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InterPro: IPR002018 Carboxylesterase, type B

Protein matches Help

UniProtKB

Matches:

3846 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR002018 CarbesteraseB

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00135	COesterase	3656
PANTHER	PTHR11559	CarbesteraseB	3697
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000460 Neuroligin
IPR000908 Acetylcholinesterase, fish/snake
IPR000997 Cholinesterase
IPR001445 Acetylcholinesterase, insect
IPR016324 Thyroglobulin

Contains

IPR019819 Carboxylesterase type B, conserved site
IPR019826 Carboxylesterase type B, active site

InterPro annotation

Entry Details in BioMart

Abstract

Higher eukaryotes have many distinct esterases. Among the different types are those which 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 [1, 2, 3] 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.

Structural links Help

PDB - click here

SCOP: c.69.1.1 , c.69.1.17

CATH: 3.40.50.1820

Database links Help

PDBe-motif: PS00122 , PS00941

Enzyme: EC:3.1.1

PROSITE doc: PDOC00112

PANDIT: PF00135

Pfam Clan: CL0028.18

AC	CL0028.18
ID	AB_hydrolase
DE	Alpha/Beta hydrolase fold
PF00135	IPR002018	Carboxylesterase, type B
PF00151	IPR013818	Lipase, N-terminal
PF00326	IPR001375	Peptidase S9, prolyl oligopeptidase, catalytic domain
PF00450	IPR001563	Peptidase S10, serine carboxypeptidase
PF00561	IPR000073	Alpha/beta hydrolase fold-1
PF00756	IPR000801	Putative esterase
PF00975	IPR001031	Thioesterase
PF01083	IPR000675	Cutinase
PF01674	IPR002918	Lipase, class 2
PF01738	IPR002925	Dienelactone hydrolase
PF01764	IPR002921	Lipase, class 3
PF02089	IPR002472	Palmitoyl protein thioesterase
PF02129	IPR000383	Peptidase S15
PF02230	IPR003140	Phospholipase/carboxylesterase
PF02273	IPR003157	Acyl transferase, bacterial
PF02450	IPR003386	Lecithin:cholesterol acyltransferase
PF03096	IPR004142	Ndr
PF03403	IPR005065	Platelet-activating factor acetylhydrolase, plasma/intracellular isoform II
PF03583	IPR005152	Lipase, secreted
PF03959	IPR005645	Protein of unknown function DUF341
PF04301	IPR007398	Protein of unknown function DUF452
PF05057	IPR007751	Protein of unknown function DUF676, hydrolase-like
PF05448	IPR008391	Acetyl xylan esterase
PF05576	IPR008761	Peptidase S37, tripeptidyl aminopeptidase
PF05577	IPR008758	Peptidase S28
PF05677	IPR008536	Protein of unknown function DUF818, Chlamydia
PF05705	IPR008547	Protein of unknown function DUF829, transmembrane 53
PF05728	IPR008886	Uncharacterised protein family UPF0227
PF05990	IPR010297	Protein of unknown function DUF900, hydrolase-like
PF06028	IPR010315	Protein of unknown function DUF915, hydrolase-like
PF06057	IPR010333	Bacterial virulence
PF06259	IPR010427	Protein of unknown function DUF1023
PF06342	IPR010463	Protein of unknown function DUF1057, lipase putative
PF06500	IPR010520	Protein of unknown function DUF1100, hydrolase-like
PF06821	IPR010662	Protein of unknown function DUF1234
PF06850	IPR009656	PHB de-polymerase, C-terminal
PF07082	IPR010765	Protein of unknown function DUF1350
PF07176	IPR010802	Protein of unknown function DUF1400, cynaobacterial
PF07224	IPR010821	Chlorophyllase
PF07519	IPR011118	Tannase/feruloyl esterase
PF07819	IPR012908	PGAP1-like
PF07859	IPR013094	Alpha/beta hydrolase fold-3
PF08386	IPR013595	Peptidase S33, tripeptidyl-peptidase C-terminal
PF08538	IPR013744	Protein of unknown function DUF1749
PF08840	IPR014940	BAAT/Acyl-CoA thioester hydrolase C-terminal
PF10503	IPR010126	Esterase, PHB depolymerase

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002018

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P06276 Cholinesterase

P07140 Acetylcholinesterase

P21836 Acetylcholinesterase

P37967 Para-nitrobenzyl esterase

P38433 Acetylcholinesterase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002018	Carboxylesterase, type B
IPR019819	Carboxylesterase type B, conserved site
IPR001445	Acetylcholinesterase, insect
IPR019826	Carboxylesterase type B, active site
IPR000997	Cholinesterase
IPR014788	Acetylcholinesterase, tetramerisation
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Myers M, Richmond RC, Oakeshott JG. On the origins of esterases. Mol. Biol. Evol. 5 113-9 1988 [PubMed: 3163407] http://mbe.oxfordjournals.org/cgi/content/abstract/5/2/113.pdf
2.	Krejci E, Duval N, Chatonnet A, Vincens P, Massoulie J. 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 6647-51 1991 [PubMed: 1862088] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1862088
3.	Cygler M, Schrag JD, Sussman JL, Harel M, Silman I, Gentry MK, Doctor BP. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci. 2 366-82 1993 [PubMed: 8453375] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8453375

Additional Reading Open in usermanual
	Koehnke J, Jin X, Budreck EC, Posy S, Scheiffele P, Honig B, Shapiro L. Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2. Proc. Natl. Acad. Sci. U.S.A. 105 2008 1873-8 [PubMed: 18250328] http://dx.doi.org/10.1073/pnas.0711701105
	Chen X, Liu H, Shim AH, Focia PJ, He X. Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat. Struct. Mol. Biol. 15 2008 50-6 [PubMed: 18084303] http://dx.doi.org/10.1038/nsmb1350
	Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M. Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography. Proc. Natl. Acad. Sci. U.S.A. 105 2008 11742-7 [PubMed: 18701720] http://dx.doi.org/10.1073/pnas.0804828105
	Harel M, Sonoda LK, Silman I, Sussman JL, Rosenberry TL. Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site. J. Am. Chem. Soc. 130 2008 7856-61 [PubMed: 18512913] http://dx.doi.org/10.1021/ja7109822
	Fleming CD, Edwards CC, Kirby SD, Maxwell DM, Potter PM, Cerasoli DM, Redinbo MR. Crystal structures of human carboxylesterase 1 in covalent complexes with the chemical warfare agents soman and tabun. Biochemistry 46 2007 5063-71 [PubMed: 17407327] http://dx.doi.org/10.1021/bi700246n

InterPro 23.1