NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046810818|gb|ANW09917|]
View 

bile salt hydrolase, partial [Lactiplantibacillus plantarum]

Protein Classification

choloylglycine hydrolase family protein( domain architecture ID 10087987)

choloylglycine hydrolase family protein, one of a family of linear amide C-N hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides; this family includes conjugated bile acid hydrolase (CBAH) and penicillin acylase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
1-270 6.02e-132

Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.


:

Pssm-ID: 238303  Cd Length: 303  Bit Score: 375.79  E-value: 6.02e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNV 79
Cdd:cd00542    33 PRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYpLLFDGVNEKGLAIAGLYFPGYASYSKETKEGKTNIAPFEFITWVLGNF 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  80 KSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQ 159
Cdd:cd00542   113 ASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKGGLKVYDNPVGVLTNSPDFDWHLTNLRNYINLS 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 160 PGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTP 239
Cdd:cd00542   193 PEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQPKDEEEAVNNAFHILNSVDIPKGAVITENGSS 272
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1046810818 240 DYTQYRAYMSMNEPAFYMQPYADQTITRVEL 270
Cdd:cd00542   273 DYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
 
Name Accession Description Interval E-value
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
1-270 6.02e-132

Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.


Pssm-ID: 238303  Cd Length: 303  Bit Score: 375.79  E-value: 6.02e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNV 79
Cdd:cd00542    33 PRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYpLLFDGVNEKGLAIAGLYFPGYASYSKETKEGKTNIAPFEFITWVLGNF 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  80 KSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQ 159
Cdd:cd00542   113 ASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKGGLKVYDNPVGVLTNSPDFDWHLTNLRNYINLS 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 160 PGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTP 239
Cdd:cd00542   193 PEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQPKDEEEAVNNAFHILNSVDIPKGAVITENGSS 272
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1046810818 240 DYTQYRAYMSMNEPAFYMQPYADQTITRVEL 270
Cdd:cd00542   273 DYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-280 1.11e-105

Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 442283  Cd Length: 337  Bit Score: 310.27  E-value: 1.11e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADG--FDSPYSFVGTGRDLNGYIFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGN 78
Cdd:COG3049    36 PRGYERDGEVGPNSlkWTSKYGSVGMGAYDGYPLTADGMNEKGLAAALLYFPGYADYPKRDKEGKPNLAPSEFVQWVLDN 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  79 VKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNL 158
Cdd:COG3049   116 FATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATGDSAVIEYIDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 159 QPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGT 238
Cdd:COG3049   196 SPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNALPKPADEEEAVASVFHILRNVSIPKGIVRPDEPN 275
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1046810818 239 PDYTQYRAYMSMNEPAFYMQPYADQTITRVELTPALMTAAQP 280
Cdd:COG3049   276 ISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSKGAE 317
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-270 4.86e-74

choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables commensal or pathogenic bacteria in the digestive tract to escape the antimicrobial activity of bile acids, which are cholesterol derivatives conjugated to glycine or taurine.


Pssm-ID: 468428  Cd Length: 314  Bit Score: 228.94  E-value: 4.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGfDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNV 79
Cdd:NF038245   33 PRNYPFKFRKEADL-KTHYAIIGMATVVDNYpLYFDAMNEKGLGMAGLNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQC 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  80 KSTAELGERIADLNvmeaaapLLNI-------VVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNL 152
Cdd:NF038245  112 ETVDEVKEALKNIN-------LVNIpfseqlpLSPLHWIIADKTGSSIVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 153 SNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVK 232
Cdd:NF038245  185 NNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSGDSEEENVSQFFHILGSVEQQKGCC 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1046810818 233 MQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 270
Cdd:NF038245  265 EVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDM 302
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
1-270 4.78e-72

Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.


Pssm-ID: 396726  Cd Length: 316  Bit Score: 223.93  E-value: 4.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNV 79
Cdd:pfam02275  33 PRNYKLVFEKLGNMLVTKYAVIGMGTDVGSYpLFYDGLNEKGLGIAGLYFPGYAFYSKGPKKDKVNIQPGELILWVLGNF 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  80 KSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQ 159
Cdd:pfam02275 113 TSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDASGESIVIEPRKEGLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLR 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 160 PGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTP 239
Cdd:pfam02275 193 PNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPKAKTETESVATFFHILSNVAIPKGAVLNIEGKL 272
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1046810818 240 DYTQYRAYMSMNEPAFYMQPYADQTITRVEL 270
Cdd:pfam02275 273 EYTVYTSCMDLTKGNYYFETYDNSQINAVNL 303
 
Name Accession Description Interval E-value
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
1-270 6.02e-132

Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.


