IED ID | IndEnz0001000375 |
Enzyme Type ID | amylase000375 |
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 |
Organism | Rhizobium sp. (strain M-11) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Rhizobiaceae Rhizobium/Agrobacterium group Rhizobium unclassified Rhizobium Rhizobium sp. (strain M-11) |
Enzyme Sequence | MTQPNDAAKPVQGAGRFDIWAPEAGTVTLLAGGERYEMGRRPGNGPADEGWWTAADAPTGADVDYGYLLDGDEIPLPDPRTRRQPEGVHALSRTFDPGAHRWQDAGWQGRELQGSVIYELHIGTFTPEGTLDAAAGKLDYLAGLGIDFIELLPVNAFNGTHNWGYDGVQWFAVHEGYGGPAAYQRFVDAAHAAGLGVIQDVVYNHLGPSGNYLPRYGPYLKHGEGNTWGDSVNLDGPGSDHVRQYILDNVAMWLRDYRVDGLRLDAVHALKDERAVHILEEFGALADALSSEGGRPLTLIAESDLNNPRLLYPRDVNGYGLAGQWSDDFHHAVHVNVSGETTGYYSDFDSLGALAKVLRDGFFHDGSYSSFRGRCHGRPINFSAVHPAALVVCSQNHDQIGNRATGDRLSQSLPYGSLALAAVLTLTGPFTPMLFMGEEYGATTPWQFFTSHPEPELGKATAEGRIREFERMGWDPAVVPDPQDPETFTRSKLDWAEASAGDHARLLELYRSLITLRRSTPELARLGFADTAVEFDDDARWLRYWRGGVQVVLNFADRPISLDRPGTALLLATDDAVRMDGVQVELPPLSAAVLRD |
Enzyme Length | 596 |
Uniprot Accession Number | Q53238 |
Absorption | |
Active Site | ACT_SITE 265; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q55088; ACT_SITE 302; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q55088 |
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:0000250|UniProtKB:Q55088}; |
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); Chain (1); Region (3); Site (1) |
Keywords | Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 65,263 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |