Acyl-CoA thioesterase I

NameAcyl-CoA thioesterase I
Synonyms
  • 3.1.2.-
  • apeA
  • Lecithinase B
  • Lysophospholipase L1
  • pldC
  • Protease I
Gene NametesA
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0003987|Acyl-CoA thioesterase I
MMNFNNVFRWHLPFLFLVLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSK
TSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQD
VKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFMEEVYLKPQWMQDD
GIHPNRDAQPFIADWMAKQLQPLVNHDS
Number of residuesNone
Molecular Weight23621.955
Theoretical pI7.83
GO Classification
Functions
  • peptidase activity
  • phospholipase activity
  • palmitoyl-CoA hydrolase activity
  • identical protein binding
  • lysophospholipase activity
  • acyl-CoA hydrolase activity
Processes
  • lipid metabolic process
Components
  • outer membrane-bounded periplasmic space
General FunctionPhospholipase activity
Specific FunctionHydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP0ADA1
UniProtKB Entry Name
Cellular LocationPeriplasm
Gene sequence
>lcl|BSEQ0021308|Acyl-CoA thioesterase I (tesA)
ATGATGAACTTCAACAATGTTTTCCGCTGGCATTTGCCCTTCCTGTTCCTGGTCCTGTTA
ACCTTCCGTGCCGCCGCAGCGGACACGTTATTGATTCTGGGTGATAGCCTGAGCGCCGGG
TATCGAATGTCTGCCAGCGCGGCCTGGCCTGCCTTGTTGAATGATAAGTGGCAGAGTAAA
ACGTCGGTAGTTAATGCCAGCATCAGCGGCGACACCTCGCAACAAGGACTGGCGCGCCTT
CCGGCTCTGCTGAAACAGCATCAGCCGCGTTGGGTGCTGGTTGAACTGGGCGGCAATGAC
GGTTTGCGTGGTTTTCAGCCACAGCAAACCGAGCAAACGCTGCGCCAGATTTTGCAGGAT
GTCAAAGCCGCCAACGCTGAACCATTGTTAATGCAAATACGTCTGCCTGCAAACTATGGT
CGCCGTTATAATGAAGCCTTTAGCGCCATTTACCCCAAACTCGCCAAAGAGTTTGATGTT
CCGCTGCTGCCCTTTTTTATGGAAGAGGTCTACCTCAAGCCACAATGGATGCAGGATGAC
GGTATTCATCCCAACCGCGACGCCCAGCCGTTTATTGCCGACTGGATGGCGAAGCAGTTG
CAGCCTTTAGTAAATCATGACTCATAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Cho H, Cronan JE Jr: Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme. J Biol Chem. 1993 May 5;268(13):9238-45. [8098033 ]
  2. Ichihara S, Matsubara Y, Kato C, Akasaka K, Mizushima S: Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants. J Bacteriol. 1993 Feb;175(4):1032-7. [8432696 ]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [9278503 ]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [16738553 ]
  5. Karasawa K, Kudo I, Kobayashi T, Homma H, Chiba N, Mizushima H, Inoue K, Nojima S: Lysophospholipase L1 from Escherichia coli K-12 overproducer. J Biochem. 1991 Feb;109(2):288-93. [1864840 ]
  6. Lee LC, Lee YL, Leu RJ, Shaw JF: Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1. Biochem J. 2006 Jul 1;397(1):69-76. [16515533 ]
  7. Lo YC, Lin SC, Shaw JF, Liaw YC: Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol. 2003 Jul 11;330(3):539-51. [12842470 ]
  8. Lo YC, Lin SC, Shaw JF, Liaw YC: Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement. Biochemistry. 2005 Feb 15;44(6):1971-9. [15697222 ]

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