Acyl-CoA_Thioesterase
Relationship
Comment
Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase. Long chain acyl CoA thioesterases hydrolyze long chain acyl-CoAs to the corresponding free fatty acid and CoASH. ACOTs are broadly divided into two distinct subgroups, the type-I alpha/beta-hydrolase fold enzyme superfamily and the type-II 'hot dog' fold superfamily. Here only a/b hydrolases. The major solutes in bile are N-acyl conjugates of cholanoates (C24 bile acids) with glycine or taurine. These bile acid-amino acid conjugates serve as detergents in the gastrointestinal tract. Bile acid-amino acid conjugates are formed in the liver via a 2-step pathway. The first reaction converts a bile acid to an acyl-CoA thioester and is catalyzed by the microsomal enzyme, cholyl-CoA synthetase (EC 6.2.1.7). The second reaction transfers the bile acid moiety from the acyl-CoA thioester to either glycine or taurine, and is catalyzed by bile acid-CoA:amino acid N-acyltransferase (BAAT; EC 2.3.1.65). Some homologies to Dienelactone_hydrolase and AlphaBeta-hydrolases (PF08840 BAAT only C-term PIRSF019303) The mouse ACOT gene cluster comprises six genes with localizations in cytosol (ACOT1), mitochondria (ACOT2), and peroxisomes (ACOT3-6). The corresponding human gene cluster contains only three genes (ACOT1, ACOT2, and ACOT4) coding for full-length thioesterase proteins only ACOT4 is peroxisomal. Family TE2 in ThYme database
Database
Interpro : IPR006862 Acyl-CoA thioester hydrolase\/bile acid-CoA amino acid N-acetyltransferase , IPR016662 Structures: Acyl-CoA thioesterase, long chain
PIRSF : PIRSF019303 acyl-CoA thioesterase (hydrolase)
Pdoc : No Pdoc
Pfam : PF04775 Bile_Hydr_Trans Acyl-CoA thioester hydrolase\/BAAT N-terminal region , PF08840 BAAT_C BAAT \/ Acyl-CoA thioester hydrolase C terminal
Prints : No Print
EC Number : 3.1.2.2
Sequences
| Peptide in | Fasta |
| Nucleotide in | Fasta |
| Alignment with Multalin | Text only |
| Seed alignment with MAFFT | No colour / coloured with Mview |
| Alignment with MAFFT | No colour / coloured with Mview |
| Dendrogram | The dnd file |
| Structure | Name | Proteins |
|---|---|---|
| 3K2I | Human Acyl-coenzyme A thioesterase 4 | human-ACOT4 |
| 3HLK | Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2) | human-ACOT2 |
| Gene_locus | Name | Species |
|---|---|---|
| 9eury-c1vei1 | Halogeometricum borinquense DSM 11551 Dienelactone hydrolase-like enzyme | Halogeometricum borinquense DSM 11551 |
| 9flao-q1vpk2 | Psychroflexus torquis (strain ATCC 700755 \/ ACAM 623) hypothetical protein | Psychroflexus torquis ATCC 700755 |
| 9sphn-q2n9j1 | Erythrobacter litoralis HTCC2594 dienelactone hydrolase family protein | Erythrobacter litoralis HTCC2594 |
| agrtu-ATU3652 | Agrobacterium tumefaciens (strain C58 \/ ATCC 33970) hypothetical protein atu3652 | Agrobacterium tumefaciens |
| bacld-q65ly2 | Bacillus licheniformis (strain DSM 13 \/ ATCC 14580) hypothetical protein (EC 3.1.2.2) | Bacillus licheniformis |
| bora1-q2l1v4 | Bordetella avium (strain 197N) putative acyl coenzyme a thioester hydrolase (EC 3.1.2.2) | Bordetella avium |
| borbr-q7wk25 | Bordetella bronchiseptica (Alcaligenes bronchisepticus) Bordetella parapertussis putative acyl coenzyme a thioester hydrolase (EC 3.1.2.2) | Bordetella bronchiseptica |
| caebr-a8xk76 | Caenorhabditis briggsae hypothetical protein cbg14567 | Caenorhabditis briggsae |
