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; |