BCACT_ROSHA
ID BCACT_ROSHA Reviewed; 446 AA.
AC G2SYC0; Q2TME9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Butyryl-CoA:acetate CoA-transferase {ECO:0000255|HAMAP-Rule:MF_03227, ECO:0000303|PubMed:16385128};
DE Short=Butyryl-CoA CoA-transferase {ECO:0000255|HAMAP-Rule:MF_03227};
DE EC=2.8.3.- {ECO:0000255|HAMAP-Rule:MF_03227};
GN OrderedLocusNames=RHOM_13820;
OS Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Roseburia.
OX NCBI_TaxID=585394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 11-16; 47-45 AND
RP 157-160, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183;
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 16839 / JCM 17582 / NCIMB 14029 / A2-183;
RX PubMed=26543119; DOI=10.1128/genomea.01286-15;
RA Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL Genome Announc. 3:E0128615-E0128615(2015).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.4 mM for acetate {ECO:0000269|PubMed:16385128};
CC KM=0.098 mM for butanoyl-CoA {ECO:0000269|PubMed:16385128};
CC KM=0.099 mM for propanoyl-CoA {ECO:0000269|PubMed:16385128};
CC Vmax=112 umol/min/mg enzyme with butanoyl-CoA as substrate
CC {ECO:0000269|PubMed:16385128};
CC Vmax=51 umol/min/mg enzyme with propanoyl-CoA as substrate
CC {ECO:0000269|PubMed:16385128};
CC pH dependence:
CC Optimum pH is 7-8. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY796317; AAX19660.1; -; Genomic_DNA.
DR EMBL; CP003040; AEN97870.1; -; Genomic_DNA.
DR RefSeq; WP_014080837.1; NC_015977.1.
DR AlphaFoldDB; G2SYC0; -.
DR SMR; G2SYC0; -.
DR STRING; 585394.RHOM_13820; -.
DR EnsemblBacteria; AEN97870; AEN97870; RHOM_13820.
DR KEGG; rho:RHOM_13820; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_030703_1_0_9; -.
DR OMA; EKMGIWR; -.
DR OrthoDB; 319106at2; -.
DR BioCyc; RHOM585394:G1H02-2743-MON; -.
DR BRENDA; 2.8.3.8; 10484.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000008178; Chromosome.
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 Direct protein sequencing; Fatty acid metabolism; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..446
FT /note="Butyryl-CoA:acetate CoA-transferase"
FT /id="PRO_0000447343"
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:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT 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"
SQ SEQUENCE 446 AA; 49163 MW; A3AF7CF45C20BCA0 CRC64;
MDFREEYKQK LVSADEAVKL IKSGDWVDYG WCTNTVDALD QALAKRTDEL TDVKLRGGIL
MKPLAVFARE DAGEHFCWNS WHMSGIERKM INRGVAYYCP IRYSELPRYY RELDCPDDVA
MFQVAPMDAH GYFNFGPSAS HLGAMCERAK HIIVEVNENM PRCLGGTECG IHISDVTYIV
EGSNPPIGEL GAGGPATDVD KAVAKLIVDE IPNGACLQLG IGGMPNAVGS LIAESDLKDL
GVHTEMYVDA FVDIAKAGKI NGSKKNIDRY RQTYAFGAGT KKMYDYLDDN PELMSAPVDY
TNDIRSISAL DNFISINNAV DIDLYGQVNA ESAGIKQISG AGGQLDFVLG AYLSKGGKSF
ICLSSTFKTK DGQVQSRIRP TLANGSIVTD ARPNTHYVVT EYGKVNLKGL STWQRAEALI
SIAHPDFRDD LIKEAEQMHI WRRSNR
