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Conserved domains on  [gi|493838216|ref|WP_006785385|]
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MULTISPECIES: choloylglycine hydrolase [Turicibacter]

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 NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-316 2.03e-156

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: 440.03  E-value: 2.03e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   1 MCTAITLKTQDGlHALGRNLDIVALLDVAVILIPRSYAFTHTIMSlKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAV 80
Cdd:NF038245   1 MCTALTYTTKDD-HYFGRNLDLEFSYGEKVVITPRNYPFKFRKEA-DLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  81 LELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTK 160
Cdd:NF038245  79 LNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQCETVDEVKEALKNINLVNIPFSEQLPLSPLHWIIADKTGSSIVVESTK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 161 GNFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNHIR 240
Cdd:NF038245 159 DGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSP 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493838216 241 VEKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHLFDENLDASEVKV 316
Cdd:NF038245 239 SGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDMHKEDLDGSELIS 314
 
Name Accession Description Interval E-value
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-316 2.03e-156

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: 440.03  E-value: 2.03e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   1 MCTAITLKTQDGlHALGRNLDIVALLDVAVILIPRSYAFTHTIMSlKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAV 80
Cdd:NF038245   1 MCTALTYTTKDD-HYFGRNLDLEFSYGEKVVITPRNYPFKFRKEA-DLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  81 LELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTK 160
Cdd:NF038245  79 LNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQCETVDEVKEALKNINLVNIPFSEQLPLSPLHWIIADKTGSSIVVESTK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 161 GNFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNHIR 240
Cdd:NF038245 159 DGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSP 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493838216 241 VEKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHLFDENLDASEVKV 316
Cdd:NF038245 239 SGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDMHKEDLDGSELIS 314
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
2-304 5.06e-120

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: 347.67  E-value: 5.06e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   2 CTAITLKTQDGLHALGRNLDIVALLDVAVILIPRSYAFTHTIMSLKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAVL 81
Cdd:cd00542    1 CTSLTLSTKDGDHVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYPLLFDGVNEKGLAIAGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  82 ELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTKG 161
Cdd:cd00542   81 YFPGYASYSKETKEGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 162 NFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNHIRV 241
Cdd:cd00542  161 GLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493838216 242 EKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHL 304
Cdd:cd00542  241 PKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-322 4.87e-118

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: 343.79  E-value: 4.87e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   1 MCTAITLKTQDGLHALGRNLDIVALLDVAVILIPRSYAFT--HTIMSLKKKNKYAMVGMSTtFENHVLLVDGMNEKGLAC 78
Cdd:COG3049    3 MCTRIVYKTKDGTVITGRTMDWGFDLGSNLVVFPRGYERDgeVGPNSLKWTSKYGSVGMGA-YDGYPLTADGMNEKGLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  79 AVLELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEK 158
Cdd:COG3049   82 ALLYFPGYADYPKRDKEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATGDSAVIEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 159 TKGNFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNH 238
Cdd:COG3049  162 IDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 239 IRVEKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHLFDENLDAS-EVKVF 317
Cdd:COG3049  242 LPKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSKGaEVKKL 321

                 ....*
gi 493838216 318 PYQDK 322
Cdd:COG3049  322 DLDPN 326
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-317 8.13e-102

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: 301.74  E-value: 8.13e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216    2 CTAITLKTQDGLHALGRNLDIVALLDVAVILIPRSYAFTHTIMSLKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAVL 81
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGISYGEEVIITPRNYKLVFEKLGNMLVTKYAVIGMGTDVGSYPLFYDGLNEKGLGIAGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   82 ELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTKG 161
Cdd:pfam02275  81 YFPGYAFYSKGPKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDASGESIVIEPRKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  162 NFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNHIRV 241
Cdd:pfam02275 161 GLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493838216  242 EKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHLFDENLDASEVKVF 317
Cdd:pfam02275 241 AKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKGNYYFETYDNSQINAVNLDHENLDCTELVTY 316
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
2-175 4.90e-08

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: 53.45  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   2 CTAITLKTQDGLHALGRNLDI-VALLDVAVILIPRSyafthtimslKKKNKYAMVGMSTTFENHVllvDGMNEKGLACAV 80
Cdd:NF040521  90 CSTFAVLGEDGEPILARNYDWhPELYDGCLLLTIRP----------DGGPRYASIGYAGLLPGRT---DGMNEAGLAVTL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  81 LELPKYAswskvLDKDKInvaPYDFVYW-ILANFQSLEEVKDGLKNVNlvneslegkeVSVDVHWIVTDRTGQSIVIEKT 159
Cdd:NF040521 157 NFLDGRK-----LPGVGV---PVHLLARaILENCKTVDEAIALLKEIP----------RASSFNLTLADASGRAASVEAS 218
                        170
                 ....*....|....*...
gi 493838216 160 KGNFRIYNNKVGVL--TN 175
Cdd:NF040521 219 PDRVVVVRPEDGLLvhTN 236
 
