ID   CBH_CLOPE               Reviewed;         329 AA.
AC   P54965;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Conjugated bile acid hydrolase {ECO:0000303|PubMed:15823032, ECO:0000303|PubMed:7618863};
DE            Short=CBAH {ECO:0000303|PubMed:15823032, ECO:0000303|PubMed:7618863};
DE            EC=3.5.1.- {ECO:0000269|PubMed:15823032, ECO:0000269|PubMed:7618863};
DE   AltName: Full=Bile salt hydrolase {ECO:0000303|PubMed:15823032};
DE            Short=BSH {ECO:0000303|PubMed:15823032};
DE   AltName: Full=CBAH-1 {ECO:0000303|PubMed:7618863};
DE   AltName: Full=Choloylglycine hydrolase {ECO:0000305|PubMed:7618863};
DE            EC=3.5.1.24 {ECO:0000269|PubMed:7618863};
GN   Name=cbh; OrderedLocusNames=CPE0709;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC   STRAIN=13 / Type A;
RX   PubMed=7618863; DOI=10.1128/aem.61.7.2514-2520.1995;
RA   Coleman J.P., Hudson L.L.;
RT   "Cloning and characterization of a conjugated bile acid hydrolase gene from
RT   Clostridium perfringens.";
RL   Appl. Environ. Microbiol. 61:2514-2520(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [3] {ECO:0007744|PDB:2BJF, ECO:0007744|PDB:2BJG}
RP   PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF
RP   APOENZYME AND IN COMPLEX WITH REACTION PRODUCTS DEOXYCHOLATE AND TAURINE,
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND REACTION MECHANISM.
RX   PubMed=15823032; DOI=10.1021/bi0473206;
RA   Rossocha M., Schultz-Heienbrok R., von Moeller H., Coleman J.P.,
RA   Saenger W.;
RT   "Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase
RT   with specific recognition of its cholyl but not of its tauryl product.";
RL   Biochemistry 44:5739-5748(2005).
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 humans, releasing amino acid residues and deconjugated
CC       bile salts (bile acids). Can hydrolyze the amid bond in major human
CC       bile salts, such as glycocholate (GCA), taurocholate (TCA) and
CC       taurodeoxycholate (TDCA) (PubMed:7618863, PubMed:15823032). Shows a
CC       slight preference for taurine-conjugated bile acids as substrates
CC       (PubMed:7618863). {ECO:0000269|PubMed:15823032,
CC       ECO:0000269|PubMed:7618863}.
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:7618863};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19354;
CC         Evidence={ECO:0000305|PubMed:7618863};
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:7618863};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47110;
CC         Evidence={ECO:0000305|PubMed:7618863};
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:15823032};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47557;
CC         Evidence={ECO:0000305|PubMed:15823032};
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:0000250|UniProtKB:Q9KK62};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47553;
CC         Evidence={ECO:0000250|UniProtKB:Q9KK62};
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:0000250|UniProtKB:Q9KK62};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47114;
CC         Evidence={ECO:0000250|UniProtKB:Q9KK62};
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:0000250|UniProtKB:Q9KK62};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16310;
CC         Evidence={ECO:0000250|UniProtKB:Q9KK62};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:7618863};
CC   -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC       {ECO:0000305|PubMed:7618863}.
CC   -!- SUBUNIT: Homotetramer (PubMed:7618863, PubMed:15823032). The tetramer
CC       consists of a dimer of dimers (PubMed:15823032).
CC       {ECO:0000269|PubMed:15823032, ECO:0000269|PubMed:7618863}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene continue to express
CC       conjugated bile acid hydrolase activity at 86% of wild-type levels.
CC       {ECO:0000269|PubMed:7618863}.
CC   -!- SIMILARITY: Belongs to the peptidase C59 family. {ECO:0000305}.
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DR   EMBL; U20191; AAC43454.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB80415.1; -; Genomic_DNA.
DR   PIR; I40881; I40881.
DR   RefSeq; WP_003461725.1; NC_003366.1.
DR   PDB; 2BJF; X-ray; 1.67 A; A=1-329.
