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P54965 (CBH_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Choloylglycine hydrolase
EC=3.5.1.24
Alternative name(s):
Bile salt hydrolase
Conjugated bile acid hydrolase
Short name=CBAH
Gene names
Name:cbh
Ordered Locus Names:CPE0709
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The enzyme catalyzes the degradation of conjugated bile acids in the mammalian gut.

Catalytic activity

3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholan-24-oylglycine + H2O = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + glycine.

Subunit structure

Homotetramer. Ref.3

Sequence similarities

Belongs to the peptidase C59 family.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functioncholoylglycine hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 329328Choloylglycine hydrolase
PRO_0000073019

Sites

Active site21

Secondary structure

1 .................................................................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54965 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B0643160A27A368D

FASTA32937,185
        10         20         30         40         50         60 
MCTGLALETK DGLHLFGRNM DIEYSFNQSI IFIPRNFKCV NKSNKKELTT KYAVLGMGTI 

        70         80         90        100        110        120 
FDDYPTFADG MNEKGLGCAG LNFPVYVSYS KEDIEGKTNI PVYNFLLWVL ANFSSVEEVK 

       130        140        150        160        170        180 
EALKNANIVD IPISENIPNT TLHWMISDIT GKSIVVEQTK EKLNVFDNNI GVLTNSPTFD 

       190        200        210        220        230        240 
WHVANLNQYV GLRYNQVPEF KLGDQSLTAL GQGTGLVGLP GDFTPASRFI RVAFLRDAMI 

       250        260        270        280        290        300 
KNDKDSIDLI EFFHILNNVA MVRGSTRTVE EKSDLTQYTS CMCLEKGIYY YNTYENNQIN 

       310        320 
AIDMNKENLD GNEIKTYKYN KTLSINHVN

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens."
Coleman J.P., Hudson L.L.
Appl. Environ. Microbiol. 61:2514-2520(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 13 / Type A.
[2]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.
[3]"Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product."
Rossocha M., Schultz-Heienbrok R., von Moeller H., Coleman J.P., Saenger W.
Biochemistry 44:5739-5748(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT, PROTEIN SEQUENCE OF N-TERMINUS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U20191 Genomic DNA. Translation: AAC43454.1.
BA000016 Genomic DNA. Translation: BAB80415.1.
PIRI40881.
RefSeqNP_561625.1. NC_003366.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJFX-ray1.67A1-329[»]
2BJGX-ray2.10A/B1-329[»]
2RF8X-ray2.90A/B3-329[»]
2RG2X-ray1.80A2-329[»]
2RLCX-ray1.80A2-329[»]
ProteinModelPortalP54965.
SMRP54965. Positions 2-329.
ModBaseSearch...

Protein-protein interaction databases

STRING195102.CPE0709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB80415; BAB80415; BAB80415.
GeneID988968.
KEGGcpe:CPE0709.
PATRIC19495345. VBICloPer59675_0771.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3049.
HOGENOMHOG000039938.
KOK01442.
OMAASFEFIP.
ProtClustDBCLSK518734.

Enzyme and pathway databases

BioCycCPER195102:GJFM-752-MONOMER.
MetaCyc:MONOMER-15681.

Family and domain databases

Gene3D3.60.60.10. 1 hit.
InterProIPR003199. Chologlycine_hydro.
[Graphical view]
PfamPF02275. CBAH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54965.

Entry information

Entry nameCBH_CLOPE
AccessionPrimary (citable) accession number: P54965
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 82 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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