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Identification
HMDB Protein ID HMDBP11000
Secondary Accession Numbers
  • 17324
Name Acyl-coenzyme A thioesterase 1
Synonyms
  1. Acyl-CoA thioesterase 1
  2. CTE-I
  3. CTE-Ib
  4. Inducible cytosolic acyl-coenzyme A thioester hydrolase
  5. Long chain acyl-CoA hydrolase
  6. Long chain acyl-CoA thioester hydrolase
Gene Name ACOT1
Protein Type Enzyme
Biological Properties
General Function Involved in thiolester hydrolase activity
Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active towards fatty acyl-CoA with chain-lengths of C12-C16 (By similarity).
Pathways
  • Biosynthesis of unsaturated fatty acids
  • Fatty acid elongation
Reactions
hexadecanoyl-CoA + Water → Coenzyme A + Palmitic acid details
Stearoyl-CoA + Water → Coenzyme A + Stearic acid details
Eicosanoyl-CoA + Water → Coenzyme A + Arachidic acid details
Oleoyl-CoA + Water → Coenzyme A + Oleic acid details
Linoleoyl-CoA + Water → Coenzyme A + Linoleic acid details
Alpha-Linolenoyl-CoA + Water → Coenzyme A + Alpha-Linolenic acid details
(5Z,8Z,11Z,14Z,17Z)-Icosapentaenoyl-CoA + Water → Coenzyme A + Eicosapentaenoic acid details
Cervonyl coenzyme A + Water → Coenzyme A + Docosahexaenoic acid details
Gamma-linolenoyl-CoA + Water → Coenzyme A + Gamma-Linolenic acid details
Dihomo-gamma-linolenyl coenzyme A + Water → Coenzyme A + 8,11,14-Eicosatrienoic acid details
Arachidonyl-CoA + Water → Coenzyme A + Arachidonic acid details
Propionyl-CoA + Water → Long-chain fatty acid + Coenzyme A details
GO Classification
Biological Process
very long-chain fatty acid metabolic process
acyl-CoA metabolic process
long-chain fatty acid metabolic process
Cellular Component
cytosol
mitochondrion
Function
coa hydrolase activity
hydrolase activity, acting on ester bonds
acyl-coa thioesterase activity
palmitoyl-coa hydrolase activity
catalytic activity
hydrolase activity
thiolester hydrolase activity
Molecular Function
acyl-CoA hydrolase activity
carboxylesterase activity
palmitoyl-CoA hydrolase activity
Process
acyl-coa metabolic process
metabolic process
primary metabolic process
cellular metabolic process
lipid metabolic process
cofactor metabolic process
coenzyme metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 14
Locus 14q24.3
SNPs ACOT1
Gene Sequence
>1266 bp
ATGGCGGCGACGCTGATCCTGGAGCCCGCGGGCCGCTGCTGCTGGGACGAACCGGTGCGA
ATCGCCGTGCGCGGCCTAGCCCCGGAGCAGCCGGTCACGCTGCGCGCGTCCCTGCGCGAC
GAGAAGGGCGCGCTTTTCCAGGCCCACGCGCGCTACCGCGCCGACACCCTTGGCGAGCTG
GACCTGGAGCGCGCGCCCGCGCTGGGCGGCAGCTTCGCGGGGCTTGAGCCCATGGGGCTG
CTCTGGGCCTTGGAGCCCGAGAAACCCTTGGTGCGGCTGGTGAAGCGCGACGTGCGAACG
CCCTTGGCCGTGGAGCTGGAGGTGCTGGATGGCCACGACCCCGACCCCGGGCGGCTGCTG
TGCCGGGTGCGGCACGAGCGCTACTTCCTCCCGCCCGGGGTGCGGCGCGAGCCGGTGCGC
GCGGGCCGGGTGCGAGGCACGCTCTTCCTGCCGCCAGAACCTGGGCCCTTTCCTGGCATT
GTGGACATGTTCGGAACTGGAGGTGGCCTGCTGGAGTATCGGGCTAGTCTGCTGGCTGGG
AAGGGTTTTGCTGTGATGGCTCTGGCTTACTATAACTATGAAGACCTCCCCAAGACCATG
GAGACGCTCCATCTGGAGTACTTTGAAGAAGCTGTGAACTACTTGCTCAGTCATCCTGAG
GTAAAAGGTCCAGGAGTTGGGCTGCTTGGAATTTCCAAAGGGGGTGAGCTCTGCCTTTCC
ATGGCCTCTTTCCTGAAGGGCATCACGGCTGCTGTCGTCATCAACGGCTCTGTGGCCAAT
GTTGGGGGAACCTTACGCTACAAGGGCGAGACCCTGCCCCCTGTGGGCGTCAACAGAAAT
CGCATCAAGGTGACCAAAGATGGCTATGCAGACATTGTGGATGTCCTGAACAGCCCTTTG
GAAGGACCTGACCAGAAGAGCTTCATTCCTGTGGAAAGGGCAGAGAGCACCTTCCTGTTC
CTGGTAGGTCAGGATGACCACAACTGGAAGAGTGAGTTCTATGCTAATGAGGCCTGTAAA
CGCTTGCAGGCCCATGGGAGGAGAAAGCCCCAGATCATCTGTTACCCAGAGACAGGGCAC
TATATTGAGCCTCCTTACTTCCCCCTGTGTCGGGCTTCCCTGCATGCCTTGGTGGGCAGT
CCTATTATCTGGGGAGGGGAGCCCAGGGCTCATGCCATGGCTCAGGTGGATGCTTGGAAA
CAACTCCAGACTTTCTTCCACAAACACTTGGGTGGCCACGAGGGGACAATCCCATCAAAA
GTGTAA
Protein Properties
Number of Residues 421
Molecular Weight 46276.96
Theoretical pI 7.339
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Acyl-coenzyme A thioesterase 1
MAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLL
CRVRHERYFLPPGVRREPVRAGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAG
KGFAVMALAYYNYEDLPKTMETLHLEYFEEAVNYLLSHPEVKGPGVGLLGISKGGELCLS
MASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPL
EGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGH
YIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSK
V
GenBank ID Protein 121934111
UniProtKB/Swiss-Prot ID Q86TX2
UniProtKB/Swiss-Prot Entry Name ACOT1_HUMAN
PDB IDs Not Available
GenBank Gene ID BC127748
GeneCard ID ACOT1
GenAtlas ID ACOT1
HGNC ID HGNC:33128
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: 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. FASEB J. 2006 Sep;20(11):1855-64. [PubMed:16940157 ]