| IED ID | IndEnz0010000276 |
| Enzyme Type ID | esterase000276 |
| Protein Name |
Bile acid-CoA:amino acid N-acyltransferase BACAT BAT EC 2.3.1.65 Bile acid-CoA thioesterase Choloyl-CoA hydrolase EC 3.1.2.27 Glycine N-choloyltransferase Long-chain fatty-acyl-CoA hydrolase EC 3.1.2.2 |
| Gene Name | Baat |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAKLTAVPLSALVDEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLLGRLIKRDVMNSPYQIHIKACHPYFPLQDIVVSPPLDSLTLERWYVAPGVKRIQVKESRIRGALFLPPGEGPFPGVIDLFGGAGGLMEFRASLLASRGFATLALAYWNYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFVVTNALGLVEFYRTFQETADKDSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKKNWTLLSYPGAGHLIEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLPDLSSQL |
| Enzyme Length | 420 |
| Uniprot Accession Number | Q91X34 |
| Absorption | |
| Active Site | ACT_SITE 235; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 328; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 362; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=choloyl-CoA + glycine = CoA + glycocholate + H(+); Xref=Rhea:RHEA:14001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57373; EC=2.3.1.65; Evidence={ECO:0000269|PubMed:9215542};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14002; Evidence={ECO:0000305|PubMed:9215542}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=choloyl-CoA + H2O = cholate + CoA + H(+); Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373; EC=3.1.2.27; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+); Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989; EC=3.1.2.27; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+); Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate; Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate; Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=choloyl-CoA + taurine = CoA + H(+) + taurocholate; Xref=Rhea:RHEA:47100, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47101; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholoyl-CoA + glycine = CoA + glycochenodeoxycholate + H(+); Xref=Rhea:RHEA:49788, ChEBI:CHEBI:15378, ChEBI:CHEBI:36252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:62989; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49789; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholoyl-CoA + taurine = CoA + H(+) + taurochenodeoxycholate; Xref=Rhea:RHEA:49784, ChEBI:CHEBI:9407, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989, ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49785; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + glycine = CoA + H(+) + N-eicosanoylglycinate; Xref=Rhea:RHEA:49792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57380, ChEBI:CHEBI:87391; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49793; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=glycine + hexacosanoyl-CoA = CoA + H(+) + N-hexacosanoylglycine; Xref=Rhea:RHEA:49772, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:64868, ChEBI:CHEBI:87414; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49773; Evidence={ECO:0000250|UniProtKB:Q14032}; CATALYTIC ACTIVITY: Reaction=docosanoyl-CoA + glycine = CoA + H(+) + N-docosanoylglycine; Xref=Rhea:RHEA:49780, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:65059, ChEBI:CHEBI:87410; Evidence={ECO:0000250|UniProtKB:Q14032};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49781; Evidence={ECO:0000250|UniProtKB:Q14032}; |
| DNA Binding | |
| EC Number | 2.3.1.65; 3.1.2.27; 3.1.2.2 |
| Enzyme Function | FUNCTION: Catalyzes the amidation of bile acids (BAs) with the amino acid taurine (PubMed:9215542). Selective for taurine conjugation of cholyl CoA and only taurine-conjugated BAs are found in bile (PubMed:9215542). Amidation of BAs in the liver with taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (By similarity). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity). In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:Q14032, ECO:0000269|PubMed:9215542}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Frameshift (2); Modified residue (6); Sequence conflict (5) |
| Keywords | Acyltransferase;Cytoplasm;Fatty acid metabolism;Hydrolase;Lipid metabolism;Peroxisome;Phosphoprotein;Reference proteome;Serine esterase;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14032}. Peroxisome {ECO:0000250|UniProtKB:Q63276}. |
| Modified Residue | MOD_RES 40; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 125; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q63276; MOD_RES 346; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 350; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 409; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 418; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q63276 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 11722848; 12239217; 12466851; 14681479; 15760467; 21267068; 21677750; 9250880; 9721207; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,482 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for taurine toward choloyl-CoA {ECO:0000269|PubMed:9215542}; |
| Metal Binding | |
| Rhea ID | RHEA:14001; RHEA:14002; RHEA:16645; RHEA:16646; RHEA:14541; RHEA:14542; RHEA:31511; RHEA:31512; RHEA:40147; RHEA:40148; RHEA:30139; RHEA:30140; RHEA:40783; RHEA:40784; RHEA:40787; RHEA:40788; RHEA:40791; RHEA:40792; RHEA:30135; RHEA:30136; RHEA:40119; RHEA:40120; RHEA:47100; RHEA:47101; RHEA:49788; RHEA:49789; RHEA:49784; RHEA:49785; RHEA:49792; RHEA:49793; RHEA:49772; RHEA:49773; RHEA:49780; RHEA:49781 |
| Cross Reference Brenda |