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Conserved domains on  [gi|110225339|ref|NP_031545|]
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bile acid-CoA:amino acid N-acyltransferase [Mus musculus]

Protein Classification

acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase family protein( domain architecture ID 10521460)

acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase (BAAT) family protein may catalyze the hydrolysis of acyl-CoA or catalyze the amidation of bile acids with the amino acids taurine and glycine

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917
SCOP:  3000102

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
206-414 4.23e-100

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


:

Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 296.88  E-value: 4.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339  206 VDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFV 285
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339  286 VTNALGLVEFYRTFQETADK-DSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKK-NWTLLSYPGAGHL 363
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110225339  364 IEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLP 414
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
14-140 2.92e-60

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


:

Pssm-ID: 428115  Cd Length: 120  Bit Score: 191.59  E-value: 2.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339   14 DEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLL-GRLI 92
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRASLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVEPMGLFWSMKPEPGFrLRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 110225339   93 KRDVMnSPYQIHIKachpyfpLQDIVVSPPLDSLTLERWYVAPGVKRI 140
Cdd:pfam04775  81 KRDVL-TPFVVTLS-------VYDEVEGKPLASTTVERWYMAPGVTRI 120
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
206-414 4.23e-100

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 296.88  E-value: 4.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339  206 VDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFV 285
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339  286 VTNALGLVEFYRTFQETADK-DSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKK-NWTLLSYPGAGHL 363
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110225339  364 IEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLP 414
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
14-140 2.92e-60

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


Pssm-ID: 428115  Cd Length: 120  Bit Score: 191.59  E-value: 2.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339   14 DEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLL-GRLI 92
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRASLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVEPMGLFWSMKPEPGFrLRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 110225339   93 KRDVMnSPYQIHIKachpyfpLQDIVVSPPLDSLTLERWYVAPGVKRI 140
Cdd:pfam04775  81 KRDVL-TPFVVTLS-------VYDEVEGKPLASTTVERWYMAPGVTRI 120
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
140-412 1.63e-09

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223489 [Multi-domain]  Cd Length: 236  Bit Score: 57.78  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339 140 IQVKESRIRGALFLPPGEGPFPGVIdLFGGAGGLMEF---RASLLASRGFATLALA-YW------NYDDLPSRLEKVDLE 209
Cdd:COG0412    7 IPAPDGELPAYLARPAGAGGFPGVI-VLHEIFGLNPHirdVARRLAKAGYVVLAPDlYGrqgdptDIEDEPAELETGLVE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339 210 YF---------EEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVlingpnfvsqsphVYHGQVYPPvps 280
Cdd:COG0412   86 RVdpaevladiDAALDYLARQPQVDPKRIGVVGFCMGGGLALLAATRAPEVKAAV-------------AFYGGLIAD--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339 281 neefvvtnalglvefyrtfqETADKDSKYCfPIekahghfLFVVGEDDKNLNSKvhANQAIAQLMKNGKKNWTLLSYPGA 360
Cdd:COG0412  150 --------------------DTADAPKIKV-PV-------LLHLAGEDPYIPAA--DVDALAAALEDAGVKVDLEIYPGA 199
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 110225339 361 GHlieppytplcqasrmpilipslSW-----GGEVIPHAAAQEHSWKEIQKFLKQHL 412
Cdd:COG0412  200 GH----------------------GFandraDYHPGYDAAAAEDAWQRVLAFFKRLL 234
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
206-414 4.23e-100

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 296.88  E-value: 4.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339  206 VDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFV 285
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339  286 VTNALGLVEFYRTFQETADK-DSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKK-NWTLLSYPGAGHL 363
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKpDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110225339  364 IEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLP 414
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
14-140 2.92e-60

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


Pssm-ID: 428115  Cd Length: 120  Bit Score: 191.59  E-value: 2.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339   14 DEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLL-GRLI 92
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRASLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVEPMGLFWSMKPEPGFrLRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 110225339   93 KRDVMnSPYQIHIKachpyfpLQDIVVSPPLDSLTLERWYVAPGVKRI 140
Cdd:pfam04775  81 KRDVL-TPFVVTLS-------VYDEVEGKPLASTTVERWYMAPGVTRI 120
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
140-412 1.63e-09

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223489 [Multi-domain]  Cd Length: 236  Bit Score: 57.78  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339 140 IQVKESRIRGALFLPPGEGPFPGVIdLFGGAGGLMEF---RASLLASRGFATLALA-YW------NYDDLPSRLEKVDLE 209
Cdd:COG0412    7 IPAPDGELPAYLARPAGAGGFPGVI-VLHEIFGLNPHirdVARRLAKAGYVVLAPDlYGrqgdptDIEDEPAELETGLVE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339 210 YF---------EEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVlingpnfvsqsphVYHGQVYPPvps 280
Cdd:COG0412   86 RVdpaevladiDAALDYLARQPQVDPKRIGVVGFCMGGGLALLAATRAPEVKAAV-------------AFYGGLIAD--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225339 281 neefvvtnalglvefyrtfqETADKDSKYCfPIekahghfLFVVGEDDKNLNSKvhANQAIAQLMKNGKKNWTLLSYPGA 360
Cdd:COG0412  150 --------------------DTADAPKIKV-PV-------LLHLAGEDPYIPAA--DVDALAAALEDAGVKVDLEIYPGA 199
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 110225339 361 GHlieppytplcqasrmpilipslSW-----GGEVIPHAAAQEHSWKEIQKFLKQHL 412
Cdd:COG0412  200 GH----------------------GFandraDYHPGYDAAAAEDAWQRVLAFFKRLL 234
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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