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Database: UniProt
Entry: R9M8K4_9FIRM
LinkDB: R9M8K4_9FIRM
Original site: R9M8K4_9FIRM 
ID   R9M8K4_9FIRM            Unreviewed;       443 AA.
AC   R9M8K4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Probable butyrate:acetyl-CoA coenzyme A-transferase {ECO:0000256|HAMAP-Rule:MF_03228};
DE            Short=Butyrate CoA-transferase {ECO:0000256|HAMAP-Rule:MF_03228};
DE            EC=2.8.3.- {ECO:0000256|HAMAP-Rule:MF_03228};
GN   ORFNames=C816_01175 {ECO:0000313|EMBL:EOS67026.1};
OS   Oscillibacter sp. 1-3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillibacter.
OX   NCBI_TaxID=1235797 {ECO:0000313|EMBL:EOS67026.1, ECO:0000313|Proteomes:UP000014108};
RN   [1] {ECO:0000313|EMBL:EOS67026.1, ECO:0000313|Proteomes:UP000014108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-3 {ECO:0000313|EMBL:EOS67026.1,
RC   ECO:0000313|Proteomes:UP000014108};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Oscillibacter bacterium 1-3.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Coenzyme A-transferase that converts butyrate to butyryl-CoA.
CC       {ECO:0000256|HAMAP-Rule:MF_03228}.
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_03228};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_03228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03228}.
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000256|ARBA:ARBA00009632, ECO:0000256|HAMAP-Rule:MF_03228}.
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:EOS67026.1}.
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DR   EMBL; ASTC01000006; EOS67026.1; -; Genomic_DNA.
DR   RefSeq; WP_016321493.1; NZ_KE159703.1.
DR   AlphaFoldDB; R9M8K4; -.
DR   STRING; 1235797.C816_01175; -.
DR   PATRIC; fig|1235797.3.peg.1271; -.
DR   eggNOG; COG0427; Bacteria.
DR   HOGENOM; CLU_030703_1_0_9; -.
DR   OrthoDB; 9801795at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000014108; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0019605; P:butyrate metabolic 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_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   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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03228};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_03228};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03228};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014108};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03228}.
FT   DOMAIN          4..186
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          276..431
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        242
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT   BINDING         217..221
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT   BINDING         317
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
FT   BINDING         340
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03228"
SQ   SEQUENCE   443 AA;  49221 MW;  3B3573D6A3669ADD CRC64;
     MLLEEYRQKL RTPQEAVKAV KSGDWVDYTS NVCFPTLLDQ ALAARRDELT DVKVRGNLCF
     GPIRIVECDP GREHFTYNSW HCSAYERKLC DRGQCSYIPM IFRNVVPYYR HFLTVNVAMM
     CVPPMDRHGY FNLSCASGIA RGILEKADIV ILEVNEHLPR ILGGFDESIH LSDVDYVVEG
     EHAPLPQFPV APPTNEDRKI AELLIPHIPS GAALQLGIGG MPNVVGSLLA QSDLKDLGMH
     TELCGDAYYE LFRAGKLTNA RKNIHRHKGM TGIVFGSRAL YDWVDQNPGV VAAPLEYVNA
     PEVIAQLDNM ISINSCIAAD LYGQVCAESA GLRQISGTGG QLDYLTGAAM SKGGKAFICM
     TSSFTDKTGV RRSRVLPHFG GDIVTDPRSQ AYYLVTEYGA VNLAGRSVWE RAERLISIAH
     PDFREELIAA AERQKIWRNS NRR
//
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