Name Accession Description Interval E-value
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-316 2.03e-156

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: 440.03  E-value: 2.03e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   1 MCTAITLKTQDGlHALGRNLDIVALLDVAVILIPRSYAFTHTIMSlKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAV 80
Cdd:NF038245   1 MCTALTYTTKDD-HYFGRNLDLEFSYGEKVVITPRNYPFKFRKEA-DLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  81 LELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTK 160
Cdd:NF038245  79 LNFPGNAYYAEEVEGGKDNVAPFEFIPWILGQCETVDEVKEALKNINLVNIPFSEQLPLSPLHWIIADKTGSSIVVESTK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 161 GNFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNHIR 240
Cdd:NF038245 159 DGLHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSP 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493838216 241 VEKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHLFDENLDASEVKV 316
Cdd:NF038245 239 SGDSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDMHKEDLDGSELIS 314
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
2-304 5.06e-120

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: 347.67  E-value: 5.06e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   2 CTAITLKTQDGLHALGRNLDIVALLDVAVILIPRSYAFTHTIMSLKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAVL 81
Cdd:cd00542    1 CTSLTLSTKDGDHVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQGKSYTTKYAFIGMGAVGDDYPLLFDGVNEKGLAIAGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  82 ELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTKG 161
Cdd:cd00542   81 YFPGYASYSKETKEGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSGRSIVVEPTKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 162 NFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNHIRV 241
Cdd:cd00542  161 GLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493838216 242 EKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHL 304
Cdd:cd00542  241 PKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-322 4.87e-118

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: 343.79  E-value: 4.87e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   1 MCTAITLKTQDGLHALGRNLDIVALLDVAVILIPRSYAFT--HTIMSLKKKNKYAMVGMSTtFENHVLLVDGMNEKGLAC 78
Cdd:COG3049    3 MCTRIVYKTKDGTVITGRTMDWGFDLGSNLVVFPRGYERDgeVGPNSLKWTSKYGSVGMGA-YDGYPLTADGMNEKGLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  79 AVLELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEK 158
Cdd:COG3049   82 ALLYFPGYADYPKRDKEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATGDSAVIEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 159 TKGNFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNH 238
Cdd:COG3049  162 IDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 239 IRVEKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHLFDENLDAS-EVKVF 317
Cdd:COG3049  242 LPKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSKGaEVKKL 321

                 ....*
gi 493838216 318 PYQDK 322
Cdd:COG3049  322 DLDPN 326
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-317 8.13e-102

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: 301.74  E-value: 8.13e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216    2 CTAITLKTQDGLHALGRNLDIVALLDVAVILIPRSYAFTHTIMSLKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAVL 81
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGISYGEEVIITPRNYKLVFEKLGNMLVTKYAVIGMGTDVGSYPLFYDGLNEKGLGIAGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   82 ELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTKG 161
Cdd:pfam02275  81 YFPGYAFYSKGPKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDASGESIVIEPRKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  162 NFRIYNNKVGVLTNAPTFDWHLINLNRYMNIQVTNPHKVKWGHQELSFDSEGFGGIGLPGDVSSSSRFVKAAFLRNHIRV 241
Cdd:pfam02275 161 GLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493838216  242 EKGEDALITSTFHILSNVAVIKGTAVTCHQQYLKTQCTSCMCLETGVYYYNTYNNNQINAIHLFDENLDASEVKVF 317
Cdd:pfam02275 241 AKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKGNYYFETYDNSQINAVNLDHENLDCTELVTY 316
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
2-283 4.45e-65

