CBH_LACPL
ID CBH_LACPL Reviewed; 324 AA.
AC Q06115; F9UUJ8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Conjugated bile acid hydrolase {ECO:0000303|PubMed:1476424};
DE EC=3.5.1.- {ECO:0000269|PubMed:1476424};
DE AltName: Full=Bile salt hydrolase;
DE Short=BSH;
DE AltName: Full=Choloylglycine hydrolase {ECO:0000303|PubMed:1476424};
DE EC=3.5.1.24 {ECO:0000269|PubMed:1476424};
GN Name=cbh {ECO:0000303|PubMed:1476424}; Synonyms=bsh;
GN OrderedLocusNames=lp_3536;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 4229 / 80;
RX PubMed=1476424; DOI=10.1128/aem.58.12.3792-3798.1992;
RA Christiaens H., Leer R.J., Pouwels P.H., Verstraete W.;
RT "Cloning and expression of a conjugated bile acid hydrolase gene from
RT Lactobacillus plantarum by using a direct plate assay.";
RL Appl. Environ. Microbiol. 58:3792-3798(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
CC -!- FUNCTION: Bile salt hydrolase that catalyzes the deconjugation of
CC glycine- and taurine-linked bile salts, which occurs naturally in the
CC intestines of animals, releasing amino acid residues and deconjugated
CC bile salts (bile acids). Can hydrolyze the amid bond in the bile salts
CC glycocholate (GCA), glycodeoxycholate (GDCA), glycochenodeoxycholate
CC (GCDCA), taurocholate (TCA), taurodeoxycholate (TDCA) and
CC taurochenodeoxycholate (TCDCA). Shows a preference for glycine-
CC conjugated bile acids as substrates. {ECO:0000269|PubMed:1476424}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycocholate + H2O = cholate + glycine; Xref=Rhea:RHEA:19353,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29746, ChEBI:CHEBI:29747,
CC ChEBI:CHEBI:57305; EC=3.5.1.24;
CC Evidence={ECO:0000269|PubMed:1476424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19354;
CC Evidence={ECO:0000305|PubMed:1476424};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycodeoxycholate + H2O = deoxycholate + glycine;
CC Xref=Rhea:RHEA:47552, ChEBI:CHEBI:15377, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:82982;
CC Evidence={ECO:0000269|PubMed:1476424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47553;
CC Evidence={ECO:0000305|PubMed:1476424};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + glycine = glycochenodeoxycholate + H2O;
CC Xref=Rhea:RHEA:47112, ChEBI:CHEBI:15377, ChEBI:CHEBI:36234,
CC ChEBI:CHEBI:36252, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000269|PubMed:1476424};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47114;
CC Evidence={ECO:0000305|PubMed:1476424};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholate + taurine = H2O + taurocholate; Xref=Rhea:RHEA:47108,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29747, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:1476424};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47110;
CC Evidence={ECO:0000305|PubMed:1476424};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + taurodeoxycholate = deoxycholate + taurine;
CC Xref=Rhea:RHEA:47556, ChEBI:CHEBI:15377, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:36261, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:1476424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47557;
CC Evidence={ECO:0000305|PubMed:1476424};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + taurochenodeoxycholate = chenodeoxycholate + taurine;
CC Xref=Rhea:RHEA:16309, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36234, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:1476424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16310;
CC Evidence={ECO:0000305|PubMed:1476424};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for glycodeoxycholate {ECO:0000269|PubMed:1476424};
CC Vmax=1.56 umol/min/mg enzyme with glycodeoxycholate as substrate
CC {ECO:0000269|PubMed:1476424};
CC pH dependence:
CC Optimum pH is 4.7-5.5. {ECO:0000269|PubMed:1476424};
CC Temperature dependence:
CC Optimum temperature is 30-45 degrees Celsius.
CC {ECO:0000269|PubMed:1476424};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000305|PubMed:1476424}.
CC -!- SUBUNIT: Homotetramer. The tetramer consists of a dimer of dimers.
CC {ECO:0000250|UniProtKB:P54965}.
CC -!- SIMILARITY: Belongs to the peptidase C59 family. {ECO:0000305}.
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DR EMBL; S51638; AAB24746.1; -; Genomic_DNA.
DR EMBL; M96175; AAA25233.1; -; Genomic_DNA.
DR EMBL; AL935263; CCC80500.1; -; Genomic_DNA.
DR PIR; A48953; A48953.
DR RefSeq; WP_011102211.1; NC_004567.2.
DR RefSeq; YP_004891014.1; NC_004567.2.
DR AlphaFoldDB; Q06115; -.
DR SMR; Q06115; -.
DR STRING; 220668.lp_3536; -.
DR MEROPS; C59.951; -.
DR PRIDE; Q06115; -.
DR EnsemblBacteria; CCC80500; CCC80500; lp_3536.
DR KEGG; lpl:lp_3536; -.
DR PATRIC; fig|220668.9.peg.2947; -.
DR eggNOG; COG3049; Bacteria.
DR HOGENOM; CLU_045206_1_1_9; -.
DR OMA; HYAIIGI; -.
DR PhylomeDB; Q06115; -.
DR BioCyc; LPLA220668:G1GW0-2988-MON; -.
DR BRENDA; 3.5.1.24; 2849.
DR UniPathway; UPA00221; -.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0047742; F:chenodeoxycholoyltaurine hydrolase activity; IEA:RHEA.
DR GO; GO:0045302; F:choloylglycine hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR029132; CBAH/NAAA_C.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR Pfam; PF02275; CBAH; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid metabolism; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..324
FT /note="Conjugated bile acid hydrolase"
FT /id="PRO_0000073020"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54965"
FT BINDING 2
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:P54965"
FT BINDING 16
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:P54965"
FT BINDING 79
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000250|UniProtKB:P54965"
FT CONFLICT 236
FT /note="S -> P (in Ref. 1; AAB24746/AAA25233)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="S -> N (in Ref. 1; AAB24746/AAA25233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 37042 MW; B5E53F74AD742347 CRC64;
MCTAITYQSY NNYFGRNFDY EISYNEMVTI TPRKYPLVFR KVENLDHHYA IIGITADVES
YPLYYDAMNE KGLCIAGLNF AGYADYKKYD ADKVNITPFE LIPWLLGQFS SVREVKKNIQ
KLNLVNINFS EQLPLSPLHW LVADKQESIV IESVKEGLKI YDNPVGVLTN NPNFDYQLFN
LNNYRALSNS TPQNSFSEKV DLDSYSRGMG GLGLPGDLSS MSRFVRAAFT KLNSLSMQTE
SGSVSQFFHI LGSVEQQKGL CEVTDGKYEY TIYSSCCDMD KGVYYYRTYD NSQINSVSLN
HEHLDTTELI SYPLRSEAQY YAVN
