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InterPro: IPR003337 Trehalose-phosphatase

Protein matchesHelp
UniProtKB
Matches:
1102 proteins
AccessionHelp IPR003337 Trehalose_PPase
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR006379 HAD-superfamily hydrolase, subfamily IIB
GO Term annotationHelp
Process GO:0005992 trehalose biosynthetic process
Function GO:0003824 catalytic activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Trehalose-phosphatases EC:3.1.3.12 catalyse the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance. A pathway for trehalose biosynthesis may also exist in plants [1]. The trehalose-phosphatase signature is found in the C terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain (see IPR001830). It would appear that the two equivalent genes in the Escherichia coli otsBA operon: otsA, the trehalose-6-phosphate synthase and otsB, trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes [2].

Structural linksHelp
SCOP: c.108.1.15
Database linksHelp
PANDIT: PF02358
Pfam Clan: CL0137.11

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003337 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A0PMI0 Trehalose-phosphate phosphatase

O14081 Putative alpha,alpha-trehalose-phosphate synthase [UDP-forming] 106 kDa subunit

O23617 Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5

P31688 Trehalose-phosphatase

Q54K57 Alpha,alpha-trehalose-phosphate synthase [UDP-forming] A

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR003337 Trehalose-phosphatase
IPR012766 Alpha,alpha-trehalose-phosphate synthase
IPR006379 HAD-superfamily hydrolase, subfamily IIB
IPR001830 Glycosyl transferase, family 20
SWISS-MODEL
ModBase

PublicationsHelp
1. Vogel G, Aeschbacher RA, Muller J, Boller T, Wiemken A.
Trehalose-6-phosphate phosphatases from Arabidopsis thaliana: identification by functional complementation of the yeast tps2 mutant.
Plant J. 13 673-83 1998 [PubMed: 9681009]
http://dx.doi.org/10.1046/j.1365-313X.1998.00064.x
2. Kaasen I, McDougall J, Strom AR.
Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex.
Gene 145 9-15 1994 [PubMed: 8045430]
http://dx.doi.org/10.1016/0378-1119(94)90316-6

Additional ReadingHelp
Ryll R, Kumazawa Y, Yano I.
Immunological properties of trehalose dimycolate (cord factor) and other mycolic acid-containing glycolipids--a review.
Microbiol. Immunol. 45 2001 801-11 [PubMed: 11838897]
http://www.jstage.jst.go.jp/article/mandi/45/12/45_801/_article
Eastmond PJ, van Dijken AJ, Spielman M, Kerr A, Tissier AF, Dickinson HG, Jones JD, Smeekens SC, Graham IA.
Trehalose-6-phosphate synthase 1, which catalyses the first step in trehalose synthesis, is essential for Arabidopsis embryo maturation.
Plant J. 29 2002 225-35 [PubMed: 11851922]
http://dx.doi.org/10.1046/j.1365-313x.2002.01220.x
Leyman B, Van Dijck P, Thevelein JM.
An unexpected plethora of trehalose biosynthesis genes in Arabidopsis thaliana.
Trends Plant Sci. 6 2001 510-3 [PubMed: 11701378]
http://dx.doi.org/10.1016/S1360-1385(01)02125-2
De Virgilio C, Burckert N, Bell W, Jeno P, Boller T, Wiemken A.
Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity.
Eur. J. Biochem. 212 1993 315-23 [PubMed: 8444170]
http://dx.doi.org/10.1111/j.1432-1033.1993.tb17664.x
Rao KN, Kumaran D, Seetharaman J, Bonanno JB, Burley SK, Swaminathan S.
Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications.
Protein Sci. 15 2006 1735-44 [PubMed: 16815921]
http://dx.doi.org/10.1110/ps.062096606
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InterPro 23.1