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: 204.90  E-value: 4.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   2 CTAITLKTQDGLHALGRNLDIVALLDVAVILIPRSYAFTHTIMslKKKNKYAMVGMSTTFENHVLLVDGMNEKGLACAVL 81
Cdd:cd01935    1 CTSIVAQTKDGGVYLGRNMDFSFDYELRLLVFPRGYQRNGQTG--DKSKWYAKYGSGGTSAGYIGLVDGMNEKGLSVSLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  82 ELPKYASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNLVNESLEGKEVSVDVHWIVTDRTGQSIVIEKTKG 161
Cdd:cd01935   79 YFPGYAYYPAGIKEGKDGLPAFELIRWVLENCDSVEEVKEALKKIPIVDFPIPLGGPAAPLHYILSDKSGDSAVIEPIDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 162 NFRIY-NNKVGVLTNAPTFDWHLInlnrymniqvtnphkvkwghqelsfdsegfggiglpgdvsssSRFVKAAFLRNHIR 240
Cdd:cd01935  159 GLKIYdNPWFGVMTNHPTFDWHLP------------------------------------------RRFVRVAYLKNTAQ 196
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 493838216 241 VEKGEDALITSTFHILSNVAVIKGTavtchqqylkTQCTSCMC 283
Cdd:cd01935  197 KNKETVEDVKNLFHILESVPIPNGL----------TVYTTVMD 229
Ntn_CGH cd01902
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
1-261 7.68e-28

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: 109.73  E-value: 7.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   1 MCTAITLKTQDGLHALGRNLDIVAllDVAVIL--IPR-SYAFTHT-IMSLKKKNKYAMVGMSTTfenHVLLVDGMNEKGL 76
Cdd:cd01902    1 ACTRILWNTNNQGVITGRSMDWKE--DTGPNLwvFPRgMERDGGTgDNSAKWTSKYGSVVASMY---DIGTVDGMNEKGL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  77 ACAVLELPkyASWSKVLDKDKINVAPYDFVYWILANFQSLEEVKDGLKNVNL-VNESLEGKEVSVDVHWIVTDRTGQSIV 155
Cdd:cd01902   76 VANLLYLT--ESDYGPADPNKPTLSAGAWGQYLLDNYATVEEAVKALAKEPFvIVASVPGDGREATLHLSISDATGDSAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216 156 IEKTKGNFRIYNNK-VGVLTNAPTFDWHLINLNRYMNIQvtnphkvkwghqelsfdsEGFGGIGLPGDVSSSSRFVKAAF 234
Cdd:cd01902  154 IEYIDGKLVIHHGKqYQVMTNSPTYDQQLALNKYWKQEK------------------DIGGTTGLPGNNNPADRFVRASY 215
                        250       260
                 ....*....|....*....|....*..
gi 493838216 235 LRNHIRVEKGEDALITSTFHILSNVAV 261
Cdd:cd01902  216 YISALPKTADEREAVASVLSVIRNVSV 242
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
2-175 4.90e-08

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: 53.45  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   2 CTAITLKTQDGLHALGRNLDI-VALLDVAVILIPRSyafthtimslKKKNKYAMVGMSTTFENHVllvDGMNEKGLACAV 80
Cdd:NF040521  90 CSTFAVLGEDGEPILARNYDWhPELYDGCLLLTIRP----------DGGPRYASIGYAGLLPGRT---DGMNEAGLAVTL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  81 LELPKYAswskvLDKDKInvaPYDFVYW-ILANFQSLEEVKDGLKNVNlvneslegkeVSVDVHWIVTDRTGQSIVIEKT 159
Cdd:NF040521 157 NFLDGRK-----LPGVGV---PVHLLARaILENCKTVDEAIALLKEIP----------RASSFNLTLADASGRAASVEAS 218
                        170
                 ....*....|....*...
gi 493838216 160 KGNFRIYNNKVGVL--TN 175
Cdd:NF040521 219 PDRVVVVRPEDGLLvhTN 236
COG4927 COG4927
Predicted choloylglycine hydrolase [General function prediction only];
2-175 2.94e-07

Predicted choloylglycine hydrolase [General function prediction only];


Pssm-ID: 443955 [Multi-domain]  Cd Length: 242  Bit Score: 50.72  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216   2 CTAITLKTQDGLhALGRNLDivalldvaviLIPRSYAFTHtIMSLKKKNKYAMVGMSTTFENHVllvDGMNEKGLACAVL 81
Cdd:COG4927   88 CSQFAVAPEGEP-LLARNYD----------FHPDLYEGRL-LLTVQPDGGYAFIGVTDGLIGRL---DGMNEKGLAVGLN 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493838216  82 ELpkyaswskvldkdKINVAPYDFVYWILANF-----QSLEEVKDGLKNVnlvneslegkEVSVDVHWIVTDRTGQSIVI 156
Cdd:COG4927  153 FV-------------GRKVAGPGFPIPLLIRYiletcSTVDEAIALLKEI----------PHASSYNLTLADASGNAAVV 209
                        170       180
                 ....*....|....*....|
gi 493838216 157 EKTKGNFRIYN-NKVGVLTN 175
Cdd:COG4927  210 EVSPRGVEVREpNGFLVCTN 229
 
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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