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Database: UniProt
Entry: A0A1I3F560_9FIRM
LinkDB: A0A1I3F560_9FIRM
Original site: A0A1I3F560_9FIRM 
ID   A0A1I3F560_9FIRM        Unreviewed;       448 AA.
AC   A0A1I3F560;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SAMN04487830_12041 {ECO:0000313|EMBL:SFI06369.1};
OS   Pseudobutyrivibrio sp. OR37.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=1798186 {ECO:0000313|EMBL:SFI06369.1, ECO:0000313|Proteomes:UP000198895};
RN   [1] {ECO:0000313|Proteomes:UP000198895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR37 {ECO:0000313|Proteomes:UP000198895};
RA   Varghese N., Submissions S.;
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; FOQF01000020; SFI06369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3F560; -.
DR   STRING; 1798186.SAMN04487830_12041; -.
DR   OrthoDB; 9801795at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000198895; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03227}.
FT   DOMAIN          4..182
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   448 AA;  49245 MW;  3A83488CA9B785B6 CRC64;
     MDFQAEYKSK LTTAEEAVKV VKSGDWVDYG WCTGTPDALD KALAARTDEL RDVKVRGGIL
     MKLPAIFERE DAGEHFCWNS WHMGGIERKL IARGCSYYAP IRYSELPRYY REHIEPNDVL
     MIQTTTMDNH GYFNFGPNAS HLMAAVEKSK HIIVEVNENM PRCLGGFEEG IHISKVDAIV
     EGSNPAISEM GAGGAPTDVD KAVAKLIVEE IPNGACLQLG IGGMPNTVGA MIADSDLKDL
     GVHTEMYVDA FVDIAKAGKI NGSKKNIDRF RQTYAFGAGT KKMYDYMDEN PELMSAPVDY
     TNDIRQISAL DNFISINNAV DVDLFGQINA ESAGTKHISG AGGQLDFVLG AYLSNGGKSF
     VCLSSTFTTK DGTVKSRIRP TLADGSIVTD TRANTHYLVT EYGKVCLKGL SAWERAEKII
     SIAHPDFRDE LIAEAEKMHI WRKSNKIS
//
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