Acyl-CoA thioesterase I
Details
- Name
- Acyl-CoA thioesterase I
- Synonyms
- 3.1.2.-
- apeA
- Lecithinase B
- Lysophospholipase L1
- pldC
- Protease I
- Gene Name
- tesA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0003987|Acyl-CoA thioesterase I MMNFNNVFRWHLPFLFLVLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSK TSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQD VKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFMEEVYLKPQWMQDD GIHPNRDAQPFIADWMAKQLQPLVNHDS
- Number of residues
- 208
- Molecular Weight
- 23621.955
- Theoretical pI
- 7.83
- GO Classification
- Functionsacyl-CoA hydrolase activity / identical protein binding / lysophospholipase activity / palmitoyl-CoA hydrolase activity / peptidase activity / phospholipase activityProcesseslipid metabolic processComponentsouter membrane-bounded periplasmic space
- General Function
- Phospholipase activity
- Specific Function
- Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin.
- Pfam Domain Function
- Lipase_GDSL_2 (PF13472)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0021308|Acyl-CoA thioesterase I (tesA) ATGATGAACTTCAACAATGTTTTCCGCTGGCATTTGCCCTTCCTGTTCCTGGTCCTGTTA ACCTTCCGTGCCGCCGCAGCGGACACGTTATTGATTCTGGGTGATAGCCTGAGCGCCGGG TATCGAATGTCTGCCAGCGCGGCCTGGCCTGCCTTGTTGAATGATAAGTGGCAGAGTAAA ACGTCGGTAGTTAATGCCAGCATCAGCGGCGACACCTCGCAACAAGGACTGGCGCGCCTT CCGGCTCTGCTGAAACAGCATCAGCCGCGTTGGGTGCTGGTTGAACTGGGCGGCAATGAC GGTTTGCGTGGTTTTCAGCCACAGCAAACCGAGCAAACGCTGCGCCAGATTTTGCAGGAT GTCAAAGCCGCCAACGCTGAACCATTGTTAATGCAAATACGTCTGCCTGCAAACTATGGT CGCCGTTATAATGAAGCCTTTAGCGCCATTTACCCCAAACTCGCCAAAGAGTTTGATGTT CCGCTGCTGCCCTTTTTTATGGAAGAGGTCTACCTCAAGCCACAATGGATGCAGGATGAC GGTATTCATCCCAACCGCGACGCCCAGCCGTTTATTGCCGACTGGATGGCGAAGCAGTTG CAGCCTTTAGTAAATCATGACTCATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0ADA1 UniProtKB Entry Name TESA_ECOLI GenBank Protein ID 290474 GenBank Gene ID L06182 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]