DR   PDB; 2BJG; X-ray; 2.10 A; A/B=1-329.
DR   PDB; 2RF8; X-ray; 2.90 A; A/B=1-329.
DR   PDB; 2RG2; X-ray; 1.80 A; A=2-329.
DR   PDB; 2RLC; X-ray; 1.80 A; A=2-329.
DR   PDBsum; 2BJF; -.
DR   PDBsum; 2BJG; -.
DR   PDBsum; 2RF8; -.
DR   PDBsum; 2RG2; -.
DR   PDBsum; 2RLC; -.
DR   AlphaFoldDB; P54965; -.
DR   SMR; P54965; -.
DR   STRING; 195102.gene:10489971; -.
DR   DrugBank; DB02659; Cholic Acid.
DR   DrugBank; DB03619; Deoxycholic acid.
DR   DrugBank; DB01956; Taurine.
DR   SwissLipids; SLP:000001734; -.
DR   MEROPS; C59.951; -.
DR   GeneID; 69448463; -.
DR   KEGG; cpe:CPE0709; -.
DR   HOGENOM; CLU_045206_1_0_9; -.
DR   BioCyc; MetaCyc:MONOMER-15681; -.
DR   BRENDA; 3.5.1.24; 1503.
DR   SABIO-RK; P54965; -.
DR   UniPathway; UPA00221; -.
DR   EvolutionaryTrace; P54965; -.
DR   Proteomes; UP000000818; 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   CDD; cd00542; Ntn_PVA; 1.
DR   InterPro; IPR047711; CBAH.
DR   InterPro; IPR029132; CBAH/NAAA_C.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   NCBIfam; NF038245; bile_salt_hydro; 1.
DR   PANTHER; PTHR35527; CHOLOYLGLYCINE HYDROLASE; 1.
DR   PANTHER; PTHR35527:SF2; HYDROLASE-RELATED; 1.
DR   Pfam; PF02275; CBAH; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Lipid metabolism;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15823032"
FT   CHAIN           2..329
FT                   /note="Conjugated bile acid hydrolase"
FT                   /id="PRO_0000073019"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:15823032"
FT   BINDING         2
FT                   /ligand="deoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:23614"
FT                   /evidence="ECO:0000269|PubMed:15823032,
FT                   ECO:0007744|PDB:2BJF"
FT   BINDING         18
FT                   /ligand="deoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:23614"
FT                   /evidence="ECO:0000269|PubMed:15823032,
FT                   ECO:0007744|PDB:2BJF"
FT   BINDING         82
FT                   /ligand="taurine"
FT                   /ligand_id="ChEBI:CHEBI:507393"
FT                   /evidence="ECO:0000269|PubMed:15823032,
FT                   ECO:0007744|PDB:2BJF"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          14..24
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          54..61
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          64..72
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          77..82
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:2RG2"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           105..112
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           116..123
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          142..147
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:2RG2"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           179..186
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:2RLC"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           225..243
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           249..257
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   TURN            263..265
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          275..283
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   TURN            284..287
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          288..295
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          300..303
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:2BJF"
FT   STRAND          315..318
FT                   /evidence="ECO:0007829|PDB:2BJF"
SQ   SEQUENCE   329 AA;  37185 MW;  B0643160A27A368D CRC64;
     MCTGLALETK DGLHLFGRNM DIEYSFNQSI IFIPRNFKCV NKSNKKELTT KYAVLGMGTI
     FDDYPTFADG MNEKGLGCAG LNFPVYVSYS KEDIEGKTNI PVYNFLLWVL ANFSSVEEVK
     EALKNANIVD IPISENIPNT TLHWMISDIT GKSIVVEQTK EKLNVFDNNI GVLTNSPTFD
     WHVANLNQYV GLRYNQVPEF KLGDQSLTAL GQGTGLVGLP GDFTPASRFI RVAFLRDAMI
     KNDKDSIDLI EFFHILNNVA MVRGSTRTVE EKSDLTQYTS CMCLEKGIYY YNTYENNQIN
     AIDMNKENLD GNEIKTYKYN KTLSINHVN
//