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Conserved domains on  [gi|1377671652|gb|AVZ46808|]
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bile salt hydrolase, partial [Lactiplantibacillus plantarum]

Protein Classification

choloylglycine hydrolase family protein( domain architecture ID 17609175)

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

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List of domain hits

Name Accession Description Interval E-value
bile_salt_hydro super family cl41894
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-267 0e+00

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.


The actual alignment was detected with superfamily member NF038245:

Pssm-ID: 468428  Cd Length: 314  Bit Score: 503.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   1 NLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKL 79
Cdd:NF038245   45 DLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAGLNFPGNAYYAEEVEgGKDNVAPFEFIPWILGQCETVDEVKEALKNI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  80 NLVNINFSEQLPLSPLHWLVADKQE-SIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVD 158
Cdd:NF038245  125 NLVNIPFSEQLPLSPLHWIIADKTGsSIVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 159 LDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDK 238
Cdd:NF038245  205 LTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDK 284
                         250       260
                  ....*....|....*....|....*....
gi 1377671652 239 GVYYYRTYDNSQINSVNLNHEHLDTTELI 267
Cdd:NF038245  285 GIYYYKTYENSQINAVDMHKEDLDGSELI 313
 
Name Accession Description Interval E-value
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-267 0e+00

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: 503.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   1 NLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKL 79
Cdd:NF038245   45 DLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAGLNFPGNAYYAEEVEgGKDNVAPFEFIPWILGQCETVDEVKEALKNI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  80 NLVNINFSEQLPLSPLHWLVADKQE-SIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVD 158
Cdd:NF038245  125 NLVNIPFSEQLPLSPLHWIIADKTGsSIVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 159 LDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDK 238
Cdd:NF038245  205 LTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDK 284
                         250       260
                  ....*....|....*....|....*....
gi 1377671652 239 GVYYYRTYDNSQINSVNLNHEHLDTTELI 267
Cdd:NF038245  285 GIYYYKTYENSQINAVDMHKEDLDGSELI 313
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
1-256 9.65e-135

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: 382.33  E-value: 9.65e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   1 NLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKL 79
Cdd:cd00542    46 SYTTKYAFIGMGAVGDDYPLLFDGVNEKGLAIAGLYFPGYASYSKETKeGKTNIAPFEFITWVLGNFASVEEVKEALKNI 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  80 NLVNINFSEQLPLSPLHWLVADKQ-ESIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVD 158
Cdd:cd00542   126 NVVDDPINLLGPVPPLHWIISDKSgRSIVVEPTKGGLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVN 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 159 LDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDK 238
Cdd:cd00542   206 LTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQPKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLET 285
                         250
                  ....*....|....*...
gi 1377671652 239 GVYYYRTYDNSQINSVNL 256
Cdd:cd00542   286 GTYYYKTYDNNQIRAVDL 303
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-267 9.00e-129

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: 367.61  E-value: 9.00e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   2 LDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKY-DADKVNITPFELIPWLLGQFSSVREVKKNIQKLN 80
Cdd:pfam02275  47 LVTKYAVIGMGTDVGSYPLFYDGLNEKGLGIAGLYFPGYAFYSKGpKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLN 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  81 LVNINFSEQLPLSPLHWLVADK-QESIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDL 159
Cdd:pfam02275 127 IVNEALDILGGKAPLHWIISDAsGESIVIEPRKEGLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 160 DSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKG 239
Cdd:pfam02275 207 TPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPKAKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKG 286
                         250       260
                  ....*....|....*....|....*...
gi 1377671652 240 VYYYRTYDNSQINSVNLNHEHLDTTELI 267
Cdd:pfam02275 287 NYYFETYDNSQINAVNLDHENLDCTELV 314
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
5-262 4.70e-122

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: 351.49  E-value: 4.70e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   5 HYAIIGITAdVESYPLYYDAMNEKGLCIAGLNFAGYADYKKYD-ADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVN 83
Cdd:COG3049    55 KYGSVGMGA-YDGYPLTADGMNEKGLAAALLYFPGYADYPKRDkEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  84 INFSEQLPLSPLHWLVADKQ-ESIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSY 162
Cdd:COG3049   134 DPVPGLGRVAPLHLSISDATgDSAVIEYIDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPF 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 163 SRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYY 242
Cdd:COG3049   214 GQGSGTLGLPGDYTSPSRFVRAAFLKNALPKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYY 293
                         250       260
                  ....*....|....*....|
gi 1377671652 243 YRTYDNSQINSVNLNHEHLD 262
Cdd:COG3049   294 FETYDNPNIFWVDLKKLDFS 313
 
Name Accession Description Interval E-value
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-267 0e+00

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: 503.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   1 NLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKL 79
Cdd:NF038245   45 DLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAGLNFPGNAYYAEEVEgGKDNVAPFEFIPWILGQCETVDEVKEALKNI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  80 NLVNINFSEQLPLSPLHWLVADKQE-SIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVD 158
Cdd:NF038245  125 NLVNIPFSEQLPLSPLHWIIADKTGsSIVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 159 LDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDK 238
Cdd:NF038245  205 LTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDK 284
                         250       260
                  ....*....|....*....|....*....
gi 1377671652 239 GVYYYRTYDNSQINSVNLNHEHLDTTELI 267
Cdd:NF038245  285 GIYYYKTYENSQINAVDMHKEDLDGSELI 313
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
1-256 9.65e-135

