Summary: Carboxylesterase family
This is the Wikipedia entry entitled "Carboxylesterase family". More...
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Carboxylesterase family Edit Wikipedia article
|Structure of ethylphosphorylated Butyrylcholinesterase.|
Carboxylesterase, type B is a family of evolutionarily related proteins.
Higher eukaryotes have many distinct esterases. The different types include those that act on carboxylic esters (EC 3.1.1). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases indicates that the majority are evolutionarily related. As is the case for lipases and serine proteases, the catalytic apparatus of esterases involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine. This family belongs to the superfamily of proteins with the Alpha/beta hydrolase fold.
Human genes that encode proteins containing the carboxylesterase domain include:
 See also
- Nachon F, Asojo OA, Borgstahl GE, Masson P, Lockridge O (February 2005). "Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging". Biochemistry 44 (4): 1154–62. DOI:10.1021/bi048238d. PMID 15667209.
- Myers M, Richmond RC, Oakeshott JG (1988). "On the origins of esterases". Mol. Biol. Evol. 5 (2): 113–119. PMID 3163407.
- Chatonnet A, Krejci E, Duval N, Vincens P, Massoulie J (1991). "Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid". Proc. Natl. Acad. Sci. U.S.A. 88 (15): 6647–6651. DOI:10.1073/pnas.88.15.6647. PMC 52145. PMID 1862088. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=52145.
- Sussman JL, Cygler M, Harel M, Silman I, Schrag JD, Doctor BP, Gentry MK (1993). "Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins". Protein Sci. 2 (3): 366–382. DOI:10.1002/pro.5560020309. PMC 2142374. PMID 8453375. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2142374.
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Carboxylesterase family Provide feedback
No Pfam abstract.
Internal database links
|Similarity to PfamA using HHSearch:||Peptidase_S9 Abhydrolase_3 DUF2424 Abhydrolase_5|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002018Higher eukaryotes have many distinct esterases. Among the different types are those which act on carboxylic esters (EC). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases indicates [PUBMED:3163407, PUBMED:1862088, PUBMED:8453375] that the majority are evolutionary related. As is the case for lipases and serine proteases, the catalytic apparatus of esterases involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||123|
|Number in full:||8736|
|Average length of the domain:||405.50 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||85.47 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||23|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the COesterase domain has been found. There are 371 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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