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InterPro: IPR001031 Thioesterase

Protein matches Help

UniProtKB

Matches:

2543 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

IPR001031 Thioesterase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00975	Thioesterase	2543
Signatures in BioMart

InterPro Relationships Help

Children

IPR020802 Polyketide synthase, thioesterase domain

Found in

IPR011412 Coronamic acid biosynthesis thioesterase CmaT
IPR012223 Thioesterase type II, NRPS/PKS/S-FAS

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0016788 hydrolase activity, acting on ester bonds

InterPro annotation

Entry Details in BioMart

Abstract

Thioesterase domains often occur integrated in or associated with peptide synthetases which are involved in the non-ribosomal synthesis of peptide antibiotics [1]. Thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates.

Structural links Help

PDB - click here

SCOP: c.69.1.22

CATH: 1.10.1470.20 , 1.10.287.490 , 3.40.50.1820

Database links Help

PANDIT: PF00975

Blocks: IPB001031

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

IPR001031

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O30409 Tyrocidine synthetase 3

P12785 Fatty acid synthase

P19096 Fatty acid synthase

P49327 Fatty acid synthase

Q12053 Aflatoxin biosynthesis polyketide synthase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001227	Acyl transferase domain
IPR013149	Alcohol dehydrogenase, zinc-binding
IPR020843	Polyketide synthase, enoylreductase
IPR020845	AMP-binding, conserved site
IPR016039	Thiolase-like
IPR014030	Beta-ketoacyl synthase, N-terminal
IPR016038	Thiolase-like, subgroup
IPR018201	Beta-ketoacyl synthase, active site
IPR020842	Polyketide synthase/Fatty acid synthase, KR
IPR002198	Short-chain dehydrogenase/reductase SDR
IPR016036	Malonyl-CoA ACP transacylase, ACP-binding
IPR014031	Beta-ketoacyl synthase, C-terminal
IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase
IPR020801	Polyketide synthase, acyl transferase domain
IPR011032	GroES-like
IPR016040	NAD(P)-binding domain
IPR006162	Phosphopantetheine attachment site
IPR009081	Acyl carrier protein-like
IPR006163	Phosphopantetheine-binding
IPR010071	Amino acid adenylation
IPR000794	Beta-ketoacyl synthase
IPR020806	Polyketide synthase, phosphopantetheine-binding
IPR000873	AMP-dependent synthetase/ligase
IPR001242	Condensation domain
IPR014043	Acyl transferase
IPR001031	Thioesterase
IPR013217	Methyltransferase type 12
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Schneider A, Marahiel MA. Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis. Arch. Microbiol. 169 404-10 1998 [PubMed: 9560421] http://dx.doi.org/10.1007/s002030050590

Additional Reading Open in usermanual
	Samel SA, Wagner B, Marahiel MA, Essen LO. The thioesterase domain of the fengycin biosynthesis cluster: a structural base for the macrocyclization of a non-ribosomal lipopeptide. J. Mol. Biol. 359 2006 876-89 [PubMed: 16697411] http://dx.doi.org/10.1016/j.jmb.2006.03.062
	Chakravarty B, Gu Z, Chirala SS, Wakil SJ, Quiocho FA. Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain. Proc. Natl. Acad. Sci. U.S.A. 101 2004 15567-72 [PubMed: 15507492] http://dx.doi.org/10.1073/pnas.0406901101
	Giraldes JW, Akey DL, Kittendorf JD, Sherman DH, Smith JL, Fecik RA. Structural and mechanistic insights into polyketide macrolactonization from polyketide-based affinity labels. Nat. Chem. Biol. 2 2006 531-6 [PubMed: 16969373] http://dx.doi.org/10.1038/nchembio822
	Akey DL, Kittendorf JD, Giraldes JW, Fecik RA, Sherman DH, Smith JL. Structural basis for macrolactonization by the pikromycin thioesterase. Nat. Chem. Biol. 2 2006 537-42 [PubMed: 16969372] http://dx.doi.org/10.1038/nchembio824
	Pemble CW 4th, Johnson LC, Kridel SJ, Lowther WT. Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat. Struct. Mol. Biol. 14 2007 704-9 [PubMed: 17618296] http://dx.doi.org/10.1038/nsmb1265

InterPro 23.1