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Conserved domains on  [gi|489739426|ref|WP_003643511|]
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MULTISPECIES: choloylglycine hydrolase family protein [Lactiplantibacillus]

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

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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), ...
2-303 2.09e-152

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: 429.71  E-value: 2.09e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   2 CTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAAL 80
Cdd:cd00542    1 CTSLTLSTKDGDHVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYpLLFDGVNEKGLAIAGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  81 YFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELEND 160
Cdd:cd00542   81 YFPGYASYSKETKEGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 161 GVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTVFMREHTDA 240
Cdd:cd00542  161 GLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489739426 241 VTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 303
Cdd:cd00542  241 PKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
 
Name Accession Description Interval E-value
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
2-303 2.09e-152

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: 429.71  E-value: 2.09e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   2 CTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAAL 80
Cdd:cd00542    1 CTSLTLSTKDGDHVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYpLLFDGVNEKGLAIAGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  81 YFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELEND 160
Cdd:cd00542   81 YFPGYASYSKETKEGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 161 GVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTVFMREHTDA 240
Cdd:cd00542  161 GLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489739426 241 VTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 303
Cdd:cd00542  241 PKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-324 1.48e-124

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: 360.35  E-value: 1.48e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   1 MCTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADG--FDSPYSFVGTGRDLNGYIFVDGVNEHGVSAA 78
Cdd:COG3049    3 MCTRIVYKTKDGTVITGRTMDWGFDLGSNLVVFPRGYERDGEVGPNSlkWTSKYGSVGMGAYDGYPLTADGMNEKGLAAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  79 ALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELE 158
Cdd:COG3049   83 LLYFPGYADYPKRDKEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATGDSAVIEYI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 159 NDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTVFMREHT 238
Cdd:COG3049  163 DGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNAL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 239 DAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVELTPALMT-AAQPTEFE 317
Cdd:COG3049  243 PKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSkGAEVKKLD 322

                 ....*..
gi 489739426 318 LKTTQQF 324
Cdd:COG3049  323 LDPNEQL 329
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-303 1.25e-85

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: 260.53  E-value: 1.25e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   1 MCTSLTIqTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGfDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAA 79
Cdd:NF038245   1 MCTALTY-TTKDDHYFGRNLDLEFSYGEKVVITPRNYPFKFRKEADL-KTHYAIIGMATVVDNYpLYFDAMNEKGLGMAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  80 LYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNvmeaaapLLNI-------VVPLHWIISDKSGST 152
Cdd:NF038245  79 LNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQCETVDEVKEALKNIN-------LVNIpfseqlpLSPLHWIIADKTGSS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 153 YVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTV 232
Cdd:NF038245 152 IVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAA 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489739426 233 FMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 303
Cdd:NF038245 232 FTKANSPSGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDM 302
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-303 1.40e-82

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: 252.82  E-value: 1.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426    2 CTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAAL 80
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGISYGEEVIITPRNYKLVFEKLGNMLVTKYAVIGMGTDVGSYpLFYDGLNEKGLGIAGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   81 YFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELEND 160
Cdd:pfam02275  81 YFPGYAFYSKGPKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDASGESIVIEPRKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  161 GVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTVFMREHTDA 240
Cdd:pfam02275 161 GLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPK 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489739426  241 VTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 303
Cdd:pfam02275 241 AKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKGNYYFETYDNSQINAVNL 303
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
2-174 1.46e-05

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 46.13  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   2 CTSLTIQTTAGDQFLARTMDFAFEL-GGRPVAiprnhhfdSVTNADGFDspYSFVGTGrdlnGYIF--VDGVNEHGVSAA 78
Cdd:NF040521  90 CSTFAVLGEDGEPILARNYDWHPELyDGCLLL--------TIRPDGGPR--YASIGYA----GLLPgrTDGMNEAGLAVT 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  79 alyfsgqAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMeaaapllnivVPLHWIISDKSGSTYVLELE 158
Cdd:NF040521 156 -------LNFLDGRKLPGVGVPVHLLARAILENCKTVDEAIALLKEIPRA----------SSFNLTLADASGRAASVEAS 218
                        170
                 ....*....|....*...
gi 489739426 159 NDGVHYMKNPVGVM--TN 174
Cdd:NF040521 219 PDRVVVVRPEDGLLvhTN 236
 
Name Accession Description Interval E-value
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
2-303 2.09e-152

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: 429.71  E-value: 2.09e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   2 CTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAAL 80
Cdd:cd00542    1 CTSLTLSTKDGDHVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYpLLFDGVNEKGLAIAGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  81 YFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELEND 160
Cdd:cd00542   81 YFPGYASYSKETKEGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 161 GVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTVFMREHTDA 240
Cdd:cd00542  161 GLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489739426 241 VTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 303
Cdd:cd00542  241 PKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-324 1.48e-124

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: 360.35  E-value: 1.48e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   1 MCTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADG--FDSPYSFVGTGRDLNGYIFVDGVNEHGVSAA 78
Cdd:COG3049    3 MCTRIVYKTKDGTVITGRTMDWGFDLGSNLVVFPRGYERDGEVGPNSlkWTSKYGSVGMGAYDGYPLTADGMNEKGLAAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  79 ALYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELE 158
Cdd:COG3049   83 LLYFPGYADYPKRDKEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATGDSAVIEYI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 159 NDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTVFMREHT 238
Cdd:COG3049  163 DGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNAL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 239 DAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVELTPALMT-AAQPTEFE 317
Cdd:COG3049  243 PKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSkGAEVKKLD 322

                 ....*..
gi 489739426 318 LKTTQQF 324
Cdd:COG3049  323 LDPNEQL 329
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-303 1.25e-85

