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InterPro: IPR006379 HAD-superfamily hydrolase, subfamily IIB

Protein matchesHelp
UniProtKB
Matches:
6890 proteins
AccessionHelp IPR006379 HAD-SF_hydro_IIB
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR000150 Cof protein
IPR005002 Eukaryotic phosphomannomutase
IPR006378 Sucrose-phosphate phosphatase
IPR006381 HAD-superfamily hydrolase, superfamily IIB, YedP
Contains IPR003337 Trehalose-phosphatase
IPR013200 HAD superfamily hydrolase-like, type 3
GO Term annotationHelp
Process GO:0008152 metabolic process
Function GO:0003824 catalytic activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterised by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (IPR006357) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamilys Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of trehalose-6-phosphatase, plant and cyanobacterial sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase, a large subfamily of Cof-like hydrolases, containing many closely related bacterial sequences, a hypothetical equivalog containing the Escherichia coli YedP protein, as well as two other small clusters whose relationship to the other groups is unclear.

Structural linksHelp
Database linksHelp
Blocks: IPB006379

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006379 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O15305 Phosphomannomutase 2

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

O35621 Phosphomannomutase 1

P07283 Phosphomannomutase

Q9VTZ6 Probable phosphomannomutase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR005002 Eukaryotic phosphomannomutase
IPR003337 Trehalose-phosphatase
IPR006379 HAD-superfamily hydrolase, subfamily IIB
IPR001830 Glycosyl transferase, family 20
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr.
Ensemble refinement of protein crystal structures: validation and application.
Structure 15 2007 1040-52 [PubMed: 17850744]
http://dx.doi.org/10.1016/j.str.2007.06.019
Lu Z, Dunaway-Mariano D, Allen KN.
The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 5687-92 [PubMed: 18398008]
http://dx.doi.org/10.1073/pnas.0710800105
Fieulaine S, Lunn JE, Ferrer JL.
Crystal structure of a cyanobacterial sucrose-phosphatase in complex with glucose-containing disaccharides.
Proteins 68 2007 796-801 [PubMed: 17510968]
http://dx.doi.org/10.1002/prot.21481
Kawamura T, Watanabe N, Tanaka I.
Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii.
Acta Crystallogr. D Biol. Crystallogr. 64 2008 1267-76 [PubMed: 19018103]
http://dx.doi.org/10.1107/S0907444908033817
Yamamoto H, Takio K, Sugahara M, Kunishima N.
Structure of a haloacid dehalogenase superfamily phosphatase PH1421 from Pyrococcus horikoshii OT3: oligomeric state and thermoadaptation mechanism.
Acta Crystallogr. D Biol. Crystallogr. 64 2008 1068-77 [PubMed: 18931414]
http://dx.doi.org/10.1107/S0907444908025948
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InterPro 23.1