| caebr-A8XG15 | Caenorhabditis briggsae hypothetical protein cbg12559 | Caenorhabditis briggsae |
| caebr-A8XFE8 | Caenorhabditis briggsae hypothetical protein CBG12426 (fragment) | Caenorhabditis briggsae |
| caebr-A8WW80 | Caenorhabditis briggsae hypothetical protein cbg04103 | Caenorhabditis briggsae |
| caeel-C31H5.6 | Caenorhabditis elegans c31h5.6 protein | Caenorhabditis elegans |
| caeel-K05B2.4 | Caenorhabditis elegans hypothetical 43.5 kda protein | Caenorhabditis elegans |
| caeel-T05E7.1 | Caenorhabditis elegans t05e7.1 protein | Caenorhabditis elegans |
| caeel-W03D8.8 | Caenorhabditis elegans w03d8.8 protein | Caenorhabditis elegans |
| cloac-CAC3407 | Clostridium acetobutylicum Acyl-CoA thioesterase 1 | Clostridium acetobutylicum |
| clob8-a6lt95 | Clostridium beijerinckii (strain ATCC 51743 \/ NCIMB 8052) (Clostridium acetobutylicum) Acyl-CoA thioesterase 1 | Clostridium beijerincki NCIMB 8052 |
| danre-q5rh34 | Danio rerio (Zebrafish) (Brachydanio rerio) similar to cytosolic Acyl-CoA amino acid n-acetyltransferase domain zgc:7765 | Danio rerio |
| danre-q5rh35 | Danio rerio (Zebrafish) (Brachydanio rerio) similar to cytosolic Acyl-CoA amino acid n-acetyltransferase domain | Danio rerio |
| danre-q5rhg4 | Danio rerio (Zebrafish) (Brachydanio rerio) similar to cytosolic Acyl-CoA amino acid n-acetyltransferase domain | Danio rerio |
| danre-q5rhg5 | Danio rerio (Zebrafish) (Brachydanio rerio) similar to cytosolic Acyl-CoA amino acid n-acetyltransferase domain | Danio rerio |
| danre-q5spg7 | Danio rerio (Zebrafish) (Brachydanio rerio) thioesterase. (fragment) | Danio rerio |
| danre-q5spg8 | Danio rerio (Zebrafish) (Brachydanio rerio) novel protein similar to vertebrate Acyl-CoA thioesterase family | Danio rerio |
| danre-q5u3w6 | Danio rerio (Zebrafish) (Brachydanio rerio) zgc:101553 | Danio rerio |
| danre-q6gmj5 | Danio rerio (Zebrafish) (Brachydanio rerio) hypothetical protein (fragment) | Danio rerio |
| danre-q6ph28 | Danio rerio (Zebrafish) (Brachydanio rerio) loc402867 CoA amino acid n-acetyltransferase domain (zgc:77651) (fragment) | Danio rerio |
| human-ACOT1 | Homo sapiens (Human) Inducible cytosolic acyl-coenzyme A thioester hydrolase Long chain Acyl-CoA hydrolase) (cte-i) (cte-ib) | Homo sapiens |
| human-ACOT2 |  Homo sapiens (Human) peroxisomal long-chain Acyl-CoA thioesterase 2 (zap128) (protein for mgc:3983) mitochondrial (EC 3.1.2.2) CTE-1a |
Homo sapiens |
| human-ACOT4 | Homo sapiens (Human) Q8N9L9 Acyl-coenzyme A thioesterase 4, inducible (EC 3.1.2.2) |
Homo sapiens |
| human-ACOT6 | Homo sapiens (Human) Acyl-CoA thioesterase 6 (EC 3.1.2.2) | Homo sapiens |
| human-BAAT | Homo sapiens (Human) bile acid CoA: amino acid n-acyltransferase (EC 3.1.2.2) | Homo sapiens |
| macfa-q4r4j8 | Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey) Acyl-CoA thioesterase (zap128),mrna, refseq: nm_006821.3 | Macaca fascicularis |
| mouse-acnt1 | Mus musculus (Mouse) Acyl-coenzyme A amino acid N-acyltransferase 1 | Mus musculus |
| mouse-acot1 | Mus musculus (Mouse) hydrolase) ACOT1 (cte-I) cytosolic long chain Acyl-CoA thioesterase | Mus musculus |
| mouse-acot2 | Mus musculus (Mouse) (EC 3.1.2.2) very-long-chain Acyl-CoA thioesterase (MTE-I) ACOT2 | Mus musculus |
| mouse-acot3 | Mus musculus (Mouse) (peroxisomal long-chain Acyl-CoA thioesterase 2) (pte-IA) (EC 3.1.2.2) | Mus musculus |
