BAIF_CLOSV
ID BAIF_CLOSV Reviewed; 426 AA.
AC P19413;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bile acid CoA-transferase BaiF {ECO:0000305|PubMed:22021638};
DE EC=2.8.3.25 {ECO:0000269|PubMed:22021638};
DE AltName: Full=Bile acid coenzyme A transferase {ECO:0000303|PubMed:22021638};
DE AltName: Full=Bile acid-inducible operon protein F;
DE AltName: Full=Lithocholoyl-CoA:cholate CoA-transferase {ECO:0000305|PubMed:22021638};
GN Name=baiF {ECO:0000303|PubMed:9869646};
OS Clostridium scindens (strain JCM 10418 / VPI 12708).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=29347;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=2254270; DOI=10.1128/jb.172.12.7011-7019.1990;
RA Mallonee D.H., White W.B., Hylemon P.B.;
RT "Cloning and sequencing of a bile acid-inducible operon from Eubacterium
RT sp. strain VPI 12708.";
RL J. Bacteriol. 172:7011-7019(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=3170477; DOI=10.1128/jb.170.10.4555-4561.1988;
RA White W.B., Franklund C.V., Coleman J.P., Hylemon P.B.;
RT "Evidence for a multigene family involved in bile acid 7-dehydroxylation in
RT Eubacterium sp. strain VPI 12708.";
RL J. Bacteriol. 170:4555-4561(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35, AND PROTEIN SEQUENCE OF 2-29.
RX PubMed=2448288; DOI=10.1128/jb.170.2.611-616.1988;
RA White W.B., Coleman J.P., Hylemon P.B.;
RT "Molecular cloning of a gene encoding a 45,000-dalton polypeptide
RT associated with bile acid 7-dehydroxylation in Eubacterium sp. strain VPI
RT 12708.";
RL J. Bacteriol. 170:611-616(1988).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=9869646;
RA Ye H.Q., Mallonee D.H., Wells J.E., Bjorkhem I., Hylemon P.B.;
RT "The bile acid-inducible baiF gene from Eubacterium sp. strain VPI 12708
RT encodes a bile acid-coenzyme A hydrolase.";
RL J. Lipid Res. 40:17-23(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=22021638; DOI=10.1194/jlr.m020313;
RA Ridlon J.M., Hylemon P.B.;
RT "Identification and characterization of two bile acid coenzyme A
RT transferases from Clostridium scindens, a bile acid 7alpha-dehydroxylating
RT intestinal bacterium.";
RL J. Lipid Res. 53:66-76(2012).
CC -!- FUNCTION: Functions in the bile acid 7alpha-dehydroxylation pathway,
CC which forms secondary bile acids via the 7alpha-dehydroxylation of
CC primary bile acids, and is carried out by intestinal anaerobic
CC bacteria. Acts as a bile acid CoA transferase with broad bile acid
CC substrate specificity. Catalyzes the transfer of the CoA moiety of
CC secondary bile acid-CoA compounds to primary bile acids. Can use
CC lithocholoyl-CoA, deoxycholoyl-CoA and allodeoxycholoyl-CoA as bile
CC acid CoA donors and cholate, allocholate, chenodeoxycholate,
CC ursodeoxycholate, and beta-muricholate as bile acid CoA acceptors
CC (PubMed:22021638). Also displays CoA hydrolase activity, being able to
CC catalyze the hydrolysis of choloyl-CoA, 3-dehydrocholoyl-CoA, and
CC chenodeoxycholoyl-CoA, releasing CoA and the corresponding free bile
CC acid (PubMed:9869646). However, this latter activity may not represent
CC the actual activity of this enzyme, since using a transferase rather
CC than hydrolase, the bacteria conserve the thioester bond energy, saving
CC ATP molecules (Probable). Shows no hydrolytic activity with acetyl-CoA,
CC isovaleryl-CoA, palmitoyl-CoA, or phenylacetyl-CoA as substrates
CC (PubMed:9869646). {ECO:0000269|PubMed:22021638,
CC ECO:0000269|PubMed:9869646, ECO:0000305|PubMed:22021638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholate + lithocholoyl-CoA = choloyl-CoA + lithocholate;
CC Xref=Rhea:RHEA:49432, ChEBI:CHEBI:29744, ChEBI:CHEBI:29747,
CC ChEBI:CHEBI:57373, ChEBI:CHEBI:87438; EC=2.8.3.25;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49433;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholate + deoxycholoyl-CoA = choloyl-CoA + deoxycholate;
CC Xref=Rhea:RHEA:49436, ChEBI:CHEBI:23614, ChEBI:CHEBI:29747,
CC ChEBI:CHEBI:57373, ChEBI:CHEBI:58810; EC=2.8.3.25;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49437;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allodeoxycholoyl-CoA + cholate = allodeoxycholate + choloyl-
CC CoA; Xref=Rhea:RHEA:53756, ChEBI:CHEBI:29747, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:137662, ChEBI:CHEBI:137664;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53757;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allocholate + deoxycholoyl-CoA = allocholoyl-CoA +
CC deoxycholate; Xref=Rhea:RHEA:53760, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:58810, ChEBI:CHEBI:137661, ChEBI:CHEBI:137663;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53761;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allocholate + lithocholoyl-CoA = allocholoyl-CoA +
CC lithocholate; Xref=Rhea:RHEA:53764, ChEBI:CHEBI:29744,
CC ChEBI:CHEBI:87438, ChEBI:CHEBI:137661, ChEBI:CHEBI:137663;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53765;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allocholate + allodeoxycholoyl-CoA = allocholoyl-CoA +
