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P54965

- CBH_CLOPE

UniProt

P54965 - CBH_CLOPE

Protein

Choloylglycine hydrolase

Gene

cbh

Organism
Clostridium perfringens (strain 13 / Type A)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

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

    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 – 86
    Beta strandi14 – 2411
    Beta strandi29 – 335
    Beta strandi38 – 403
    Turni42 – 443
    Beta strandi47 – 493
    Beta strandi54 – 618
    Beta strandi64 – 729
    Beta strandi77 – 826
    Turni84 – 863
    Beta strandi90 – 923
    Beta strandi97 – 1015
    Helixi102 – 1043
    Helixi105 – 1128
    Helixi116 – 1238
    Beta strandi126 – 1294
    Beta strandi142 – 1476
    Beta strandi153 – 1586
    Beta strandi163 – 1675
    Beta strandi170 – 1734
    Beta strandi175 – 1773
    Helixi179 – 1868
    Helixi187 – 1893
    Beta strandi199 – 2024
    Beta strandi205 – 2084
    Beta strandi210 – 2123
    Helixi214 – 2163
    Helixi225 – 24319
    Helixi244 – 2463
    Helixi249 – 2579
    Turni263 – 2653
    Beta strandi275 – 2839
    Turni284 – 2874
    Beta strandi288 – 2958
    Beta strandi300 – 3034
    Helixi304 – 3063
    Beta strandi315 – 3184

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MCTGLALETK DGLHLFGRNM DIEYSFNQSI IFIPRNFKCV NKSNKKELTT    50
    KYAVLGMGTI FDDYPTFADG MNEKGLGCAG LNFPVYVSYS KEDIEGKTNI 100
    PVYNFLLWVL ANFSSVEEVK EALKNANIVD IPISENIPNT TLHWMISDIT 150
    GKSIVVEQTK EKLNVFDNNI GVLTNSPTFD WHVANLNQYV GLRYNQVPEF 200
    KLGDQSLTAL GQGTGLVGLP GDFTPASRFI RVAFLRDAMI KNDKDSIDLI 250
    EFFHILNNVA MVRGSTRTVE EKSDLTQYTS CMCLEKGIYY YNTYENNQIN 300
    AIDMNKENLD GNEIKTYKYN KTLSINHVN 329
    Length:329
    Mass (Da):37,185
    Last modified:January 23, 2007 - v3
    Checksum:iB0643160A27A368D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20191 Genomic DNA. Translation: AAC43454.1 .
    BA000016 Genomic DNA. Translation: BAB80415.1 .
    PIRi I40881.
    RefSeqi NP_561625.1. NC_003366.1.
    WP_003461725.1. NC_003366.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BJF X-ray 1.67 A 1-329 [» ]
    2BJG X-ray 2.10 A/B 1-329 [» ]
    2RF8 X-ray 2.90 A/B 1-329 [» ]
    2RG2 X-ray 1.80 A 2-329 [» ]
    2RLC X-ray 1.80 A 2-329 [» ]
    ProteinModelPortali P54965.
    SMRi P54965. Positions 2-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 195102.CPE0709.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB80415 ; BAB80415 ; BAB80415 .
    GeneIDi 988968.
    KEGGi cpe:CPE0709.
    PATRICi 19495345. VBICloPer59675_0771.

    Phylogenomic databases

    eggNOGi COG3049.
    HOGENOMi HOG000039938.
    KOi K01442.
    OMAi ASFEFIP.
    OrthoDBi EOG66QKTP.

    Enzyme and pathway databases

    BioCyci CPER195102:GJFM-752-MONOMER.
    MetaCyc:MONOMER-15681.

    Miscellaneous databases

    EvolutionaryTracei P54965.

    Family and domain databases

    Gene3Di 3.60.60.10. 1 hit.
    InterProi IPR029132. CBAH/NAAA_C.
    IPR003199. Chologlycine_hydro/PeptC59.
    IPR029055. Ntn_hydrolases_N.
    [Graphical view ]
    Pfami PF02275. CBAH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 92 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