BAIK_CLOSV
ID BAIK_CLOSV Reviewed; 437 AA.
AC B4YST4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Bile acid CoA-transferase BaiK {ECO:0000305|PubMed:22021638};
DE EC=2.8.3.25 {ECO:0000269|PubMed:22021638};
GN Name=baiK {ECO:0000303|PubMed:22021638, ECO:0000312|EMBL:ACF20979.1};
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].
RC STRAIN=JCM 10418 /VPI 12708;
RA Ridlon J.M., Kang D., Hylemon P.B.;
RT "Identification and characterization of novel genes involved in bile acid
RT metabolism in intestinal Clostridia.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 deoxycholoyl-CoA and allodeoxycholoyl-CoA as bile acid CoA donors and
CC cholate, allocholate and ursodeoxycholate as bile acid CoA acceptors.
CC Shows no activity when lithocholoyl-CoA is used as the CoA donor.
CC {ECO:0000269|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 + 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=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=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 -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000305|PubMed:22021638}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR EMBL; EU675330; ACF20979.1; -; Genomic_DNA.
DR AlphaFoldDB; B4YST4; -.
DR SMR; B4YST4; -.
DR SwissLipids; SLP:000001733; -.
DR KEGG; ag:ACF20979; -.
DR BioCyc; MetaCyc:MON-18545; -.
DR UniPathway; UPA00221; -.
DR GO; GO:0033881; F:bile-acid-CoA transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Transferase.
FT CHAIN 1..437
FT /note="Bile acid CoA-transferase BaiK"
FT /id="PRO_0000451589"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P31572"
SQ SEQUENCE 437 AA; 49137 MW; 507F258871335350 CRC64;
MKGTGLNNFP QFGVMEGVKI LVCGGAIAGP FGATLLGEIG AEVVHFESPK NPDSVRGHYG
YSQNHRNQLS MVADMKTPEG LEIFKKLIKW TDIFIESSKG GTYEKMGLTD EVLWEINPRL
AIVHVSGFGQ TGVPEYIDRA SYDAVGQAFS GYMSFNGTPK EAMKVSPYLS DYVTALNTCW
TALAAYVHVL RTGKGESVDV AQYESLARIL DTRPMEYFTD GKEFPRTGNK DTQAALFSFY
TCKDGGEIFI GMNGYGPVRR GYPLIGLPKP GDGDPEIDEI LSGWMADTDL GRRLEAAMEK
FVSEHTVDEV EKIMLENQIP CLKVYTLKDC AKDPHWKARD IFVEWDDPMM GRVKGLGIIN
KWKNNPGEIK WGAPLFGENN EEVLKDLGYT EEEIEDFAKR GITASFDFDQ TYEIYKLEEL
FPHYREGFTE RWKKEEE