| mouse-acot4 | Mus musculus (Mouse) peroxisomal long chain Acyl-CoA thioesterase Ib (pte-Ib) (pte-2b) | Mus musculus |
| mouse-acot5 | Mus musculus (Mouse) (peroxisomal cytosolic Acyl-CoA thioesterase Ic) | Mus musculus |
| mouse-BAAT | Mus musculus (Mouse) bile acid CoA: amino acid n-acyltransferase (EC 3.1.2.2) | Mus musculus |
| mouse-ACOT6 | Mus musculus (Mouse)acyl-CoA thioesterase 6 (EC 3.1.2.2). Weakly similar to peroxisomal acyl-coenzyme A thioester hydrolase2 | Mus musculus |
| mouse-Q8BGG9 | Mus musculus (Mouse) Similar to bile acid coenzyme A: amino acid N-acyltransferase | Mus musculus |
| pelts-a5czq3 | Pelotomaculum thermopropionicum (strain DSM 13744 \/ JCM 10971 \/ SI) hydrolases of the alpha\/beta superfamily | Pelotomaculum thermopropionicum SI |
| ralso-RSC1887 | Ralstonia solanacearum (Pseudomonas solanacearum) Putative uncharacterized protein (EC 3.1.2.2) | Ralstonia solanacearum |
| ratno-acot1 | Rattus norvegicus (Rat) hydrolase) (cte-I) (lach2) (ach2) | Rattus norvegicus |
| ratno-acot2 | Rattus norvegicus (Rat) (EC 3.1.2.2) ACOT2 mitochondrial Acyl-CoA thioesterase 1 very-long-chain Acyl-CoA thioesterase (MTE-I) | Rattus norvegicus |
| ratno-BAAT | Rattus norvegicus (Rat) bile acid CoA: amino acid n-acyltransferase kan-1 (EC 3.1.2.2) | Rattus norvegicus |
| ratno-q5fvr5 | Rattus norvegicus (Rat) hypothetical loc313220 | Rattus norvegicus |
| rhil3-q1mg17 | Rhizobium leguminosarum bv. viciae (strain 3841) hypothetical protein | Rhizobium leguminosarum bv. viciae |
| rhilo-MLR4383 | Rhizobium loti (Mesorhizobium loti) Acyl-CoA thioesterase | Rhizobium loti |
| solus-q43mm3 | Solibacter usitatus Ellin6076 palmitoyl-coa hydrolase precursor (EC 3.1.2.2) | Solibacter usitatus Ellin6076 |
| strmu-SMU.633 | Streptococcus mutans putative thioesterase | Streptococcus mutans |
| strmu-SMU.1678 | Streptococcus mutans conserved hypothetical protein, possible Acyl-CoA thioesterase | Streptococcus mutans |
| tetng-q4rqz6 | Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon nigroviridis) hypothetical protein (fragment) | Tetraodon nigroviridis |
| trede-q73kp3 | Treponema denticola hypothetical protein | Treponema denticola |
| xenla-q6ntq4 | Xenopus laevis (African clawed frog) mgc83099 protein | Xenopus laevis |
| Gene_locus_frgt | Name | Species |
|---|---|---|
| alkmq-a6tuz7 | Alkaliphilus metalliredigens (strain QYMF), Acyl-CoA thioesterase 1 | Alkaliphilus metalliredigenes QYMF |
| antel-q2f6g5 | Anthopleura elegantissima (Sea anemone) long chain Acyl-CoA thioesterase-like protein (fragment) | Anthopleura elegantissima |
| caucr-CC0882 | Caulobacter crescentus dienelactone hydrolase family protein | Caulobacter crescentus |
| clobe-q2wku2 | Clostridium beijerincki NCIMB 8052 Acyl-CoA thioesterase 1 | Clostridium beijerincki NCIMB 8052 |
| tetng-q4s5e6 | Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon nigroviridis) chromosome 19 scaf14731, whole genome shotgun sequence | Tetraodon nigroviridis |
| tetng-q4se67 | Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon nigroviridis) chromosome undetermined scaf14625, whole genome shotgun sequence | Tetraodon nigroviridis |
| tetng-q4t6v2 | Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon nigroviridis) (fragment) | Tetraodon nigroviridis |
| Substrate | Chemical Nomenclature | Proteins |
|---|---|---|
