Detail Information for IndEnz0001000392
IED ID IndEnz0001000392
Enzyme Type ID amylase000392
Protein Name Malto-oligosyltrehalose trehalohydrolase
MTHase
EC 3.2.1.141
4-alpha-D-
1-
4
-alpha-D-glucano
trehalose trehalohydrolase
Glycosyltrehalose trehalohydrolase
GTHase
Maltooligosyl trehalose trehalohydrolase
Gene Name treZ
Organism Saccharolobus solfataricus (Sulfolobus solfataricus)
Taxonomic Lineage cellular organisms Archaea TACK group Crenarchaeota Thermoprotei Sulfolobales Sulfolobaceae Saccharolobus Saccharolobus solfataricus (Sulfolobus solfataricus)
Enzyme Sequence MTFAYKIDGNEVIFTLWAPYQKSVKLKVLEKGLYEMERDEKGYFTITLNNVKVRDRYKYVLDDASEIPDPASRYQPEGVHGPSQIIQESKEFNNETFLKKEDLIIYEIHVGTFTPEGTFEGVIRKLDYLKDLGITAIEIMPIAQFPGKRDWGYDGVYLYAVQNSYGGPEGFRKLVDEAHKKGLGVILDVVYNHVGPEGNYMVKLGPYFSQKYKTPWGLTFNFDDAESDEVRKFILENVEYWIKEYNVDGFRLDAVHAIIDTSPKHILEEIADVVHKYNRIVIAESDLNDPRVVNPKEKCGYNIDAQWVDDFHHSIHAYLTGERQGYYTDFGNLDDIVKSYKDVFVYDGKYSNFRRKTHGEPVGELDGCNFVVYIQNHDQVGNRGKGERIIKLVDRESYKIAAALYLLSPYIPMIFMGEEYGEENPFYFFSDFSDSKLIQGVREGRKKENGQDTDPQDESTFNASKLSWKIDEEIFSFYKILIKMRKELSIACDRRVNVVNGENWLIIKGREYFSLYVFSKSSIEVKYSGTLLLSSNNSFPQHIEEGKYEFDKGFALYKL
Enzyme Length 559
Uniprot Accession Number Q55088
Absorption
Active Site ACT_SITE 253; /note=Nucleophile; /evidence=ECO:0000305|PubMed:22334583; ACT_SITE 284; /note=Proton donor; /evidence=ECO:0000305|PubMed:22334583
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan.; EC=3.2.1.141; Evidence={ECO:0000269|PubMed:22334583};
DNA Binding
EC Number 3.2.1.141
Enzyme Function
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan biosynthesis; trehalose biosynthesis. {ECO:0000305|PubMed:22334583, ECO:0000305|PubMed:8901122}.
nucleotide Binding
Features Active site (2); Beta strand (34); Chain (1); Helix (23); Mutagenesis (3); Region (3); Site (1); Turn (3)
Keywords 3D-structure;Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8901122}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (8)
Cross Reference PDB 1EH9; 1EHA; 3VGB; 3VGD; 3VGE; 3VGF; 3VGG; 3VGH;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 64,790
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.141;