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InterPro: IPR015156 Malto-oligosyltrehalose trehalohydrolase, C-terminal

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UniProtKB

Matches:

13 proteins

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

Accession

IPR015156 MTHase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF09071	Alpha-amyl_C	13
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013780 Glycosyl hydrolase, family 13, all-beta

Found in

IPR012768 Malto-oligosyltrehalose trehalohydrolase

InterPro annotation

Entry Details in BioMart

Abstract

This C-terminal domain is found in the prokaryotic protein glycosyltrehalose trehalohydrolase; it assumes a gamma-crystallin-type fold with a five-stranded anti-parallel beta-sheet that packs against the C-terminal side of a beta-alpha barrel. The domain is common to family 13 glycosidases and typically contains a five to ten strand beta-sheet, however its precise fold varies [1].

Structural links Help

PDB - click here

SCOP: b.71.1.1

CATH: 2.60.40.1180 , 3.20.20.80

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR015156

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

Q55088 Alpha-amylase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR012768	Malto-oligosyltrehalose trehalohydrolase
IPR013780	Glycosyl hydrolase, family 13, all-beta
IPR013783	Immunoglobulin-like fold
IPR006047	Glycosyl hydrolase, family 13, catalytic domain
IPR014756	Immunoglobulin E-set
IPR004193	Glycoside hydrolase, family 13, N-terminal
IPR015156	Malto-oligosyltrehalose trehalohydrolase, C-terminal
IPR017853	Glycoside hydrolase, catalytic core
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Feese MD, Kato Y, Tamada T, Kato M, Komeda T, Miura Y, Hirose M, Hondo K, Kobayashi K, Kuroki R. Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus. J. Mol. Biol. 301 451-64 2000 [PubMed: 10926520] http://dx.doi.org/10.1006/jmbi.2000.3977

InterPro 23.1