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: 382.33  E-value: 9.65e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   1 NLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKL 79
Cdd:cd00542    46 SYTTKYAFIGMGAVGDDYPLLFDGVNEKGLAIAGLYFPGYASYSKETKeGKTNIAPFEFITWVLGNFASVEEVKEALKNI 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  80 NLVNINFSEQLPLSPLHWLVADKQ-ESIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVD 158
Cdd:cd00542   126 NVVDDPINLLGPVPPLHWIISDKSgRSIVVEPTKGGLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVN 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 159 LDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDK 238
Cdd:cd00542   206 LTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQPKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLET 285
                         250
                  ....*....|....*...
gi 1377671652 239 GVYYYRTYDNSQINSVNL 256
Cdd:cd00542   286 GTYYYKTYDNNQIRAVDL 303
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-267 9.00e-129

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: 367.61  E-value: 9.00e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   2 LDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKY-DADKVNITPFELIPWLLGQFSSVREVKKNIQKLN 80
Cdd:pfam02275  47 LVTKYAVIGMGTDVGSYPLFYDGLNEKGLGIAGLYFPGYAFYSKGpKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLN 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  81 LVNINFSEQLPLSPLHWLVADK-QESIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDL 159
Cdd:pfam02275 127 IVNEALDILGGKAPLHWIISDAsGESIVIEPRKEGLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 160 DSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKG 239
Cdd:pfam02275 207 TPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPKAKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKG 286
                         250       260
                  ....*....|....*....|....*...
gi 1377671652 240 VYYYRTYDNSQINSVNLNHEHLDTTELI 267
Cdd:pfam02275 287 NYYFETYDNSQINAVNLDHENLDCTELV 314
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
5-262 4.70e-122

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: 351.49  E-value: 4.70e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   5 HYAIIGITAdVESYPLYYDAMNEKGLCIAGLNFAGYADYKKYD-ADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVN 83
Cdd:COG3049    55 KYGSVGMGA-YDGYPLTADGMNEKGLAAALLYFPGYADYPKRDkEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  84 INFSEQLPLSPLHWLVADKQ-ESIVIESVKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSY 162
Cdd:COG3049   134 DPVPGLGRVAPLHLSISDATgDSAVIEYIDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPF 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 163 SRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYY 242
Cdd:COG3049   214 GQGSGTLGLPGDYTSPSRFVRAAFLKNALPKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYY 293
                         250       260
                  ....*....|....*....|
gi 1377671652 243 YRTYDNSQINSVNLNHEHLD 262
Cdd:COG3049   294 FETYDNPNIFWVDLKKLDFS 313
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
1-221 2.66e-50

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: 164.84  E-value: 2.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   1 NLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLNFAGYADYKKY-DADKVNITPFELIPWLLGQFSSVREVKKNIQKL 79
Cdd:cd01935    44 DKSKWYAKYGSGGTSAGYIGLVDGMNEKGLSVSLLYFPGYAYYPAGiKEGKDGLPAFELIRWVLENCDSVEEVKEALKKI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  80 NLVNINFSEQLPLSPLHWLVADKQ-ESIVIESVKEGLKIYDNP-VGVLTNNPNFDYQLfnlnnyralsnstpqnsfsekv 157
Cdd:cd01935   124 PIVDFPIPLGGPAAPLHYILSDKSgDSAVIEPIDGGLKIYDNPwFGVMTNHPTFDWHL---------------------- 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1377671652 158 dldsysrgmgglglpgdlssMSRFVRAAFTKLNSLPMQTESGSVSQFFHILGSVEQQKGLCEVT 221
Cdd:cd01935   182 --------------------PRRFVRVAYLKNTAQKNKETVEDVKNLFHILESVPIPNGLTVYT 225
Ntn_CGH cd01902
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
6-266 1.68e-18

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: 82.77  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652   6 YAIIGITAdvesyplYY----DAMNEKGLcIAGLNFAGYADYKKYDADKVNITPFELIPWLLGQFSSVREVKKNIQKLNL 81
Cdd:cd01902    54 YGSVVASM-------YDigtvDGMNEKGL-VANLLYLTESDYGPADPNKPTLSAGAWGQYLLDNYATVEEAVKALAKEPF 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652  82 VNINFSEQLPLSP-LHWLVADKQ-ESIVIESVKEGLKIYDNP-VGVLTNNPNFDYQLFNLNNYRALSNSTpqnsfsekvd 158
Cdd:cd01902   126 VIVASVPGDGREAtLHLSISDATgDSAIIEYIDGKLVIHHGKqYQVMTNSPTYDQQLALNKYWKQEKDIG---------- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377671652 159 ldsysrgmGGLGLPGDLSSMSRFVRAAFTkLNSLP-MQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMD 237
Cdd:cd01902   196 --------GTTGLPGNNNPADRFVRASYY-ISALPkTADEREAVASVLSVIRNVSVPFGIPTPAPPNISDTRWRTVADHK 266
                         250       260
                  ....*....|....*....|....*....
gi 1377671652 238 KGVYYYrtydnsqINSVNLNHEHLDTTEL 266
Cdd:cd01902   267 MKRYFF-------ESTLTPNLFWVDLKKL 288
 
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.
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