BCACT_ANACD
ID BCACT_ANACD Reviewed; 446 AA.
AC B0MC58; Q2QB27;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Butyryl-CoA:acetate CoA-transferase {ECO:0000255|HAMAP-Rule:MF_03227, ECO:0000303|PubMed:16385128};
DE EC=2.8.3.- {ECO:0000255|HAMAP-Rule:MF_03227};
DE AltName: Full=Butyryl-CoA CoA-transferase {ECO:0000255|HAMAP-Rule:MF_03227};
GN ORFNames=ANACAC_01149;
OS Anaerostipes caccae (strain DSM 14662 / CCUG 47493 / JCM 13470 / NCIMB
OS 13811 / L1-92).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=411490;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=DSM 14662 / CCUG 47493 / JCM 13470 / NCIMB 13811 / L1-92;
RX PubMed=16385128; DOI=10.1099/mic.0.28412-0;
RA Charrier C., Duncan G.J., Reid M.D., Rucklidge G.J., Henderson D.,
RA Young P., Russell V.J., Aminov R.I., Flint H.J., Louis P.;
RT "A novel class of CoA-transferase involved in short-chain fatty acid
RT metabolism in butyrate-producing human colonic bacteria.";
RL Microbiology 152:179-185(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14662 / CCUG 47493 / JCM 13470 / NCIMB 13811 / L1-92;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerostipes caccae (DSM 14662).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14662 / CCUG 47493 / JCM 13470 / NCIMB 13811 / L1-92;
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Coenzyme A-transferase that converts butyryl-CoA to butyrate.
CC Can also use proprionyl-CoA as substrate in vitro. {ECO:0000255|HAMAP-
CC Rule:MF_03227, ECO:0000269|PubMed:16385128}.
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:0000255|HAMAP-
CC Rule:MF_03227, ECO:0000269|PubMed:16385128};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30073;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03227,
CC ECO:0000269|PubMed:16385128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + propanoate = acetate + propanoyl-CoA;
CC Xref=Rhea:RHEA:23520, ChEBI:CHEBI:17272, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000269|PubMed:16385128};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23522;
CC Evidence={ECO:0000269|PubMed:16385128};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_03227, ECO:0000305}.
CC -!- MISCELLANEOUS: The fermentation acid butyrate is of special interest,
CC as it has been shown to serve as the preferred energy source for the
CC gut wall and also influences cell differentiation and apoptosis in the
CC colon, and this seems to aid in protection against colon cancer and
CC inflammatory bowel disease. Formation of butyrate via butyryl-CoA CoA-
CC transferase is the only available route for butyrate synthesis in the
CC majority of human gut isolates. {ECO:0000305|PubMed:16385128}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC Butyryl-CoA CoA-transferase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03227}.
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DR EMBL; DQ151450; ABA39273.1; -; Genomic_DNA.
DR EMBL; ABAX03000012; EDR97528.1; -; Genomic_DNA.
DR RefSeq; WP_006566634.1; NZ_DS499733.1.
DR AlphaFoldDB; B0MC58; -.
DR SMR; B0MC58; -.
DR STRING; 411490.ANACAC_01149; -.
DR EnsemblBacteria; EDR97528; EDR97528; ANACAC_01149.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_030703_1_0_9; -.
DR OrthoDB; 319106at2; -.
DR BRENDA; 2.8.3.8; 10485.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000004935; Unassembled WGS sequence.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:InterPro.
DR GO; GO:0018729; F:propionate CoA-transferase activity; IEA:RHEA.
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 GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR Gene3D; 3.40.1080.20; -; 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; IPR003702; ActCoA_hydro.
DR InterPro; IPR023990; Butryl-CoA_acetate_CoA_Tfrase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR Pfam; PF02550; AcetylCoA_hydro; 1.
DR SUPFAM; SSF100950; SSF100950; 2.
DR TIGRFAMs; TIGR03948; butyr_acet_CoA; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Lipid metabolism; Transferase.
FT CHAIN 1..446
FT /note="Butyryl-CoA:acetate CoA-transferase"
FT /id="PRO_0000447681"
FT ACT_SITE 245
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT Rule:MF_03227"
FT BINDING 220..224
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT Rule:MF_03227"
FT BINDING 320
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03227"
FT BINDING 343
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT Rule:MF_03227"
FT BINDING 370
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ SEQUENCE 446 AA; 49064 MW; 668F3FB33F93E01B CRC64;
MSFKEEYQKK LKTADEAVKV VKSGDWLEYG WCVTTPAALD KALAKRMPEL ENINIRGGIV
MWPLEITKID SPADHFTWNS WHMGGLERKW IKEGFSYYAP IRYSELPGYY RNYIDHVDVA
MMQVAPMDEH GFFNFGPSAS HLAAMLEKAD CVIVEVNENM PRCLGGFEEG VHISKVDMIV
EGENPAIAEL GGGGAATDVD KAVAKLIVDQ IPNGACLQLG IGGMPNAVGS MIAESDLKDL
GVHTEMYVDA FVDIAKAGKI TGARKNIDRY RQTYAFAAGT KKLYDYLNDN PECMSAPVNY
TNDIARVSSI DNFISINNAV DVDLYGQISA ESSGIKQISG AGGQLDFVMG AYLSNGGKSF
VCLSSTFTDK AGQMHSRILP TLHNGSIVTD TRANAHYIVT EYGMANMKGL SAWQRAEALI
NIAHPDFRDQ LIKDAEKAQI WRRSNK
