CBH_CLOPE
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 03-AUG-2022, entry version 127.
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; Firmicutes; 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 EnsemblBacteria; BAB80415; BAB80415; BAB80415.
DR GeneID; 29572173; -.
DR KEGG; cpe:CPE0709; -.
DR HOGENOM; CLU_045206_1_0_9; -.
DR OMA; HYAIIGI; -.
DR BioCyc; MetaCyc:MON-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 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 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