CC allodeoxycholate; Xref=Rhea:RHEA:53768, ChEBI:CHEBI:137661,
CC ChEBI:CHEBI:137662, ChEBI:CHEBI:137663, ChEBI:CHEBI:137664;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53769;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + lithocholoyl-CoA = chenodeoxycholoyl-CoA +
CC lithocholate; Xref=Rhea:RHEA:53772, ChEBI:CHEBI:29744,
CC ChEBI:CHEBI:36234, ChEBI:CHEBI:62989, ChEBI:CHEBI:87438;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53773;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=deoxycholoyl-CoA + ursodeoxycholate = deoxycholate +
CC ursodeoxycholoyl-CoA; Xref=Rhea:RHEA:53796, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:58810, ChEBI:CHEBI:78604, ChEBI:CHEBI:137679;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53797;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lithocholoyl-CoA + ursodeoxycholate = lithocholate +
CC ursodeoxycholoyl-CoA; Xref=Rhea:RHEA:53800, ChEBI:CHEBI:29744,
CC ChEBI:CHEBI:78604, ChEBI:CHEBI:87438, ChEBI:CHEBI:137679;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53801;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allodeoxycholoyl-CoA + ursodeoxycholate = allodeoxycholate +
CC ursodeoxycholoyl-CoA; Xref=Rhea:RHEA:53804, ChEBI:CHEBI:78604,
CC ChEBI:CHEBI:137662, ChEBI:CHEBI:137664, ChEBI:CHEBI:137679;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53805;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-muricholate + lithocholoyl-CoA = beta-muricholoyl-CoA +
CC lithocholate; Xref=Rhea:RHEA:53780, ChEBI:CHEBI:29744,
CC ChEBI:CHEBI:87438, ChEBI:CHEBI:134119, ChEBI:CHEBI:137668;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53781;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-muricholate + deoxycholoyl-CoA = beta-muricholoyl-CoA +
CC deoxycholate; Xref=Rhea:RHEA:53784, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:58810, ChEBI:CHEBI:134119, ChEBI:CHEBI:137668;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53785;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allodeoxycholoyl-CoA + beta-muricholate = allodeoxycholate +
CC beta-muricholoyl-CoA; Xref=Rhea:RHEA:53788, ChEBI:CHEBI:134119,
CC ChEBI:CHEBI:137662, ChEBI:CHEBI:137664, ChEBI:CHEBI:137668;
CC Evidence={ECO:0000269|PubMed:22021638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53789;
CC Evidence={ECO:0000305|PubMed:22021638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = cholate + CoA + H(+);
CC Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373;
CC Evidence={ECO:0000269|PubMed:9869646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542;
CC Evidence={ECO:0000305|PubMed:9869646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+);
CC Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989;
CC Evidence={ECO:0000269|PubMed:9869646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512;
CC Evidence={ECO:0000305|PubMed:9869646};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=175 uM for choloyl-CoA (in the assay for hydrolysis of choloyl-
CC CoA) {ECO:0000269|PubMed:9869646};
CC Vmax=374 umol/min/mg enzyme for the hydrolysis of choloyl-CoA
CC {ECO:0000269|PubMed:9869646};
CC pH dependence:
CC Optimum pH is between pH 6.0 and 7.0 or the hydrolysis of choloyl-
CC CoA. No activity is detected below pH 4.0 or above pH 9.0.
CC {ECO:0000269|PubMed:9869646};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000305|PubMed:22021638}.
CC -!- INDUCTION: Induced by bile acids. {ECO:0000305|PubMed:2254270}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR EMBL; M22623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U57489; AAC45415.1; -; Genomic_DNA.
DR RefSeq; WP_025645819.1; NZ_CP080442.1.
DR AlphaFoldDB; P19413; -.
DR SMR; P19413; -.
DR SwissLipids; SLP:000001348; -.
DR KEGG; ag:AAC45415; -.
DR BioCyc; MetaCyc:BAIFEUBSP-MON; -.
DR BRENDA; 2.8.3.25; 1513.
DR SABIO-RK; P19413; -.
DR UniPathway; UPA00221; -.
DR GO; GO:0033881; F:bile-acid-CoA transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 1: Evidence at protein level;
KW Bile acid catabolism; Direct protein sequencing; Hydrolase;
KW Lipid degradation; Lipid metabolism; Steroid metabolism; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2448288"
FT CHAIN 2..426
FT /note="Bile acid CoA-transferase BaiF"
FT /id="PRO_0000194715"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P31572"
FT CONFLICT 33..34
FT /note="LL -> FW (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 47469 MW; 929C5D8DDB5C2003 CRC64;
MAGIKDFPKF GALAGLKILD SGSNIAGPLG GGLLAECGAT VIHFEGPKKP DNQRGWYGYP
QNHRNQLSMV ADIKSEEGRK IFLDLIKWAD IWVESSKGGQ YDRLGLSDEV IWEVNPKIAI
VHVSGYGQTG DPSYVTRASY DAVGQAFSGY MSLNGTTEAL KINPYLSDFV CGLTTCWAML
ACYVSTILTG KGESVDVAQY EALARIMDGR MIQYATDGVK MPRTGNKDAQ AALFSFYTCK
DGRTIFIGMT GAEVCKRGFP IIGLPVPGTG DPDFPEGFTG WMIYTPVGQR MEKAMEKYVS
EHTMEEVEAE MQAHQIPCQR VYELEDCLND PHWKARGTIT EWDDPMMGHI TGLGLINKFK
RNPSEIWRGA PLFGMDNRDI LKDLGYDDAK IDELYEQGIV NEFDLDTTIK RYRLDEVIPH
MRKKEE