Pssm-ID: 238303  Cd Length: 303  Bit Score: 375.79  E-value: 6.02e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNV 79
Cdd:cd00542    33 PRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYpLLFDGVNEKGLAIAGLYFPGYASYSKETKEGKTNIAPFEFITWVLGNF 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  80 KSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQ 159
Cdd:cd00542   113 ASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKGGLKVYDNPVGVLTNSPDFDWHLTNLRNYINLS 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 160 PGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTP 239
Cdd:cd00542   193 PEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQPKDEEEAVNNAFHILNSVDIPKGAVITENGSS 272
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1046810818 240 DYTQYRAYMSMNEPAFYMQPYADQTITRVEL 270
Cdd:cd00542   273 DYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-280 1.11e-105

Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 442283  Cd Length: 337  Bit Score: 310.27  E-value: 1.11e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADG--FDSPYSFVGTGRDLNGYIFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGN 78
Cdd:COG3049    36 PRGYERDGEVGPNSlkWTSKYGSVGMGAYDGYPLTADGMNEKGLAAALLYFPGYADYPKRDKEGKPNLAPSEFVQWVLDN 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  79 VKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNL 158
Cdd:COG3049   116 FATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATGDSAVIEYIDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 159 QPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGT 238
Cdd:COG3049   196 SPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNALPKPADEEEAVASVFHILRNVSIPKGIVRPDEPN 275
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1046810818 239 PDYTQYRAYMSMNEPAFYMQPYADQTITRVELTPALMTAAQP 280
Cdd:COG3049   276 ISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSKGAE 317
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-270 4.86e-74

choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables commensal or pathogenic bacteria in the digestive tract to escape the antimicrobial activity of bile acids, which are cholesterol derivatives conjugated to glycine or taurine.


Pssm-ID: 468428  Cd Length: 314  Bit Score: 228.94  E-value: 4.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGfDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNV 79
Cdd:NF038245   33 PRNYPFKFRKEADL-KTHYAIIGMATVVDNYpLYFDAMNEKGLGMAGLNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQC 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  80 KSTAELGERIADLNvmeaaapLLNI-------VVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNL 152
Cdd:NF038245  112 ETVDEVKEALKNIN-------LVNIpfseqlpLSPLHWIIADKTGSSIVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 153 SNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVK 232
Cdd:NF038245  185 NNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSGDSEEENVSQFFHILGSVEQQKGCC 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1046810818 233 MQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 270
Cdd:NF038245  265 EVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDM 302
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
1-270 4.78e-72

Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.


Pssm-ID: 396726  Cd Length: 316  Bit Score: 223.93  E-value: 4.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNV 79
Cdd:pfam02275  33 PRNYKLVFEKLGNMLVTKYAVIGMGTDVGSYpLFYDGLNEKGLGIAGLYFPGYAFYSKGPKKDKVNIQPGELILWVLGNF 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  80 KSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQ 159
Cdd:pfam02275 113 TSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDASGESIVIEPRKEGLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLR 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 160 PGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTP 239
Cdd:pfam02275 193 PNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPKAKTETESVATFFHILSNVAIPKGAVLNIEGKL 272
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1046810818 240 DYTQYRAYMSMNEPAFYMQPYADQTITRVEL 270
Cdd:pfam02275 273 EYTVYTSCMDLTKGNYYFETYDNSQINAVNL 303
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
1-249 8.52e-51

Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.


Pssm-ID: 238910  Cd Length: 229  Bit Score: 166.76  E-value: 8.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818   1 PRNHHFDSVTNADGfDSPYSFVGTGRDLNGYIFVDGVNEHGVSAAALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVK 80
Cdd:cd01935    33 PRGYQRNGQTGDKS-KWYAKYGSGGTSAGYIGLVDGMNEKGLSVSLLYFPGYAYYPAGIKEGKDGLPAFELIRWVLENCD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  81 STAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDGVHYMKNP-VGVMTNTPDFEWHLknlsnyvnlq 159
Cdd:cd01935   112 SVEEVKEALKKIPIVDFPIPLGGPAAPLHYILSDKSGDSAVIEPIDGGLKIYDNPwFGVMTNHPTFDWHL---------- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 160 pgphpsrqygdmtvnpfgpgtgalgmpgdytsVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVkmqdngtp 239
Cdd:cd01935   182 --------------------------------PRRFVRVAYLKNTAQKNKETVEDVKNLFHILESVPIPNGL-------- 221
                         250
                  ....*....|
gi 1046810818 240 dyTQYRAYMS 249
Cdd:cd01935   222 --TVYTTVMD 229
Ntn_CGH cd01902
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
30-247 5.38e-15

Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile. CGH is present in a number of probiotic microbial organisms that inhabit the gut. CGH has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which CGH belongs.


Pssm-ID: 238885  Cd Length: 291  Bit Score: 73.14  E-value: 5.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818  30 GYIFVDGVNEHGVSAAALYFSGqAHFTQQTKaGKVNLApheVLMW---ILGNVKSTAELGERIADLN-VMEAAAPLLNIV 105
Cdd:cd01902    63 DIGTVDGMNEKGLVANLLYLTE-SDYGPADP-NKPTLS---AGAWgqyLLDNYATVEEAVKALAKEPfVIVASVPGDGRE 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046810818 106 VPLHWIISDKSGSTYVLELENDG--VHYMKNpVGVMTNTPDFEWHLKNLSNYVNLQpgphpsrqygdmtvnpfgPGTGAL 183
Cdd:cd01902   138 ATLHLSISDATGDSAIIEYIDGKlvIHHGKQ-YQVMTNSPTYDQQLALNKYWKQEK------------------DIGGTT 198
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046810818 184 GMPGDYTSVARFVRMVFMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAY 247
Cdd:cd01902   199 GLPGNNNPADRFVRASYYISALPKTADEREAVASVLSVIRNVSVPFGIPTPAPPNISDTRWRTV 262
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH