG01000060; RKJ61735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9G556; -.
DR   OrthoDB; 9801795at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000279120; 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:UP000279120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03227}.
FT   DOMAIN          5..183
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          279..435
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        245
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT   BINDING         220..224
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT   BINDING         320
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
FT   BINDING         343
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03227"
SQ   SEQUENCE   446 AA;  49150 MW;  42D244460C806A06 CRC64;
     MDFAKEYEQK LTTADEAVKI IKSGDWVDYG WCNGTPDALD KALAKRTDEL KDINLRGGIL
     LKPLAVFERE DAGEHFTWNS WHMSGLERKY INRGCAYYAP IRYSELPRYY RESATKNDVA
     MFQVTPMDKH GYFNFGPNAS HLMAVCETSK KIIVEVNENM PRCLGGFENG IHISQVDYIV
     EGENPAIGEL GAGGEPTDVD IAVAKLIVEE IPNGACLQLG IGGMPNTVGS MIAESDLKDL
     GVHTEMYVDA FVDIAKAGKI NGSKKNIDRF RQTFGFGCGT KKMYDYLDNN PEMLSAPVSY
     TNDIRSVSSL DNFISINNAV DLDLFGQVNA ESAGVKHISG AGGQLDFVLG AYLSNGGKSF
     ICCSSTFKTK DGTLKSRILP TLNPGSIVTD TRANVHYVVT EYGKVNLKGL SAWQRAEALI
     SIAHPDFRDE LIAEADKMKI WRRSNK
//
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