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Protein

Choloylglycine hydrolase

Gene

cbh

Organism
Clostridium perfringens (strain 13 / Type A)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21

GO - Molecular functioni

  1. choloylglycine hydrolase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciCPER195102:GJFM-752-MONOMER.
MetaCyc:MONOMER-15681.
SABIO-RKP54965.

Names & Taxonomyi

Protein namesi
Recommended name:
Choloylglycine hydrolase (EC:3.5.1.24)
Alternative name(s):
Bile salt hydrolase
Conjugated bile acid hydrolase
Short name:
CBAH
Gene namesi
Name:cbh
Ordered Locus Names:CPE0709
OrganismiClostridium perfringens (strain 13 / Type A)
Taxonomic identifieri195102 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000000818: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 329328Choloylglycine hydrolasePRO_0000073019Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi195102.CPE0709.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Beta strandi14 – 2411Combined sources
Beta strandi29 – 335Combined sources
Beta strandi38 – 403Combined sources
Turni42 – 443Combined sources
Beta strandi47 – 493Combined sources
Beta strandi54 – 618Combined sources
Beta strandi64 – 729Combined sources
Beta strandi77 – 826Combined sources
Turni84 – 863Combined sources
Beta strandi90 – 923Combined sources
Beta strandi97 – 1015Combined sources
Helixi102 – 1043Combined sources
Helixi105 – 1128Combined sources
Helixi116 – 1238Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi153 – 1586Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi175 – 1773Combined sources
Helixi179 – 1868Combined sources
Helixi187 – 1893Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi210 – 2123Combined sources
Helixi214 – 2163Combined sources
Helixi225 – 24319Combined sources
Helixi244 – 2463Combined sources
Helixi249 – 2579Combined sources
Turni263 – 2653Combined sources
Beta strandi275 – 2839Combined sources
Turni284 – 2874Combined sources
Beta strandi288 – 2958Combined sources
Beta strandi300 – 3034Combined sources
Helixi304 – 3063Combined sources
Beta strandi315 – 3184Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJFX-ray1.67A1-329[»]
2BJGX-ray2.10A/B1-329[»]
2RF8X-ray2.90A/B1-329[»]
2RG2X-ray1.80A2-329[»]
2RLCX-ray1.80A2-329[»]
ProteinModelPortaliP54965.
SMRiP54965. Positions 2-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54965.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C59 family.Curated

Phylogenomic databases

eggNOGiCOG3049.
HOGENOMiHOG000039938.
KOiK01442.
OMAiASFEFIP.
OrthoDBiEOG66QKTP.

Family and domain databases

Gene3Di3.60.60.10. 1 hit.
InterProiIPR029132. CBAH/NAAA_C.
IPR003199. Chologlycine_hydro/PeptC59.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCTGLALETK DGLHLFGRNM DIEYSFNQSI IFIPRNFKCV NKSNKKELTT
60 70 80 90 100
KYAVLGMGTI FDDYPTFADG MNEKGLGCAG LNFPVYVSYS KEDIEGKTNI
110 120 130 140 150
PVYNFLLWVL ANFSSVEEVK EALKNANIVD IPISENIPNT TLHWMISDIT
160 170 180 190 200
GKSIVVEQTK EKLNVFDNNI GVLTNSPTFD WHVANLNQYV GLRYNQVPEF
210 220 230 240 250
KLGDQSLTAL GQGTGLVGLP GDFTPASRFI RVAFLRDAMI KNDKDSIDLI
260 270 280 290 300
EFFHILNNVA MVRGSTRTVE EKSDLTQYTS CMCLEKGIYY YNTYENNQIN
310 320
AIDMNKENLD GNEIKTYKYN KTLSINHVN
Length:329
Mass (Da):37,185
Last modified:January 23, 2007 - v3
Checksum:iB0643160A27A368D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20191 Genomic DNA. Translation: AAC43454.1.
BA000016 Genomic DNA. Translation: BAB80415.1.
PIRiI40881.
RefSeqiNP_561625.1. NC_003366.1.
WP_003461725.1. NC_003366.1.

Genome annotation databases

EnsemblBacteriaiBAB80415; BAB80415; BAB80415.
GeneIDi988968.
KEGGicpe:CPE0709.
PATRICi19495345. VBICloPer59675_0771.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20191 Genomic DNA. Translation: AAC43454.1.
BA000016 Genomic DNA. Translation: BAB80415.1.
PIRiI40881.
RefSeqiNP_561625.1. NC_003366.1.
WP_003461725.1. NC_003366.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJFX-ray1.67A1-329[»]
2BJGX-ray2.10A/B1-329[»]
2RF8X-ray2.90A/B1-329[»]
2RG2X-ray1.80A2-329[»]
2RLCX-ray1.80A2-329[»]
ProteinModelPortaliP54965.
SMRiP54965. Positions 2-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi195102.CPE0709.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB80415; BAB80415; BAB80415.
GeneIDi988968.
KEGGicpe:CPE0709.
PATRICi19495345. VBICloPer59675_0771.

Phylogenomic databases

eggNOGiCOG3049.
HOGENOMiHOG000039938.
KOiK01442.
OMAiASFEFIP.
OrthoDBiEOG66QKTP.

Enzyme and pathway databases

BioCyciCPER195102:GJFM-752-MONOMER.
MetaCyc:MONOMER-15681.
SABIO-RKP54965.

Miscellaneous databases

EvolutionaryTraceiP54965.

Family and domain databases

Gene3Di3.60.60.10. 1 hit.
InterProiIPR029132. CBAH/NAAA_C.
IPR003199. Chologlycine_hydro/PeptC59.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCBH_CLOPE
AccessioniPrimary (citable) accession number: P54965
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.