Detail Information for IndEnz0001000379
IED ID IndEnz0001000379
Enzyme Type ID amylase000379
Protein Name Malto-oligosyltrehalose trehalohydrolase
MTHase
EC 3.2.1.141
4-alpha-D-
1-
4
-alpha-D-glucano
trehalose trehalohydrolase
Maltooligosyl trehalose trehalohydrolase
Gene Name treZ DR_0464
Organism Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Deinococcales Deinococcaceae Deinococcus Deinococcus radiodurans Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Enzyme Sequence MTQTQPVTPTPPASFQTQHDPRTRLGATPLPGGAGTRFRLWTSTARTVAVRVNGTEHVMTSLGGGIYELELPVGPGARYLFVLDGVPTPDPYARFLPDGVHGEAEVVDFGTFDWTDADWHGIKLADCVFYEVHVGTFTPEGTYRAAAEKLPYLKELGVTAIQVMPLAAFDGQRGWGYDGAAFYAPYAPYGRPEDLMALVDAAHRLGLGVFLDVVYNHFGPSGNYLSSYAPSYFTDRFSSAWGMGLDYAEPHMRRYVTGNARMWLRDYHFDGLRLDATPYMTDDSETHILTELAQEIHELGGTHLLLAEDHRNLPDLVTVNHLDGIWTDDFHHETRVTLTGEQEGYYAGYRGGAEALAYTIRRGWRYEGQFWAVKGEEHERGHPSDALEAPNFVYCIQNHDQIGNRPLGERLHQSDGVTLHEYRGAAALLLPMTPLLFQGQEWAASTPFQFFSDHAGELGQAVSEGRKKEFGGFSGFSGEDVPDPQAEQTFLNSKLNWAEREGGEHARTLRLYRDLLRLRREDPVLHNRQRENLTTGHDGDVLWVRTVTGAGERVLLWNLGQDTRAVAEVKLPFTVPRRLLLHTEGREDLTLGAGEAVLVG
Enzyme Length 600
Uniprot Accession Number Q9RX51
Absorption
Active Site ACT_SITE 275; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 308; /note=Proton donor; /evidence=ECO:0000305
Activity Regulation
Binding Site BINDING 376; /note=Substrate; /evidence=ECO:0000305|PubMed:15784255
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;
DNA Binding
EC Number 3.2.1.141
Enzyme Function
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
nucleotide Binding
Features Active site (2); Beta strand (33); Binding site (1); Chain (1); Compositional bias (1); Helix (30); Region (4); Site (1); Turn (2)
Keywords 3D-structure;Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (9)
Cross Reference PDB 2BHU; 2BHY; 2BHZ; 2BXY; 2BXZ; 2BY0; 2BY1; 2BY2; 2BY3;
Mapped Pubmed ID 16421442;
Motif
Gene Encoded By
Mass 66,910
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.141;