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: 260.53  E-value: 1.25e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   1 MCTSLTIqTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGfDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAA 79
Cdd:NF038245   1 MCTALTY-TTKDDHYFGRNLDLEFSYGEKVVITPRNYPFKFRKEADL-KTHYAIIGMATVVDNYpLYFDAMNEKGLGMAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  80 LYFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNvmeaaapLLNI-------VVPLHWIISDKSGST 152
Cdd:NF038245  79 LNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQCETVDEVKEALKNIN-------LVNIpfseqlpLSPLHWIIADKTGSS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 153 YVLELENDGVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTV 232
Cdd:NF038245 152 IVVESTKDGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAA 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489739426 233 FMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 303
Cdd:NF038245 232 FTKANSPSGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDM 302
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-303 1.40e-82

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: 252.82  E-value: 1.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426    2 CTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGFDSPYSFVGTGRDLNGY-IFVDGVNEHGVSAAAL 80
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGISYGEEVIITPRNYKLVFEKLGNMLVTKYAVIGMGTDVGSYpLFYDGLNEKGLGIAGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   81 YFSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELEND 160
Cdd:pfam02275  81 YFPGYAFYSKGPKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDASGESIVIEPRKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  161 GVHYMKNPVGVMTNTPDFEWHLKNLSNYVNLQPGPHPSRQYGDMTVNPFGPGTGALGMPGDYTSVARFVRTVFMREHTDA 240
Cdd:pfam02275 161 GLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPK 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489739426  241 VTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAYMSMNEPAFYMQPYADQTITRVEL 303
Cdd:pfam02275 241 AKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKGNYYFETYDNSQINAVNL 303
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
2-282 2.41e-67

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: 210.67  E-value: 2.41e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   2 CTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGfDSPYSFVGTGRDLNGYIFVDGVNEHGVSAAALY 81
Cdd:cd01935    1 CTSIVAQTKDGGVYLGRNMDFSFDYELRLLVFPRGYQRNGQTGDKS-KWYAKYGSGGTSAGYIGLVDGMNEKGLSVSLLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  82 FSGQAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMEAAAPLLNIVVPLHWIISDKSGSTYVLELENDG 161
Cdd:cd01935   80 FPGYAYYPAGIKEGKDGLPAFELIRWVLENCDSVEEVKEALKKIPIVDFPIPLGGPAAPLHYILSDKSGDSAVIEPIDGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 162 VHYMKNP-VGVMTNTPDFEWHLknlsnyvnlqpgphpsrqygdmtvnpfgpgtgalgmpgdytsVARFVRTVFMREHTDA 240
Cdd:cd01935  160 LKIYDNPwFGVMTNHPTFDWHL------------------------------------------PRRFVRVAYLKNTAQK 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489739426 241 VTTDAEAVNALSHMLNSVEIPKGVkmqdngtpdyTQYRAYMS 282
Cdd:cd01935  198 NKETVEDVKNLFHILESVPIPNGL----------TVYTTVMD 229
Ntn_CGH cd01902
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
1-280 3.64e-20

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: 88.55  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   1 MCTSLTIQTTAGDQFLARTMDFAFELGGRPVAIPRNHHFDSVTNADGFD--SPYSFVGTGrdLNGYIFVDGVNEHGVSAA 78
Cdd:cd01902    1 ACTRILWNTNNQGVITGRSMDWKEDTGPNLWVFPRGMERDGGTGDNSAKwtSKYGSVVAS--MYDIGTVDGMNEKGLVAN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  79 ALYFSGqAHFTQQTKaGKVNLApheVLMW---ILGNVKSTAELGERIADLN-VMEAAAPLLNIVVPLHWIISDKSGSTYV 154
Cdd:cd01902   79 LLYLTE-SDYGPADP-NKPTLS---AGAWgqyLLDNYATVEEAVKALAKEPfVIVASVPGDGREATLHLSISDATGDSAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426 155 LELENDG--VHYMKNpVGVMTNTPDFEWHLKNLSNYVNLQpgphpsrqygdmtvnpfgPGTGALGMPGDYTSVARFVRTV 232
Cdd:cd01902  154 IEYIDGKlvIHHGKQ-YQVMTNSPTYDQQLALNKYWKQEK------------------DIGGTTGLPGNNNPADRFVRAS 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489739426 233 FMREHTDAVTTDAEAVNALSHMLNSVEIPKGVKMQDNGTPDYTQYRAY 280
Cdd:cd01902  215 YYISALPKTADEREAVASVLSVIRNVSVPFGIPTPAPPNISDTRWRTV 262
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
2-174 1.46e-05

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 46.13  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426   2 CTSLTIQTTAGDQFLARTMDFAFEL-GGRPVAiprnhhfdSVTNADGFDspYSFVGTGrdlnGYIF--VDGVNEHGVSAA 78
Cdd:NF040521  90 CSTFAVLGEDGEPILARNYDWHPELyDGCLLL--------TIRPDGGPR--YASIGYA----GLLPgrTDGMNEAGLAVT 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739426  79 alyfsgqAHFTQQTKAGKVNLAPHEVLMWILGNVKSTAELGERIADLNVMeaaapllnivVPLHWIISDKSGSTYVLELE 158
Cdd:NF040521 156 -------LNFLDGRKLPGVGVPVHLLARAILENCKTVDEAIALLKEIPRA----------SSFNLTLADASGRAASVEAS 218
                        170
                 ....*....|....*...
gi 489739426 159 NDGVHYMKNPVGVM--TN 174
Cdd:NF040521 219 PDRVVVVRPEDGLLvhTN 236
 
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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