| Cholyl-CoA | S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] (4R)-4-[(3R,5S,7R,8R,9S,10S,12S,13R,14S,17R)-3,7,12-trihydroxy-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]pentanethioate | human-BAAT |
| Palmitoyl-CoA | S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] hexadecanethioate | ecoli-ybff |
| Inhibitor | Chemical Nomenclature | Proteins |
|---|---|---|
| Rocaglate-Derived-beta-Lactone-5 | (1S,9R,10S,11R,14R)-1-hydroxy-3,5-dimethoxy-9-(4-methoxyphenyl)-10-phenyl-8,13-dioxatetracyclo[7.5.0.02,7.011,14]tetradeca-2(7),3,5-trien-12-one | human-ABHD10 human-SCPEP1 human-ACOT1 human-ACOT2 human-CTSA |
References (8)
| Title : Progress of the acyl-Coenzyme A thioester hydrolase family in cancer - Bai_2024_Front.Oncol_14_1374094 |
| Author(s) : Bai L , Yang P , Han B , Kong L |
| Ref : Front Oncol , 14 :1374094 , 2024 |
| Abstract : |
| PubMedSearch : Bai_2024_Front.Oncol_14_1374094 |
| PubMedID: 38562172 |
| Title : Thioesterase enzyme families: Functions, structures, and mechanisms - Caswell_2021_Protein.Sci__ |
| Author(s) : Caswell BT , de Carvalho CC , Nguyen H , Roy M , Nguyen T , Cantu DC |
| Ref : Protein Science , : , 2021 |
| Abstract : |
| PubMedSearch : Caswell_2021_Protein.Sci__ |
| PubMedID: 34921469 |
| Title : ThYme: a database for thioester-active enzymes - Cantu_2011_Nucleic.Acids.Res_39_D342 |
| Author(s) : Cantu DC , Chen Y , Lemons ML , Reilly PJ |
| Ref : Nucleic Acids Research , 39 :D342 , 2011 |
| Abstract : |
| PubMedSearch : Cantu_2011_Nucleic.Acids.Res_39_D342 |
| PubMedID: 21045059 |
| Title : Thioesterases: a new perspective based on their primary and tertiary structures. - Cantu_2010_Protein.Sci_19_1281 |
| Author(s) : Cantu DC , Chen Y , Reilly PJ |
| Ref : Protein Science , 19 :1281 , 2010 |
| Abstract : |
| PubMedSearch : Cantu_2010_Protein.Sci_19_1281 |
| PubMedID: 20506386 |
| Title : Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2) - Mandel_2009_Biochem.Biophys.Res.Commun_385_630 |
| Author(s) : Mandel CR , Tweel B , Tong L |
| Ref : Biochemical & Biophysical Research Communications , 385 :630 , 2009 |
| Abstract : |
| PubMedSearch : Mandel_2009_Biochem.Biophys.Res.Commun_385_630 |
| PubMedID: 19497300 |
| Gene_locus related to this paper: human-ACOT2 |
| Title : Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs - Hunt_2006_FASEB.J_20_1855 |
| Author(s) : Hunt MC , Rautanen A , Westin MA , Svensson LT , Alexson SE |
| Ref : FASEB Journal , 20 :1855 , 2006 |
| Abstract : |
| PubMedSearch : Hunt_2006_FASEB.J_20_1855 |
| PubMedID: 16940157 |
| Gene_locus related to this paper: human-ACOT1 , human-ACOT2 , human-ACOT4 , human-ACOT6 , mouse-acot1 , mouse-acot2 , mouse-acot3 , mouse-acot4 , mouse-acot5 , mouse-ACOT6 |
| Title : The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha\/beta hydrolase - Huhtinen_2001_J.Biol.Chem_277_3424 |
| Author(s) : Huhtinen K , O'Byrne J , Lindquist PJ , Contreras JA , Alexson SE |
| Ref : Journal of Biological Chemistry , 277 :3424 , 2001 |
| Abstract : |
| PubMedSearch : Huhtinen_2001_J.Biol.Chem_277_3424 |
| PubMedID: 11694534 |
| Gene_locus related to this paper: mouse-acot1 |
| Title : Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. - |
| Author(s) : Jones JM , Gould SJ |
| Ref : Biochemical & Biophysical Research Communications , 275 :233 , 2000 |
| PubMedID: 10944470 |
| Gene_locus related to this paper: human-ACOT2 |